P07947 · YES_HUMAN
- ProteinTyrosine-protein kinase Yes
- GeneYES1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids543 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis. Catalyzes phosphorylation of organic cation transporter OCT2 which induces its transport activity (PubMed:26979622).
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein kinase Yes
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP07947
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway. Localized to small puncta throughout the cytoplasm and cell membrane when in the presence of SNAIL1 (By similarity).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_041879 | 198 | in dbSNP:rs34580680 | |||
Sequence: I → V | ||||||
Natural variant | VAR_041880 | 282 | in dbSNP:rs35126906 | |||
Sequence: K → R | ||||||
Mutagenesis | 426 | About 50% loss of CSK-mediated inhibition. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 633 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Lipidation | 2 | UniProt | N-myristoyl glycine | ||||
Sequence: G | |||||||
Chain | PRO_0000088181 | 2-543 | UniProt | Tyrosine-protein kinase Yes | |||
Sequence: GCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSSSAKGTAVNFSSLSMTPFGGSSGVTPFGGASSSFSVVPSSYPAGLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGENL | |||||||
Lipidation | 3 | UniProt | S-palmitoyl cysteine; in membrane form | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 16 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 21 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 32 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 40 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 40 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 111 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 195 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 223 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 336 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 336 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 345 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 345 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 426 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 426 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 427 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 446 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 446 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 537 | UniProt | Phosphotyrosine; by CSK | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 537 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylated (PubMed:11901164).
Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-426 maintains enzyme activity by blocking CSK-mediated inhibition
Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-426 maintains enzyme activity by blocking CSK-mediated inhibition
Palmitoylation at Cys-3 promotes membrane localization.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the epithelial cells of renal proximal tubules and stomach as well as hematopoietic cells in the bone marrow and spleen in the fetal tissues. In adult, expressed in epithelial cells of the renal proximal tubules and present in keratinocytes in the basal epidermal layer of epidermis.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with YAP1 and CSF1R (By similarity).
Interacts with CTNND1; this interaction allows YES1-mediated activation of FYN and FER and subsequent phosphorylation of CTNND1 (By similarity).
Interacts with FASLG. Interacts with IL6ST/gp130 (PubMed:25731159).
Interacts with SCRIB, when YES1 is in a closed conformation; the interaction facilitates YES1 autophosphorylation (PubMed:33730553).
Interacts with CTNND1; this interaction allows YES1-mediated activation of FYN and FER and subsequent phosphorylation of CTNND1 (By similarity).
Interacts with FASLG. Interacts with IL6ST/gp130 (PubMed:25731159).
Interacts with SCRIB, when YES1 is in a closed conformation; the interaction facilitates YES1 autophosphorylation (PubMed:33730553).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-45 | Disordered | ||||
Sequence: MGCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSS | ||||||
Compositional bias | 21-45 | Polar residues | ||||
Sequence: TPEPVSTSVSHYGAEPTTVSPCPSS | ||||||
Domain | 91-152 | SH3 | ||||
Sequence: GGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADS | ||||||
Domain | 158-255 | SH2 | ||||
Sequence: WYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVC | ||||||
Domain | 277-530 | Protein kinase | ||||
Sequence: LRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYF |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length543
- Mass (Da)60,801
- Last updated2007-01-23 v3
- ChecksumA2B376084686BBCD
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3QRU1 | J3QRU1_HUMAN | YES1 | 548 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 21-45 | Polar residues | ||||
Sequence: TPEPVSTSVSHYGAEPTTVSPCPSS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M15990 EMBL· GenBank· DDBJ | AAA35735.1 EMBL· GenBank· DDBJ | mRNA | ||
AP001178 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471113 EMBL· GenBank· DDBJ | EAX01709.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471113 EMBL· GenBank· DDBJ | EAX01710.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC048960 EMBL· GenBank· DDBJ | AAH48960.1 EMBL· GenBank· DDBJ | mRNA |