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P07947

- YES_HUMAN

UniProt

P07947 - YES_HUMAN

Protein

Tyrosine-protein kinase Yes

Gene

YES1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei305 – 3051ATPPROSITE-ProRule annotation
    Active sitei396 – 3961Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi283 – 2919ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. enzyme binding Source: UniProtKB
    3. ion channel binding Source: BHF-UCL
    4. non-membrane spanning protein tyrosine kinase activity Source: BHF-UCL
    5. protein binding Source: IntAct
    6. protein tyrosine kinase activity Source: Reactome

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cellular protein modification process Source: ProtInc
    3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    4. glucose transport Source: Ensembl
    5. innate immune response Source: Reactome
    6. leukocyte migration Source: Reactome
    7. peptidyl-tyrosine phosphorylation Source: GOC
    8. protein autophosphorylation Source: Ensembl
    9. regulation of vascular permeability Source: BHF-UCL
    10. T cell costimulation Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_111225. Regulation of KIT signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_12519. PECAM1 interactions.
    REACT_160274. FCGR activation.
    REACT_19183. CD28 co-stimulation.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_23787. Regulation of signaling by CBL.
    SignaLinkiP07947.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Yes (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene c-Yes
    p61-Yes
    Gene namesi
    Name:YES1
    Synonyms:YES
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:12841. YES1.

    Subcellular locationi

    Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytosol
    Note: Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: UniProtKB
    5. microtubule organizing center Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi426 – 4261Y → F: About 50% loss of CSK-mediated inhibition. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA37432.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 543542Tyrosine-protein kinase YesPRO_0000088181Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi3 – 31S-palmitoyl cysteine; in membrane formBy similarity
    Modified residuei11 – 111Phosphoserine
    Modified residuei21 – 211Phosphothreonine1 Publication
    Modified residuei26 – 261Phosphoserine
    Modified residuei32 – 321Phosphotyrosine
    Modified residuei40 – 401Phosphoserine1 Publication
    Modified residuei111 – 1111Phosphoserine
    Modified residuei194 – 1941Phosphotyrosine
    Modified residuei195 – 1951Phosphoserine
    Modified residuei222 – 2221Phosphotyrosine
    Modified residuei223 – 2231Phosphotyrosine
    Modified residuei336 – 3361Phosphotyrosine1 Publication
    Modified residuei345 – 3451Phosphotyrosine1 Publication
    Modified residuei426 – 4261Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei446 – 4461PhosphotyrosineCurated
    Modified residuei537 – 5371Phosphotyrosine; by CSK2 Publications

    Post-translational modificationi

    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.6 Publications
    Palmitoylation at Cys-3 promotes membrane localization.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP07947.
    PaxDbiP07947.
    PRIDEiP07947.

    PTM databases

    PhosphoSiteiP07947.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Gene expression databases

    ArrayExpressiP07947.
    BgeeiP07947.
    CleanExiHS_YES1.
    GenevestigatoriP07947.

    Organism-specific databases

    HPAiCAB004370.
    HPA026480.

    Interactioni

    Subunit structurei

    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.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALOX5P099172EBI-515331,EBI-79934
    ARP102755EBI-515331,EBI-608057
    EGFRP005333EBI-515331,EBI-297353
    GAB1Q134807EBI-515331,EBI-517684
    KITP107217EBI-515331,EBI-1379503
    MED28Q9H2042EBI-515331,EBI-514199
    METP085813EBI-515331,EBI-1039152

    Protein-protein interaction databases

    BioGridi113357. 49 interactions.
    DIPiDIP-33849N.
    IntActiP07947. 30 interactions.
    MINTiMINT-93566.
    STRINGi9606.ENSP00000324740.

    Structurei

    Secondary structure

    1
    543
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi93 – 1008
    Beta strandi117 – 1215
    Beta strandi126 – 1338
    Turni134 – 1363
    Beta strandi139 – 1435
    Helixi144 – 1463
    Beta strandi147 – 1493

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HDAX-ray1.90A91-152[»]
    ProteinModelPortaliP07947.
    SMRiP07947. Positions 92-543.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07947.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini91 – 15262SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini158 – 25598SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini277 – 530254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiP07947.
    KOiK05705.
    PhylomeDBiP07947.
    TreeFamiTF351634.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P07947-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGCIKSKENK SPAIKYRPEN TPEPVSTSVS HYGAEPTTVS PCPSSSAKGT    50
    AVNFSSLSMT PFGGSSGVTP FGGASSSFSV VPSSYPAGLT GGVTIFVALY 100
    DYEARTTEDL SFKKGERFQI INNTEGDWWE ARSIATGKNG YIPSNYVAPA 150
    DSIQAEEWYF GKMGRKDAER LLLNPGNQRG IFLVRESETT KGAYSLSIRD 200
    WDEIRGDNVK HYKIRKLDNG GYYITTRAQF DTLQKLVKHY TEHADGLCHK 250
    LTTVCPTVKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT 300
    KVAIKTLKPG TMMPEAFLQE AQIMKKLRHD KLVPLYAVVS EEPIYIVTEF 350
    MSKGSLLDFL KEGDGKYLKL PQLVDMAAQI ADGMAYIERM NYIHRDLRAA 400
    NILVGENLVC KIADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT 450
    IKSDVWSFGI LQTELVTKGR VPYPGMVNRE VLEQVERGYR MPCPQGCPES 500
    LHELMNLCWK KDPDERPTFE YIQSFLEDYF TATEPQYQPG ENL 543
    Length:543
    Mass (Da):60,801
    Last modified:January 23, 2007 - v3
    Checksum:iA2B376084686BBCD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti198 – 1981I → V.1 Publication
    Corresponds to variant rs34580680 [ dbSNP | Ensembl ].
    VAR_041879
    Natural varianti282 – 2821K → R.1 Publication
    Corresponds to variant rs35126906 [ dbSNP | Ensembl ].
    VAR_041880

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15990 mRNA. Translation: AAA35735.1.
    AP001178 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01709.1.
    CH471113 Genomic DNA. Translation: EAX01710.1.
    BC048960 mRNA. Translation: AAH48960.1.
    CCDSiCCDS11824.1.
    PIRiA26714. TVHUYS.
    RefSeqiNP_005424.1. NM_005433.3.
    UniGeneiHs.194148.

    Genome annotation databases

    EnsembliENST00000314574; ENSP00000324740; ENSG00000176105.
    ENST00000584307; ENSP00000462468; ENSG00000176105.
    GeneIDi7525.
    KEGGihsa:7525.
    UCSCiuc002kky.3. human.

    Polymorphism databases

    DMDMi125870.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15990 mRNA. Translation: AAA35735.1 .
    AP001178 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01709.1 .
    CH471113 Genomic DNA. Translation: EAX01710.1 .
    BC048960 mRNA. Translation: AAH48960.1 .
    CCDSi CCDS11824.1.
    PIRi A26714. TVHUYS.
    RefSeqi NP_005424.1. NM_005433.3.
    UniGenei Hs.194148.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HDA X-ray 1.90 A 91-152 [» ]
    ProteinModelPortali P07947.
    SMRi P07947. Positions 92-543.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113357. 49 interactions.
    DIPi DIP-33849N.
    IntActi P07947. 30 interactions.
    MINTi MINT-93566.
    STRINGi 9606.ENSP00000324740.

    Chemistry

    BindingDBi P07947.
    ChEMBLi CHEMBL2363074.
    DrugBanki DB01254. Dasatinib.
    GuidetoPHARMACOLOGYi 2284.

    PTM databases

    PhosphoSitei P07947.

    Polymorphism databases

    DMDMi 125870.

    Proteomic databases

    MaxQBi P07947.
    PaxDbi P07947.
    PRIDEi P07947.

    Protocols and materials databases

    DNASUi 7525.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314574 ; ENSP00000324740 ; ENSG00000176105 .
    ENST00000584307 ; ENSP00000462468 ; ENSG00000176105 .
    GeneIDi 7525.
    KEGGi hsa:7525.
    UCSCi uc002kky.3. human.

    Organism-specific databases

    CTDi 7525.
    GeneCardsi GC18M000721.
    HGNCi HGNC:12841. YES1.
    HPAi CAB004370.
    HPA026480.
    MIMi 164880. gene.
    neXtProti NX_P07947.
    PharmGKBi PA37432.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi P07947.
    KOi K05705.
    PhylomeDBi P07947.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_111225. Regulation of KIT signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_12519. PECAM1 interactions.
    REACT_160274. FCGR activation.
    REACT_19183. CD28 co-stimulation.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_23787. Regulation of signaling by CBL.
    SignaLinki P07947.

    Miscellaneous databases

    EvolutionaryTracei P07947.
    GeneWikii YES1.
    GenomeRNAii 7525.
    NextBioi 29441.
    PROi P07947.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07947.
    Bgeei P07947.
    CleanExi HS_YES1.
    Genevestigatori P07947.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNA clones for the human c-yes gene."
      Sukegawa J., Semba K., Yamanashi Y., Nishizawa M., Miyajima N., Yamamoto T., Toyoshima K.
      Mol. Cell. Biol. 7:41-47(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. Cited for: TISSUE SPECIFICITY.
    6. "Differential expression of p62c-yes in normal, hyperplastic and neoplastic human epidermis."
      Krueger J., Zhao Y.H., Murphy D., Sudol M.
      Oncogene 6:933-940(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif."
      Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.
      Biochem. J. 303:749-753(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION.
    8. "Expression, purification, and initial characterization of human Yes protein tyrosine kinase from a bacterial expression system."
      Sun G., Budde R.J.
      Arch. Biochem. Biophys. 345:135-142(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CSK.
    9. "Autophosphorylation of Src and Yes blocks their inactivation by Csk phosphorylation."
      Sun G., Sharma A.K., Budde R.J.
      Oncogene 17:1587-1595(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-426, MUTAGENESIS OF TYR-426.
    10. "CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae."
      Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L., So M.
      J. Cell Biol. 156:951-957(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, FUNCTION.
    11. Cited for: REVIEW ON FUNCTION.
    12. "Phosphorylation of cyclin dependent kinase 4 on tyrosine 17 is mediated by Src family kinases."
      Martin N.G., McAndrew P.C., Eve P.D., Garrett M.D.
      FEBS J. 275:3099-3109(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDK4.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    16. "Phosphorylation of collapsin response mediator protein 2 on Tyr-479 regulates CXCL12-induced T lymphocyte migration."
      Varrin-Doyer M., Vincent P., Cavagna S., Auvergnon N., Noraz N., Rogemond V., Honnorat J., Moradi-Ameli M., Giraudon P.
      J. Biol. Chem. 284:13265-13276(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF DPYSL2.
    17. "Differential trafficking of Src, Lyn, Yes and Fyn is specified by the state of palmitoylation in the SH4 domain."
      Sato I., Obata Y., Kasahara K., Nakayama Y., Fukumoto Y., Yamasaki T., Yokoyama K.K., Saito T., Yamaguchi N.
      J. Cell Sci. 122:965-975(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336; TYR-345 AND TYR-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Clues for c-Yes involvement in the cell cycle and cytokinesis."
      Jung J., Lee M.K., Jin Y., Fu S.B., Rosales J.L., Lee K.Y.
      Cell Cycle 10:1502-1503(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    20. Cited for: FUNCTION.
    21. "Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation."
      Martin-Garcia J.M., Luque I., Mateo P.L., Ruiz-Sanz J., Camara-Artigas A.
      FEBS Lett. 581:1701-1706(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 91-152.
    22. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-198 AND ARG-282.

    Entry informationi

    Entry nameiYES_HUMAN
    AccessioniPrimary (citable) accession number: P07947
    Secondary accession number(s): A6NLB3, D3DUH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 176 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3