YES_HUMAN
ID YES_HUMAN Reviewed; 543 AA.
AC P07947; A6NLB3; D3DUH1;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 241.
DE RecName: Full=Tyrosine-protein kinase Yes;
DE EC=2.7.10.2;
DE AltName: Full=Proto-oncogene c-Yes;
DE AltName: Full=p61-Yes;
GN Name=YES1; Synonyms=YES;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2436037; DOI=10.1128/mcb.7.1.41-47.1987;
RA Sukegawa J., Semba K., Yamanashi Y., Nishizawa M., Miyajima N.,
RA Yamamoto T., Toyoshima K.;
RT "Characterization of cDNA clones for the human c-yes gene.";
RL Mol. Cell. Biol. 7:41-47(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=2021534; DOI=10.1038/bjc.1991.121;
RA Sugawara K., Sugawara I., Sukegawa J., Akatsuka T., Yamamoto T., Morita M.,
RA Mori S., Toyoshima K.;
RT "Distribution of c-yes-1 gene product in various cells and tissues.";
RL Br. J. Cancer 63:508-513(1991).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=2067846;
RA Krueger J., Zhao Y.H., Murphy D., Sudol M.;
RT "Differential expression of p62c-yes in normal, hyperplastic and neoplastic
RT human epidermis.";
RL Oncogene 6:933-940(1991).
RN [7]
RP PALMITOYLATION.
RX PubMed=7980442; DOI=10.1042/bj3030749;
RA Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.;
RT "Palmitoylation of multiple Src-family kinases at a homologous N-terminal
RT motif.";
RL Biochem. J. 303:749-753(1994).
RN [8]
RP PHOSPHORYLATION BY CSK.
RX PubMed=9281320; DOI=10.1006/abbi.1997.0236;
RA Sun G., Budde R.J.;
RT "Expression, purification, and initial characterization of human Yes
RT protein tyrosine kinase from a bacterial expression system.";
RL Arch. Biochem. Biophys. 345:135-142(1997).
RN [9]
RP PHOSPHORYLATION AT TYR-426, AND MUTAGENESIS OF TYR-426.
RX PubMed=9794236; DOI=10.1038/sj.onc.1202076;
RA Sun G., Sharma A.K., Budde R.J.;
RT "Autophosphorylation of Src and Yes blocks their inactivation by Csk
RT phosphorylation.";
RL Oncogene 17:1587-1595(1998).
RN [10]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND FUNCTION.
RX PubMed=11901164; DOI=10.1083/jcb.200109005;
RA Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L., So M.;
RT "CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells
RT by Neisseria gonorrhoeae.";
RL J. Cell Biol. 156:951-957(2002).
RN [11]
RP REVIEW ON FUNCTION.
RX PubMed=16338789; DOI=10.1080/08977190500199360;
RA Clump D.A., Qazi I.H., Sudol M., Flynn D.C.;
RT "c-Yes response to growth factor activation.";
RL Growth Factors 23:263-272(2005).
RN [12]
RP FUNCTION IN PHOSPHORYLATION OF CDK4.
RX PubMed=18479465; DOI=10.1111/j.1742-4658.2008.06463.x;
RA Martin N.G., McAndrew P.C., Eve P.D., Garrett M.D.;
RT "Phosphorylation of cyclin dependent kinase 4 on tyrosine 17 is mediated by
RT Src family kinases.";
RL FEBS J. 275:3099-3109(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-40, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [16]
RP FUNCTION IN PHOSPHORYLATION OF DPYSL2.
RX PubMed=19276087; DOI=10.1074/jbc.m807664200;
RA Varrin-Doyer M., Vincent P., Cavagna S., Auvergnon N., Noraz N.,
RA Rogemond V., Honnorat J., Moradi-Ameli M., Giraudon P.;
RT "Phosphorylation of collapsin response mediator protein 2 on Tyr-479
RT regulates CXCL12-induced T lymphocyte migration.";
RL J. Biol. Chem. 284:13265-13276(2009).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=19258394; DOI=10.1242/jcs.034843;
RA Sato I., Obata Y., Kasahara K., Nakayama Y., Fukumoto Y., Yamasaki T.,
RA Yokoyama K.K., Saito T., Yamaguchi N.;
RT "Differential trafficking of Src, Lyn, Yes and Fyn is specified by the
RT state of palmitoylation in the SH4 domain.";
RL J. Cell Sci. 122:965-975(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336; TYR-345 AND TYR-537, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21566460; DOI=10.4161/cc.10.9.15495;
RA Jung J., Lee M.K., Jin Y., Fu S.B., Rosales J.L., Lee K.Y.;
RT "Clues for c-Yes involvement in the cell cycle and cytokinesis.";
RL Cell Cycle 10:1502-1503(2011).
RN [20]
RP FUNCTION.
RX PubMed=21713032; DOI=10.1371/journal.pbio.1001090;
RA Tauzin S., Chaigne-Delalande B., Selva E., Khadra N., Daburon S.,
RA Contin-Bordes C., Blanco P., Le Seyec J., Ducret T., Counillon L.,
RA Moreau J.F., Hofman P., Vacher P., Legembre P.;
RT "The naturally processed CD95L elicits a c-yes/calcium/PI3K-driven cell
RT migration pathway.";
RL PLoS Biol. 9:E1001090-E1001090(2011).
RN [21]
RP INTERACTION WITH IL6ST.
RX PubMed=25731159; DOI=10.1038/nature14228;
RA Taniguchi K., Wu L.W., Grivennikov S.I., de Jong P.R., Lian I., Yu F.X.,
RA Wang K., Ho S.B., Boland B.S., Chang J.T., Sandborn W.J., Hardiman G.,
RA Raz E., Maehara Y., Yoshimura A., Zucman-Rossi J., Guan K.L., Karin M.;
RT "A gp130-Src-YAP module links inflammation to epithelial regeneration.";
RL Nature 519:57-62(2015).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 91-152.
RX PubMed=17418139; DOI=10.1016/j.febslet.2007.03.059;
RA Martin-Garcia J.M., Luque I., Mateo P.L., Ruiz-Sanz J., Camara-Artigas A.;
RT "Crystallographic structure of the SH3 domain of the human c-Yes tyrosine
RT kinase: loop flexibility and amyloid aggregation.";
RL FEBS Lett. 581:1701-1706(2007).
RN [23]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-198 AND ARG-282.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Non-receptor protein tyrosine kinase that is involved in the
CC regulation of cell growth and survival, apoptosis, cell-cell adhesion,
CC cytoskeleton remodeling, and differentiation. Stimulation by receptor
CC tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to
CC recruitment of YES1 to the phosphorylated receptor, and activation and
CC phosphorylation of downstream substrates. Upon EGFR activation,
CC promotes the phosphorylation of PARD3 to favor epithelial tight
CC junction assembly. Participates in the phosphorylation of specific
CC junctional components such as CTNND1 by stimulating the FYN and FER
CC tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by
CC CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and
CC induces T-cell migration. Participates in CD95L/FASLG signaling pathway
CC and mediates AKT-mediated cell migration. Plays a role in cell cycle
CC progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus
CC regulating the G1 phase. Also involved in G2/M progression and
CC cytokinesis. {ECO:0000269|PubMed:11901164, ECO:0000269|PubMed:18479465,
CC ECO:0000269|PubMed:19276087, ECO:0000269|PubMed:21566460,
CC ECO:0000269|PubMed:21713032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Interacts with YAP1 and CSF1R (By similarity). Interacts with
CC CTNND1; this interaction allows YES1-mediated activation of FYN and FER
CC and subsequent phosphorylation of CTNND1 (By similarity). Interacts
CC with FASLG. Interacts with IL6ST/gp130 (PubMed:25731159). {ECO:0000250,
CC ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:25731159}.
CC -!- INTERACTION:
CC P07947; O14672: ADAM10; NbExp=2; IntAct=EBI-515331, EBI-1536151;
CC P07947; P09917: ALOX5; NbExp=2; IntAct=EBI-515331, EBI-79934;
CC P07947; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-515331, EBI-746752;
CC P07947; P10275: AR; NbExp=5; IntAct=EBI-515331, EBI-608057;
CC P07947; Q12774: ARHGEF5; NbExp=3; IntAct=EBI-515331, EBI-602199;
CC P07947; Q9ULH1: ASAP1; NbExp=2; IntAct=EBI-515331, EBI-346622;
CC P07947; P56945: BCAR1; NbExp=4; IntAct=EBI-515331, EBI-702093;
CC P07947; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-515331, EBI-11975051;
CC P07947; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-515331, EBI-946029;
CC P07947; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-515331, EBI-11530605;
CC P07947; Q13191: CBLB; NbExp=3; IntAct=EBI-515331, EBI-744027;
CC P07947; Q9ULV8: CBLC; NbExp=3; IntAct=EBI-515331, EBI-2341018;
CC P07947; Q16543: CDC37; NbExp=4; IntAct=EBI-515331, EBI-295634;
CC P07947; Q9H5V8: CDCP1; NbExp=2; IntAct=EBI-515331, EBI-1019736;
CC P07947; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-515331, EBI-1104570;
CC P07947; Q9Y592-2: CEP83; NbExp=3; IntAct=EBI-515331, EBI-11123098;
CC P07947; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-515331, EBI-1057156;
CC P07947; Q16630-2: CPSF6; NbExp=3; IntAct=EBI-515331, EBI-11088043;
CC P07947; P46109: CRKL; NbExp=3; IntAct=EBI-515331, EBI-910;
CC P07947; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-515331, EBI-3867333;
CC P07947; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-515331, EBI-742054;
CC P07947; Q68D51-2: DENND2C; NbExp=3; IntAct=EBI-515331, EBI-13075846;
CC P07947; P17661: DES; NbExp=3; IntAct=EBI-515331, EBI-1055572;
CC P07947; O60496: DOK2; NbExp=3; IntAct=EBI-515331, EBI-1046024;
CC P07947; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-515331, EBI-2340258;
CC P07947; O43281-2: EFS; NbExp=5; IntAct=EBI-515331, EBI-11525448;
CC P07947; P00533: EGFR; NbExp=3; IntAct=EBI-515331, EBI-297353;
CC P07947; P25445-1: FAS; NbExp=2; IntAct=EBI-515331, EBI-15749113;
CC P07947; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-515331, EBI-11533409;
CC P07947; Q8IVP5: FUNDC1; NbExp=4; IntAct=EBI-515331, EBI-3059266;
CC P07947; P51114-2: FXR1; NbExp=3; IntAct=EBI-515331, EBI-11022345;
CC P07947; P51116: FXR2; NbExp=6; IntAct=EBI-515331, EBI-740459;
CC P07947; Q13480: GAB1; NbExp=7; IntAct=EBI-515331, EBI-517684;
CC P07947; O95995: GAS8; NbExp=3; IntAct=EBI-515331, EBI-1052570;
CC P07947; P14136: GFAP; NbExp=3; IntAct=EBI-515331, EBI-744302;
CC P07947; P08238: HSP90AB1; NbExp=3; IntAct=EBI-515331, EBI-352572;
CC P07947; Q9UKT9: IKZF3; NbExp=5; IntAct=EBI-515331, EBI-747204;
CC P07947; Q96N16: JAKMIP1; NbExp=3; IntAct=EBI-515331, EBI-2680803;
CC P07947; P10721: KIT; NbExp=7; IntAct=EBI-515331, EBI-1379503;
CC P07947; Q14847-2: LASP1; NbExp=3; IntAct=EBI-515331, EBI-9088686;
CC P07947; Q9NUP9: LIN7C; NbExp=3; IntAct=EBI-515331, EBI-1171517;
CC P07947; Q9H204: MED28; NbExp=2; IntAct=EBI-515331, EBI-514199;
CC P07947; P08581: MET; NbExp=3; IntAct=EBI-515331, EBI-1039152;
CC P07947; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-515331, EBI-740897;
CC P07947; Q8TAK6: OLIG1; NbExp=3; IntAct=EBI-515331, EBI-3867416;
CC P07947; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-515331, EBI-79165;
CC P07947; Q92569: PIK3R3; NbExp=3; IntAct=EBI-515331, EBI-79893;
CC P07947; Q9BXM0: PRX; NbExp=4; IntAct=EBI-515331, EBI-1753064;
CC P07947; I6L996: PTK2; NbExp=6; IntAct=EBI-515331, EBI-10181089;
CC P07947; Q05397: PTK2; NbExp=2; IntAct=EBI-515331, EBI-702142;
CC P07947; P49023-2: PXN; NbExp=3; IntAct=EBI-515331, EBI-11954250;
CC P07947; Q15428: SF3A2; NbExp=3; IntAct=EBI-515331, EBI-2462271;
CC P07947; Q9NR46: SH3GLB2; NbExp=3; IntAct=EBI-515331, EBI-749607;
CC P07947; O14508: SOCS2; NbExp=3; IntAct=EBI-515331, EBI-617737;
CC P07947; O14543: SOCS3; NbExp=6; IntAct=EBI-515331, EBI-714146;
CC P07947; O14512: SOCS7; NbExp=3; IntAct=EBI-515331, EBI-1539606;
CC P07947; Q9BWW4: SSBP3; NbExp=6; IntAct=EBI-515331, EBI-2902395;
CC P07947; Q9UGK3: STAP2; NbExp=3; IntAct=EBI-515331, EBI-1553984;
CC P07947; Q9NVV9: THAP1; NbExp=6; IntAct=EBI-515331, EBI-741515;
CC P07947; Q12933: TRAF2; NbExp=6; IntAct=EBI-515331, EBI-355744;
CC P07947; Q9Y4K3: TRAF6; NbExp=6; IntAct=EBI-515331, EBI-359276;
CC P07947; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-515331, EBI-12840050;
CC P07947; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-515331, EBI-10241197;
CC P07947; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-515331, EBI-742740;
CC P07947; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-515331, EBI-5458880;
CC P07947; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-515331, EBI-11962468;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Cytoplasm, cytosol.
CC Note=Newly synthesized protein initially accumulates in the Golgi
CC region and traffics to the plasma membrane through the exocytic
CC pathway.
CC -!- TISSUE SPECIFICITY: Expressed in the epithelial cells of renal proximal
CC tubules and stomach as well as hematopoietic cells in the bone marrow
CC and spleen in the fetal tissues. In adult, expressed in epithelial
CC cells of the renal proximal tubules and present in keratinocytes in the
CC basal epidermal layer of epidermis. {ECO:0000269|PubMed:2021534,
CC ECO:0000269|PubMed:2067846}.
CC -!- PTM: Phosphorylation by CSK on the C-terminal tail maintains the enzyme
CC in an inactive state. Autophosphorylation at Tyr-426 maintains enzyme
CC activity by blocking CSK-mediated inhibition.
CC {ECO:0000269|PubMed:11901164, ECO:0000269|PubMed:9281320,
CC ECO:0000269|PubMed:9794236}.
CC -!- PTM: Palmitoylation at Cys-3 promotes membrane localization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M15990; AAA35735.1; -; mRNA.
DR EMBL; AP001178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01709.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01710.1; -; Genomic_DNA.
DR EMBL; BC048960; AAH48960.1; -; mRNA.
DR CCDS; CCDS11824.1; -.
DR PIR; A26714; TVHUYS.
DR RefSeq; NP_005424.1; NM_005433.3.
DR RefSeq; XP_016881449.1; XM_017025960.1.
DR PDB; 2HDA; X-ray; 1.90 A; A=91-152.
DR PDBsum; 2HDA; -.
DR AlphaFoldDB; P07947; -.
DR SMR; P07947; -.
DR BioGRID; 113357; 384.
DR CORUM; P07947; -.
DR DIP; DIP-33849N; -.
DR ELM; P07947; -.
DR IntAct; P07947; 258.
DR MINT; P07947; -.
DR STRING; 9606.ENSP00000462468; -.
DR BindingDB; P07947; -.
DR ChEMBL; CHEMBL2073; -.
DR DrugBank; DB01254; Dasatinib.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; P07947; -.
DR GuidetoPHARMACOLOGY; 2284; -.
DR GlyGen; P07947; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07947; -.
DR PhosphoSitePlus; P07947; -.
DR SwissPalm; P07947; -.
DR BioMuta; YES1; -.
DR DMDM; 125870; -.
DR EPD; P07947; -.
DR jPOST; P07947; -.
DR MassIVE; P07947; -.
DR MaxQB; P07947; -.
DR PaxDb; P07947; -.
DR PeptideAtlas; P07947; -.
DR PRIDE; P07947; -.
DR ProteomicsDB; 52044; -.
DR Antibodypedia; 3819; 503 antibodies from 37 providers.
DR DNASU; 7525; -.
DR Ensembl; ENST00000314574.5; ENSP00000324740.4; ENSG00000176105.14.
DR Ensembl; ENST00000584307.5; ENSP00000462468.1; ENSG00000176105.14.
DR GeneID; 7525; -.
DR KEGG; hsa:7525; -.
DR MANE-Select; ENST00000314574.5; ENSP00000324740.4; NM_005433.4; NP_005424.1.
DR UCSC; uc002kky.4; human.
DR CTD; 7525; -.
DR DisGeNET; 7525; -.
DR GeneCards; YES1; -.
DR HGNC; HGNC:12841; YES1.
DR HPA; ENSG00000176105; Low tissue specificity.
DR MIM; 164880; gene.
DR neXtProt; NX_P07947; -.
DR OpenTargets; ENSG00000176105; -.
DR PharmGKB; PA37432; -.
DR VEuPathDB; HostDB:ENSG00000176105; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000154920; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; P07947; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; P07947; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; P07947; -.
DR Reactome; R-HSA-1227986; Signaling by ERBB2.
DR Reactome; R-HSA-1433557; Signaling by SCF-KIT.
DR Reactome; R-HSA-1433559; Regulation of KIT signaling.
DR Reactome; R-HSA-2029481; FCGR activation.
DR Reactome; R-HSA-210990; PECAM1 interactions.
DR Reactome; R-HSA-2682334; EPH-Ephrin signaling.
DR Reactome; R-HSA-389356; CD28 co-stimulation.
DR Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR Reactome; R-HSA-912631; Regulation of signaling by CBL.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-9670439; Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants.
DR SignaLink; P07947; -.
DR SIGNOR; P07947; -.
DR BioGRID-ORCS; 7525; 23 hits in 1108 CRISPR screens.
DR ChiTaRS; YES1; human.
DR EvolutionaryTrace; P07947; -.
DR GeneWiki; YES1; -.
DR GenomeRNAi; 7525; -.
DR Pharos; P07947; Tclin.
DR PRO; PR:P07947; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P07947; protein.
DR Bgee; ENSG00000176105; Expressed in secondary oocyte and 215 other tissues.
DR ExpressionAtlas; P07947; baseline and differential.
DR Genevisible; P07947; HS.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
DR GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; TAS:Reactome.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0010827; P:regulation of glucose transmembrane transport; IEA:Ensembl.
DR GO; GO:0043114; P:regulation of vascular permeability; TAS:BHF-UCL.
DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd12007; SH3_Yes; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR035751; Yes_SH3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate;
KW Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
KW Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..543
FT /note="Tyrosine-protein kinase Yes"
FT /id="PRO_0000088181"
FT DOMAIN 91..152
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 158..255
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 277..530
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 283..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 32
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q04736"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 336
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 345
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 426
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9794236"
FT MOD_RES 446
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305"
FT MOD_RES 537
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine; in membrane form"
FT /evidence="ECO:0000250"
FT VARIANT 198
FT /note="I -> V (in dbSNP:rs34580680)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041879"
FT VARIANT 282
FT /note="K -> R (in dbSNP:rs35126906)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041880"
FT MUTAGEN 426
FT /note="Y->F: About 50% loss of CSK-mediated inhibition."
FT /evidence="ECO:0000269|PubMed:9794236"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:2HDA"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:2HDA"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:2HDA"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2HDA"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2HDA"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2HDA"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2HDA"
SQ SEQUENCE 543 AA; 60801 MW; A2B376084686BBCD CRC64;
MGCIKSKENK SPAIKYRPEN TPEPVSTSVS HYGAEPTTVS PCPSSSAKGT AVNFSSLSMT
PFGGSSGVTP FGGASSSFSV VPSSYPAGLT GGVTIFVALY DYEARTTEDL SFKKGERFQI
INNTEGDWWE ARSIATGKNG YIPSNYVAPA DSIQAEEWYF GKMGRKDAER LLLNPGNQRG
IFLVRESETT KGAYSLSIRD WDEIRGDNVK HYKIRKLDNG GYYITTRAQF DTLQKLVKHY
TEHADGLCHK LTTVCPTVKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT
KVAIKTLKPG TMMPEAFLQE AQIMKKLRHD KLVPLYAVVS EEPIYIVTEF MSKGSLLDFL
KEGDGKYLKL PQLVDMAAQI ADGMAYIERM NYIHRDLRAA NILVGENLVC KIADFGLARL
IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LQTELVTKGR VPYPGMVNRE
VLEQVERGYR MPCPQGCPES LHELMNLCWK KDPDERPTFE YIQSFLEDYF TATEPQYQPG
ENL
