Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01024
Entry Name
UniProt Accession
Theoretical PI
6.32
Molecular Weight
60801.24
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Tyrosine-protein kinase Yes
Protein Synonyms/Alias
2.7.10.2; Proto-oncogene c-Yes; p61-Yes;
Gene Name
YES1
Gene Synonyms/Alias
YES;
Created Date
01-AUG-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGCIKSKEN
[2]
N-Myristoylation
3
Canonical
*****MGCIKSKENK
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
[2] Johnson DR, Bhatnagar RS, Knoll LJ, Gordon JI. Genetic and biochemical studiesof protein N-myristoylation. Annu Rev Biochem. 1994;63:869-914. Review. PubMedPMID: 7979256.[PMID:7979256]
Functional Description
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 EGRF, 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.
Sequence Annotation
Domain: 91 152 SH3.
Domain: 158 255 SH2.
Domain: 277 530 Protein kinase.
Nucleotide-binding: 283 291 ATP.
Active site: 396 396 Proton acceptor.
Binding site: 305 305 ATP.
Modified residue: 11 11 Phosphoserine.
Modified residue: 21 21 Phosphothreonine.
Modified residue: 26 26 Phosphoserine.
Modified residue: 32 32 Phosphotyrosine.
Modified residue: 40 40 Phosphoserine.
Modified residue: 111 111 Phosphoserine.
Modified residue: 194 194 Phosphotyrosine.
Modified residue: 195 195 Phosphoserine.
Modified residue: 222 222 Phosphotyrosine.
Modified residue: 223 223 Phosphotyrosine.
Modified residue: 336 336 Phosphotyrosine.
Modified residue: 345 345 Phosphotyrosine.
Modified residue: 426 426 Phosphotyrosine; by autocatalysis.
Modified residue: 446 446 Phosphotyrosine.
Modified residue: 537 537 Phosphotyrosine; by CSK.
Protein Length
543 AA.
Protein Sequence
(Canonical)
MGCIKSKENK SPAIKYRPEN TPEPVSTSVS HYGAEPTTVS PCPSSSAKGT AVNFSSLSMT  60
PFGGSSGVTP FGGASSSFSV VPSSYPAGLT GGVTIFVALY DYEARTTEDL SFKKGERFQI  120
INNTEGDWWE ARSIATGKNG YIPSNYVAPA DSIQAEEWYF GKMGRKDAER LLLNPGNQRG  180
IFLVRESETT KGAYSLSIRD WDEIRGDNVK HYKIRKLDNG GYYITTRAQF DTLQKLVKHY  240
TEHADGLCHK LTTVCPTVKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT  300
KVAIKTLKPG TMMPEAFLQE AQIMKKLRHD KLVPLYAVVS EEPIYIVTEF MSKGSLLDFL  360
KEGDGKYLKL PQLVDMAAQI ADGMAYIERM NYIHRDLRAA NILVGENLVC KIADFGLARL  420
IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LQTELVTKGR VPYPGMVNRE  480
VLEQVERGYR MPCPQGCPES LHELMNLCWK KDPDERPTFE YIQSFLEDYF TATEPQYQPG  540
ENL                                                                543
MGCIKSKENK SPAIKYRPEN TPEPVSTSVS HYGAEPTTVS PCPSSSAKGT AVNFSSLSMT  60
PFGGSSGVTP FGGASSSFSV VPSSYPAGLT GGVTIFVALY DYEARTTEDL SFKKGERFQI  120
INNTEGDWWE ARSIATGKNG YIPSNYVAPA DSIQAEEWYF GKMGRKDAER LLLNPGNQRG  180
IFLVRESETT KGAYSLSIRD WDEIRGDNVK HYKIRKLDNG GYYITTRAQF DTLQKLVKHY  240
TEHADGLCHK LTTVCPTVKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT  300
KVAIKTLKPG TMMPEAFLQE AQIMKKLRHD KLVPLYAVVS EEPIYIVTEF MSKGSLLDFL  360
KEGDGKYLKL PQLVDMAAQI ADGMAYIERM NYIHRDLRAA NILVGENLVC KIADFGLARL  420
IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LQTELVTKGR VPYPGMVNRE  480
VLEQVERGYR MPCPQGCPES LHELMNLCWK KDPDERPTFE YIQSFLEDYF TATEPQYQPG  540
ENL                                                                543
FASTA
(Canonical)
>LipidDB-9606-01024|P07947
MGCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSSSAKGTAVNFSSLSMT
PFGGSSGVTPFGGASSSFSVVPSSYPAGLTGGVTIFVALYDYEARTTEDLSFKKGERFQI
INNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRG
IFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHY
TEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTT
KVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFL
KEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARL
IEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNRE
VLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPG
ENL
MGCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSSSAKGTAVNFSSLSMT
PFGGSSGVTPFGGASSSFSVVPSSYPAGLTGGVTIFVALYDYEARTTEDLSFKKGERFQI
INNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRG
IFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHY
TEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTT
KVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFL
KEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARL
IEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNRE
VLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPG
ENL
Gene Ontology
GO:0005737; C:cytoplasm; IDA:HPA
GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW
GO:0005829; C:cytosol; TAS:Reactome
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0005794; C:Golgi apparatus; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0019899; F:enzyme binding; IPI:UniProtKB
GO:0044325; F:ion channel binding; IPI:BHF-UCL
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; TAS:BHF-UCL
GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0006464; P:cellular protein modification process; TAS:ProtInc
GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome
GO:0015758; P:glucose transport; IEA:Ensembl
GO:0045087; P:innate immune response; TAS:Reactome
GO:0050900; P:leukocyte migration; TAS:Reactome
GO:0018108; P:peptidyl-tyrosine phosphorylation; EXP:GOC
GO:0046777; P:protein autophosphorylation; IEA:Ensembl
GO:0043114; P:regulation of vascular permeability; TAS:BHF-UCL
GO:0031295; P:T cell costimulation; TAS:Reactome
Interpro
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom
InterPro; IPR000980; SH2
InterPro; IPR001452; SH3_domain
InterPro; IPR008266; Tyr_kinase_AS
InterPro; IPR020635; Tyr_kinase_cat_dom
Pfam
Pfam; PF07714; Pkinase_Tyr;
Pfam; PF00017; SH2;
Pfam; PF00018; SH3_1;
SMART
SMART; SM00252; SH2;
SMART; SM00326; SH3;
SMART; SM00219; TyrKc;
PROSITE
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00109; PROTEIN_KINASE_TYR;
PROSITE; PS50001; SH2;
PROSITE; PS50002; SH3;
PRINTS
PRINTS; PR00401; SH2DOMAIN;
PRINTS; PR00452; SH3DOMAIN;
PRINTS; PR00109; TYRKINASE;