ID SRC_HUMAN Reviewed; 536 AA. AC P12931; E1P5V4; Q76P87; Q86VB9; Q9H5A8; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 268. DE RecName: Full=Proto-oncogene tyrosine-protein kinase Src {ECO:0000305}; DE EC=2.7.10.2 {ECO:0000269|PubMed:14632929, ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:21036157, ECO:0000269|PubMed:7929427, ECO:0000269|PubMed:8759729, ECO:0000269|PubMed:9571170}; DE AltName: Full=Proto-oncogene c-Src; DE AltName: Full=pp60c-src; DE Short=p60-Src; GN Name=SRC {ECO:0000312|HGNC:HGNC:11283}; Synonyms=SRC1; 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Skin; 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185 (ISOFORM 1). RX PubMed=3299057; DOI=10.1128/mcb.7.5.1978-1983.1987; RA Tanaka A., Gibbs C.P., Arthur R.R., Anderson S.K., Kung H.-J., Fujita D.J.; RT "DNA sequence encoding the amino-terminal region of the human c-src RT protein: implications of sequence divergence among src-type kinase RT oncogenes."; RL Mol. Cell. Biol. 7:1978-1983(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-536 (ISOFORM 1). RX PubMed=2582238; DOI=10.1128/mcb.5.5.1122-1129.1985; RA Anderson S.K., Gibbs C.P., Tanaka A., Kung H.-J., Fujita D.J.; RT "Human cellular src gene: nucleotide sequence and derived amino acid RT sequence of the region coding for the carboxy-terminal two-thirds of pp60c- RT src."; RL Mol. Cell. Biol. 5:1122-1129(1985). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 98-139 (ISOFORM 2). RX PubMed=2681803; DOI=10.1002/jnr.490240113; RA Pyper J.M., Bolen J.B.; RT "Neuron-specific splicing of C-SRC RNA in human brain."; RL J. Neurosci. Res. 24:89-96(1989). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-536 (ISOFORM 1). RX PubMed=2581127; DOI=10.1128/mcb.5.4.831-838.1985; RA Parker R.C., Mardon G., Lebo R.V., Varmus H.E., Bishop J.M.; RT "Isolation of duplicated human c-src genes located on chromosomes 1 and RT 20."; RL Mol. Cell. Biol. 5:831-838(1985). RN [8] RP PHOSPHORYLATION AT TYR-419. RX PubMed=6273838; DOI=10.1073/pnas.78.10.6013; RA Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F., Erikson R.L., RA Bishop J.M.; RT "Characterization of sites for tyrosine phosphorylation in the transforming RT protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue RT (pp60c-src)."; RL Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981). RN [9] RP ROLE IN TUMOR TISSUES. RX PubMed=3093483; DOI=10.1016/s0021-9258(18)67084-x; RA Rosen N., Bolen J.B., Schwartz A.M., Cohen P., DeSeau V., Israel M.A.; RT "Analysis of pp60c-src protein kinase activity in human tumor cell lines RT and tissues."; RL J. Biol. Chem. 261:13754-13759(1986). RN [10] RP ROLE IN COLON CARCINOMA. RX PubMed=2498394; DOI=10.1172/jci114113; RA Cartwright C.A., Kamps M.P., Meisler A.I., Pipas J.M., Eckhart W.; RT "pp60c-src activation in human colon carcinoma."; RL J. Clin. Invest. 83:2025-2033(1989). RN [11] RP ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE (ISOFORMS 1; 2 AND 3). RX PubMed=1691439; DOI=10.1128/mcb.10.5.2035-2040.1990; RA Pyper J.M., Bolen J.B.; RT "Identification of a novel neuronal C-SRC exon expressed in human brain."; RL Mol. Cell. Biol. 10:2035-2040(1990). RN [12] RP TISSUE SPECIFICITY (ISOFORMS 1; 2 AND 3). RX PubMed=8319227; RA Matsunaga T., Shirasawa H., Tanabe M., Ohnuma N., Takahashi H., Simizu B.; RT "Expression of alternatively spliced src messenger RNAs related to neuronal RT differentiation in human neuroblastomas."; RL Cancer Res. 53:3179-3185(1993). RN [13] RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-530, AND MYRISTOYLATION AT RP GLY-2. RX PubMed=7525268; DOI=10.1002/j.1460-2075.1994.tb06800.x; RA Kaplan K.B., Bibbins K.B., Swedlow J.R., Arnaud M., Morgan D.O., RA Varmus H.E.; RT "Association of the amino-terminal half of c-Src with focal adhesions RT alters their properties and is regulated by phosphorylation of tyrosine RT 527."; RL EMBO J. 13:4745-4756(1994). RN [14] RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PHOSPHORYLATION AT TYR-530. RX PubMed=7929427; DOI=10.1016/s0021-9258(18)47102-5; RA Stover D.R., Liebetanz J., Lydon N.B.; RT "Cdc2-mediated modulation of pp60c-src activity."; RL J. Biol. Chem. 269:26885-26889(1994). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=7853507; DOI=10.1128/jvi.69.3.1699-1713.1995; RA David-Pfeuty T., Nouvian-Dooghe Y.; RT "Highly specific antibody to Rous sarcoma virus src gene product recognizes RT nuclear and nucleolar antigens in human cells."; RL J. Virol. 69:1699-1713(1995). RN [16] RP INTERACTION WITH CEACAM1. RX PubMed=7478590; RA Bruemmer J., Neumaier M., Goepfert C., Wagener C.; RT "Association of pp60c-src with biliary glycoprotein (CD66a), an adhesion RT molecule of the carcinoembryonic antigen family downregulated in colorectal RT carcinomas."; RL Oncogene 11:1649-1655(1995). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH RP FCAMR. RX PubMed=8759729; RA Rabinowich H., Manciulea M., Metes D., Sulica A., Herberman R.B., RA Corey S.J., Whiteside T.L.; RT "Physical and functional association of Fc mu receptor on human natural RT killer cells with the zeta- and Fc epsilon RI gamma-chains and with src RT family protein tyrosine kinases."; RL J. Immunol. 157:1485-1491(1996). RN [18] RP FUNCTION IN HGF SIGNALING PATHWAY. RX PubMed=8755529; DOI=10.1073/pnas.93.15.7644; RA Grano M., Galimi F., Zambonin G., Colucci S., Cottone E., Zallone A.Z., RA Comoglio P.M.; RT "Hepatocyte growth factor is a coupling factor for osteoclasts and RT osteoblasts in vitro."; RL Proc. Natl. Acad. Sci. U.S.A. 93:7644-7648(1996). RN [19] RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=9571170; DOI=10.1006/bbrc.1998.8452; RA Yang E.B., Zhang K., Cheng L.Y., Mack P.; RT "Butein, a specific protein tyrosine kinase inhibitor."; RL Biochem. Biophys. Res. Commun. 245:435-438(1998). RN [20] RP INTERACTION WITH RACK1. RX PubMed=9584165; DOI=10.1128/mcb.18.6.3245; RA Chang B.Y., Conroy K.B., Machleder E.M., Cartwright C.A.; RT "RACK1, a receptor for activated C kinase and a homolog of the beta subunit RT of G proteins, inhibits activity of src tyrosine kinases and growth of NIH RT 3T3 cells."; RL Mol. Cell. Biol. 18:3245-3256(1998). RN [21] RP INTERACTION WITH ADRB2 AND ARRB1. RX PubMed=9924018; DOI=10.1126/science.283.5402.655; RA Luttrell L.M., Ferguson S.S.G., Daaka Y., Miller W.E., Maudsley S., RA Della Rocca G.J., Lin F.-T., Kawakatsu H., Owada K., Luttrell D.K., RA Caron M.G., Lefkowitz R.J.; RT "Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein RT kinase complexes."; RL Science 283:655-661(1999). RN [22] RP INTERACTION WITH ARRB1 AND ARRB2. RX PubMed=10753943; DOI=10.1074/jbc.275.15.11312; RA Miller W.E., Maudsley S., Ahn S., Khan K.D., Luttrell L.M., Lefkowitz R.J.; RT "beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase RT c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor RT endocytosis."; RL J. Biol. Chem. 275:11312-11319(2000). RN [23] RP INTERACTION WITH RALGPS1. RX PubMed=10747847; DOI=10.1074/jbc.c000085200; RA Rebhun J.F., Chen H., Quilliam L.A.; RT "Identification and characterization of a new family of guanine nucleotide RT exchange factors for the ras-related GTPase Ral."; RL J. Biol. Chem. 275:13406-13410(2000). RN [24] RP FUNCTION IN PHOSPHORYLATION OF RASA1 AND RASGRF1. RX PubMed=11389730; DOI=10.1046/j.1432-1327.2001.02230.x; RA Giglione C., Gonfloni S., Parmeggiani A.; RT "Differential actions of p60c-Src and Lck kinases on the Ras regulators RT p120-GAP and GDP/GTP exchange factor CDC25Mm."; RL Eur. J. Biochem. 268:3275-3283(2001). RN [25] RP INTERACTION WITH MUC1. RX PubMed=11152665; DOI=10.1074/jbc.c000754200; RA Li Y., Kuwahara H., Ren J., Wen G., Kufe D.; RT "The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 RT carcinoma-associated antigen with GSK3 beta and beta-catenin."; RL J. Biol. Chem. 276:6061-6064(2001). RN [26] RP INTERACTION WITH RACK1. RX PubMed=11279199; DOI=10.1074/jbc.m101375200; RA Chang B.Y., Chiang M., Cartwright C.A.; RT "The interaction of Src and RACK1 is enhanced by activation of protein RT kinase C and tyrosine phosphorylation of RACK1."; RL J. Biol. Chem. 276:20346-20356(2001). RN [27] RP INTERACTION WITH HEV ORF3 PROTEIN (MICROBIAL INFECTION). RX PubMed=11518702; DOI=10.1074/jbc.m101546200; RA Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., RA Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.; RT "The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and RT activates MAPK."; RL J. Biol. Chem. 276:42389-42400(2001). RN [28] RP INTERACTION WITH CAV2. RX PubMed=12091389; DOI=10.1074/jbc.m204367200; RA Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.; RT "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho- RT caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated RT with lipid rafts/caveolae, but no longer forms a high molecular mass RT hetero-oligomer with caveolin-1."; RL J. Biol. Chem. 277:34556-34567(2002). RN [29] RP RETRACTED PAPER. RX PubMed=12415108; DOI=10.1073/pnas.192569699; RA Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.; RT "Estrogen receptor-interacting protein that modulates its nongenomic RT activity-crosstalk with Src/Erk phosphorylation cascade."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002). RN [30] RP RETRACTION NOTICE OF PUBMED:12415108. RX PubMed=19666546; DOI=10.1073/pnas.0908685106; RA Wong C.W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.; RL Proc. Natl. Acad. Sci. U.S.A. 106:14180-14180(2009). RN [31] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12615910; DOI=10.1083/jcb.200209098; RA Miyazaki T., Neff L., Tanaka S., Horne W.C., Baron R.; RT "Regulation of cytochrome c oxidase activity by c-Src in osteoclasts."; RL J. Cell Biol. 160:709-718(2003). RN [32] RP INTERACTION WITH EPHB1. RX PubMed=12925710; DOI=10.1083/jcb.200302073; RA Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.; RT "EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote RT chemotaxis."; RL J. Cell Biol. 162:661-671(2003). RN [33] RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=14632929; DOI=10.1046/j.1399-3011.2003.00094.x; RA Kamath J.R., Liu R., Enstrom A.M., Lou Q., Lam K.S.; RT "Development and characterization of potent and specific peptide inhibitors RT of p60c-src protein tyrosine kinase using pseudosubstrate-based inhibitor RT design approach."; RL J. Pept. Res. 62:260-268(2003). RN [34] RP FUNCTION IN PHOSPHORYLATION OF PDPK1, AND INTERACTION WITH PTK2B/PYK2. RX PubMed=14585963; DOI=10.1128/mcb.23.22.8019-8029.2003; RA Taniyama Y., Weber D.S., Rocic P., Hilenski L., Akers M.L., Park J., RA Hemmings B.A., Alexander R.W., Griendling K.K.; RT "Pyk2- and Src-dependent tyrosine phosphorylation of PDK1 regulates focal RT adhesions."; RL Mol. Cell. Biol. 23:8019-8029(2003). RN [35] RP INTERACTION WITH CAV2. RX PubMed=15504032; DOI=10.1021/bi049295+; RA Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., RA Campos-Gonzalez R., Lisanti M.P.; RT "Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the RT spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."; RL Biochemistry 43:13694-13706(2004). RN [36] RP INTERACTION WITH PELP1. RX PubMed=14963108; DOI=10.1210/me.2003-0335; RA Barletta F., Wong C.-W., McNally C., Komm B.S., Katzenellenbogen B., RA Cheskis B.J.; RT "Characterization of the interactions of estrogen receptor and MNAR in the RT activation of cSrc."; RL Mol. Endocrinol. 18:1096-1108(2004). RN [37] RP INTERACTION WITH CBCLC, PHOSPHORYLATION AT TYR-419, AND MUTAGENESIS OF RP LYS-298. RX PubMed=14661060; DOI=10.1038/sj.onc.1207298; RA Kim M., Tezuka T., Tanaka K., Yamamoto T.; RT "Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent RT protein degradation."; RL Oncogene 23:1645-1655(2004). RN [38] RP INTERACTION WITH CDCP1. RX PubMed=15851033; DOI=10.1016/j.cell.2005.02.019; RA Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.; RT "The C2 domain of PKCdelta is a phosphotyrosine binding domain."; RL Cell 121:271-280(2005). RN [39] RP FUNCTION IN PHOSPHORYLATION OF DDR2. RX PubMed=16186108; DOI=10.1074/jbc.m506921200; RA Yang K., Kim J.H., Kim H.J., Park I.S., Kim I.Y., Yang B.S.; RT "Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src RT stimulates intramolecular autophosphorylation and Shc signaling complex RT formation."; RL J. Biol. Chem. 280:39058-39066(2005). RN [40] RP FUNCTION. RX PubMed=16619028; DOI=10.1038/sj.emboj.7601085; RA Cursi S., Rufini A., Stagni V., Condo I., Matafora V., Bachi A., RA Bonifazi A.P., Coppola L., Superti-Furga G., Testi R., Barila D.; RT "Src kinase phosphorylates Caspase-8 on Tyr380: a novel mechanism of RT apoptosis suppression."; RL EMBO J. 25:1895-1905(2006). RN [41] RP INTERACTION WITH TOM1L2. RX PubMed=16479011; DOI=10.1128/mcb.26.5.1932-1947.2006; RA Franco M., Furstoss O., Simon V., Benistant C., Hong W.J., Roche S.; RT "The adaptor protein Tom1L1 is a negative regulator of Src mitogenic RT signaling induced by growth factors."; RL Mol. Cell. Biol. 26:1932-1947(2006). RN [42] RP INTERACTION WITH TGFB1I1. RX PubMed=17202804; DOI=10.1159/000098402; RA Maudsley S., Davidson L., Pawson A.J., Freestone S.H., RA Lopez de Maturana R., Thomson A.A., Millar R.P.; RT "Gonadotropin-releasing hormone functionally antagonizes testosterone RT activation of the human androgen receptor in prostate cells through focal RT adhesion complexes involving Hic-5."; RL Neuroendocrinology 84:285-300(2006). RN [43] RP INTERACTION WITH AMOTL2. RX PubMed=17293535; DOI=10.1242/dev.02782; RA Huang H., Lu F.I., Jia S., Meng S., Cao Y., Wang Y., Ma W., Yin K., Wen Z., RA Peng J., Thisse C., Thisse B., Meng A.; RT "Amotl2 is essential for cell movements in zebrafish embryo and regulates RT c-Src translocation."; RL Development 134:979-988(2007). RN [44] RP INTERACTION WITH SRCIN1. RX PubMed=17525734; DOI=10.1038/sj.emboj.7601724; RA Di Stefano P., Damiano L., Cabodi S., Aramu S., Tordella L., Praduroux A., RA Piva R., Cavallo F., Forni G., Silengo L., Tarone G., Turco E., RA Defilippi P.; RT "p140Cap protein suppresses tumour cell properties, regulating Csk and Src RT kinase activity."; RL EMBO J. 26:2843-2855(2007). RN [45] RP FUNCTION. RX PubMed=18586953; DOI=10.1152/ajplung.90282.2008; RA Jeulin C., Seltzer V., Bailbe D., Andreau K., Marano F.; RT "EGF mediates calcium-activated chloride channel activation in the human RT bronchial epithelial cell line 16HBE14o-: involvement of tyrosine kinase RT p60c-src."; RL Am. J. Physiol. 295:L489-L496(2008). RN [46] RP INTERACTION WITH PDPK1. RX PubMed=18024423; DOI=10.1074/jbc.m706361200; RA Yang K.J., Shin S., Piao L., Shin E., Li Y., Park K.A., Byun H.S., Won M., RA Hong J., Kweon G.R., Hur G.M., Seok J.H., Chun T., Brazil D.P., RA Hemmings B.A., Park J.; RT "Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src RT involves tyrosine phosphorylation of PDK1 and Src homology 2 domain RT binding."; RL J. Biol. Chem. 283:1480-1491(2008). RN [47] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [48] RP INTERACTION WITH PTK2/FAK1; PI3KR1/2 AND ESR1. RX PubMed=18657504; DOI=10.1016/j.molcel.2008.05.025; RA Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S., RA Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.; RT "Regulation of estrogen rapid signaling through arginine methylation by RT PRMT1."; RL Mol. Cell 31:212-221(2008). RN [49] RP IDENTIFICATION BY 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 [50] 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 [51] RP INTERACTION WITH MPP2. RX PubMed=19665017; DOI=10.1016/j.yexcr.2009.07.028; RA Baumgartner M., Weiss A., Fritzius T., Heinrich J., Moelling K.; RT "The PDZ protein MPP2 interacts with c-Src in epithelial cells."; RL Exp. Cell Res. 315:2888-2898(2009). RN [52] RP FUNCTION, AND INTERACTION WITH TRAF3; MAVS; RIGI AND TBK1. RX PubMed=19419966; DOI=10.1074/jbc.m808233200; RA Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.; RT "The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)- RT elicited antiviral signaling."; RL J. Biol. Chem. 284:19122-19131(2009). RN [53] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PDLIM4, SUBCELLULAR RP LOCATION, PHOSPHORYLATION AT TYR-419 AND TYR-530, AND MUTAGENESIS OF RP PRO-302; PRO-307 AND TYR-419. RX PubMed=19307596; DOI=10.1083/jcb.200810155; RA Zhang Y., Tu Y., Zhao J., Chen K., Wu C.; RT "Reversion-induced LIM interaction with Src reveals a novel Src RT inactivation cycle."; RL J. Cell Biol. 184:785-792(2009). RN [54] RP PHOSPHORYLATION AT TYR-419, AND DEPHOSPHORYLATION AT TYR-419 BY PTPRJ. RX PubMed=18936167; DOI=10.1128/mcb.01374-08; RA Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.; RT "New role for the protein tyrosine phosphatase DEP-1 in Akt activation and RT endothelial cell survival."; RL Mol. Cell. Biol. 29:241-253(2009). RN [55] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND TYR-530, 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 [56] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [57] RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=21036157; DOI=10.1016/j.bbrc.2010.10.101; RA Yao X., Balamurugan P., Arvey A., Leslie C., Zhang L.; RT "Heme controls the regulation of protein tyrosine kinases Jak2 and Src."; RL Biochem. Biophys. Res. Commun. 403:30-35(2010). RN [58] RP FUNCTION, AND INTERACTION WITH RUNX3. RX PubMed=20100835; DOI=10.1074/jbc.m109.071381; RA Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W., Li Y.H., RA Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.; RT "Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the RT protein in the cytoplasm."; RL J. Biol. Chem. 285:10122-10129(2010). RN [59] RP FUNCTION IN CBLC PHOSPHORYLATION. RX PubMed=20525694; DOI=10.1074/jbc.m109.091157; RA Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.; RT "The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating RT affinity for the ubiquitin-conjugating enzyme."; RL J. Biol. Chem. 285:23687-23698(2010). RN [60] RP INTERACTION WITH NDFIP1 AND NDFIP2. RX PubMed=20534535; DOI=10.1073/pnas.0911714107; RA Mund T., Pelham H.R.; RT "Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin RT ligase activators Ndfip1 and Ndfip2."; RL Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010). RN [61] RP FUNCTION, AND INTERACTION WITH TNK2. RX PubMed=21309750; DOI=10.1042/bj20102156; RA Chan W., Sit S.T., Manser E.; RT "The Cdc42-associated kinase ACK1 is not auto-inhibited but requires Src RT for activation."; RL Biochem. J. 435:355-364(2011). RN [62] RP PHOSPHORYLATION AT SER-75. RX PubMed=21442427; DOI=10.1007/s00018-011-0638-1; RA Pan Q., Qiao F., Gao C., Norman B., Optican L., Zelenka P.S.; RT "Cdk5 targets active Src for ubiquitin-dependent degradation by RT phosphorylating Src(S75)."; RL Cell. Mol. Life Sci. 68:3425-3436(2011). RN [63] RP INTERACTION WITH PRR7. RX PubMed=21460222; DOI=10.1074/jbc.m110.175117; RA Hrdinka M., Draber P., Stepanek O., Ormsby T., Otahal P., Angelisova P., RA Brdicka T., Paces J., Horejsi V., Drbal K.; RT "PRR7 is a transmembrane adaptor protein expressed in activated T cells RT involved in regulation of T cell receptor signaling and apoptosis."; RL J. Biol. Chem. 286:19617-19629(2011). RN [64] RP FUNCTION IN FOCAL ADHESION DYNAMICS, AND INTERACTION WITH PTK2/FAK1 AND RP DNM2. RX PubMed=21411625; DOI=10.1091/mbc.e10-09-0785; RA Wang Y., Cao H., Chen J., McNiven M.A.; RT "A direct interaction between the large GTPase dynamin-2 and FAK regulates RT focal adhesion dynamics in response to active Src."; RL Mol. Biol. Cell 22:1529-1538(2011). RN [65] RP IDENTIFICATION IN A COMPLEX WITH PTPRA; BCAR1 AND BCAR3, AND SUBCELLULAR RP LOCATION. RX PubMed=22801373; DOI=10.1128/mcb.00214-12; RA Sun G., Cheng S.Y., Chen M., Lim C.J., Pallen C.J.; RT "Protein tyrosine phosphatase alpha phosphotyrosyl-789 binds BCAR3 to RT position Cas for activation at integrin-mediated focal adhesions."; RL Mol. Cell. Biol. 32:3776-3789(2012). RN [66] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-75, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [67] RP FUNCTION IN PHOSPHORYLATION OF BCAR1. RX PubMed=22710723; DOI=10.1038/onc.2012.220; RA Zhang P., Guo A., Possemato A., Wang C., Beard L., Carlin C., RA Markowitz S.D., Polakiewicz R.D., Wang Z.; RT "Identification and functional characterization of p130Cas as a substrate RT of protein tyrosine phosphatase nonreceptor 14."; RL Oncogene 32:2087-2095(2013). RN [68] RP INTERACTION WITH TRAP1. RX PubMed=23564345; DOI=10.1073/pnas.1220659110; RA Yoshida S., Tsutsumi S., Muhlebach G., Sourbier C., Lee M.J., Lee S., RA Vartholomaiou E., Tatokoro M., Beebe K., Miyajima N., Mohney R.P., Chen Y., RA Hasumi H., Xu W., Fukushima H., Nakamura K., Koga F., Kihara K., Trepel J., RA Picard D., Neckers L.; RT "Molecular chaperone TRAP1 regulates a metabolic switch between RT mitochondrial respiration and aerobic glycolysis."; RL Proc. Natl. Acad. Sci. U.S.A. 110:E1604-E1612(2013). RN [69] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [70] RP FUNCTION, PHOSPHORYLATION AT TYR-419, AND 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 [71] RP PHOSPHORYLATION AT TYR-419 AND TYR-530, INVOLVEMENT IN THC6, VARIANT THC6 RP LYS-527, AND CHARACTERIZATION OF VARIANT THC6 LYS-527. RX PubMed=26936507; DOI=10.1126/scitranslmed.aad7666; RG BRIDGE-BPD Consortium; RA Turro E., Greene D., Wijgaerts A., Thys C., Lentaigne C., Bariana T.K., RA Westbury S.K., Kelly A.M., Selleslag D., Stephens J.C., Papadia S., RA Simeoni I., Penkett C.J., Ashford S., Attwood A., Austin S., Bakchoul T., RA Collins P., Deevi S.V., Favier R., Kostadima M., Lambert M.P., Mathias M., RA Millar C.M., Peerlinck K., Perry D.J., Schulman S., Whitehorn D., RA Wittevrongel C., De Maeyer M., Rendon A., Gomez K., Erber W.N., RA Mumford A.D., Nurden P., Stirrups K., Bradley J.R., Raymond F.L., RA Laffan M.A., Van Geet C., Richardson S., Freson K., Ouwehand W.H.; RT "A dominant gain-of-function mutation in universal tyrosine kinase SRC RT causes thrombocytopenia, myelofibrosis, bleeding, and bone pathologies."; RL Sci. Transl. Med. 8:328RA30-328RA30(2016). RN [72] RP INTERACTION WITH P85. RX PubMed=28903391; DOI=10.18632/oncotarget.18973; RA Lu Y., Zheng X., Hu W., Bian S., Zhang Z., Tao D., Liu Y., Ma Y.; RT "Cancer/testis antigen PIWIL2 suppresses circadian rhythms by regulating RT the stability and activity of BMAL1 and CLOCK."; RL Oncotarget 8:54913-54924(2017). RN [73] RP REVIEW ON FUNCTION. RX PubMed=8672527; DOI=10.1016/0304-419x(96)00003-0; RA Brown M.T., Cooper J.A.; RT "Regulation, substrates and functions of src."; RL Biochim. Biophys. Acta 1287:121-149(1996). RN [74] RP REVIEW ON FUNCTION. RX PubMed=9442882; DOI=10.1146/annurev.cellbio.13.1.513; RA Thomas S.M., Brugge J.S.; RT "Cellular functions regulated by Src family kinases."; RL Annu. Rev. Cell Dev. Biol. 13:513-609(1997). RN [75] RP REVIEW ON FUNCTION. RX PubMed=11964124; DOI=10.1007/s00018-002-8438-2; RA Ma Y.C., Huang X.Y.; RT "Novel regulation and function of Src tyrosine kinase."; RL Cell. Mol. Life Sci. 59:456-462(2002). RN [76] RP INTERACTION WITH HCV NON-STRUCTURAL PROTEIN 5A (MICROBIAL INFECTION). RX PubMed=30862675; DOI=10.1074/jbc.ra119.007656; RA Klinker S., Stindt S., Gremer L., Bode J.G., Gertzen C.G.W., Gohlke H., RA Weiergraeber O.H., Hoffmann S., Willbold D.; RT "Phosphorylated tyrosine 93 of hepatitis C virus nonstructural protein 5A RT is essential for interaction with host c-Src and efficient viral RT replication."; RL J. Biol. Chem. 294:7388-7402(2019). RN [77] RP INTERACTION WITH HNRNPA2B1. RX PubMed=31320558; DOI=10.1126/science.aav0758; RA Wang L., Wen M., Cao X.; RT "Nuclear hnRNPA2B1 initiates and amplifies the innate immune response to RT DNA viruses."; RL Science 0:0-0(2019). RN [78] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=35927303; DOI=10.1038/s41418-022-01047-3; RA Seo S.U., Woo S.M., Kim M.W., Lee E.W., Min K.J., Kwon T.K.; RT "Phosphorylation of OTUB1 at Tyr 26 stabilizes the mTORC1 component, RT Raptor."; RL Cell Death Differ. 30:82-93(2023). RN [79] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 86-536. RX PubMed=9024657; DOI=10.1038/385595a0; RA Xu W., Harrison S.C., Eck M.J.; RT "Three-dimensional structure of the tyrosine kinase c-Src."; RL Nature 385:595-602(1997). RN [80] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 145-249. RX PubMed=9174343; DOI=10.1021/bi970019n; RA Charifson P.S., Shewchuk L.M., Rocque W., Hummel C.W., Jordan S.R., RA Mohr C., Pacofsky G.J., Peel M.R., Rodriguez M., Sternbach D.D., RA Consler T.G.; RT "Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and structural RT study."; RL Biochemistry 36:6283-6293(1997). RN [81] RP STRUCTURE BY NMR OF 204-249. RX PubMed=7532003; DOI=10.1021/bi00007a003; RA Xu R.X., Word J.M., Davis D.G., Rink M.J., Willard D.H. Jr., RA Gampe R.T. Jr.; RT "Solution structure of the human pp60c-src SH2 domain complexed with a RT phosphorylated tyrosine pentapeptide."; RL Biochemistry 34:2107-2121(1995). RN [82] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 412-424 IN COMPLEX WITH CBLC, RP UBIQUITINATION, AND INTERACTION WITH CBLC. RX PubMed=22888118; DOI=10.1093/jb/mvs085; RA Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M., RA Yamanashi Y., Yamamoto T., Nakagawa A.; RT "Structural flexibility regulates phosphopeptide-binding activity of the RT tyrosine kinase binding domain of Cbl-c."; RL J. Biochem. 152:487-495(2012). RN [83] RP VARIANT [LARGE SCALE ANALYSIS] THR-237. 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 which is activated CC following engagement of many different classes of cellular receptors CC including immune response receptors, integrins and other adhesion CC receptors, receptor protein tyrosine kinases, G protein-coupled CC receptors as well as cytokine receptors. Participates in signaling CC pathways that control a diverse spectrum of biological activities CC including gene transcription, immune response, cell adhesion, cell CC cycle progression, apoptosis, migration, and transformation. Due to CC functional redundancy between members of the SRC kinase family, CC identification of the specific role of each SRC kinase is very CC difficult. SRC appears to be one of the primary kinases activated CC following engagement of receptors and plays a role in the activation of CC other protein tyrosine kinase (PTK) families. Receptor clustering or CC dimerization leads to recruitment of SRC to the receptor complexes CC where it phosphorylates the tyrosine residues within the receptor CC cytoplasmic domains. Plays an important role in the regulation of CC cytoskeletal organization through phosphorylation of specific CC substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 CC domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal CC reorganization is also controlled through the phosphorylation of CC cortactin (CTTN) (Probable). When cells adhere via focal adhesions to CC the extracellular matrix, signals are transmitted by integrins into the CC cell resulting in tyrosine phosphorylation of a number of focal CC adhesion proteins, including PTK2/FAK1 and paxillin (PXN) CC (PubMed:21411625). In addition to phosphorylating focal adhesion CC proteins, SRC is also active at the sites of cell-cell contact adherens CC junctions and phosphorylates substrates such as beta-catenin (CTNNB1), CC delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell- CC cell junction, the gap junction, is also a target for SRC, which CC phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of CC pre-mRNA-processing and phosphorylates RNA-binding proteins such as CC KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine CC phosphorylation of both STAT1 and STAT3, leading to increased DNA CC binding activity of these transcription factors (By similarity). CC Involved in the RAS pathway through phosphorylation of RASA1 and CC RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium- CC activated chloride channel activation (PubMed:18586953). Required for CC epidermal growth factor receptor (EGFR) internalization through CC phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr- CC 1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization CC through phosphorylation and activation of GRK2, leading to beta- CC arrestin phosphorylation and internalization. Has a critical role in CC the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase CC cascade by epidermal growth factor (Probable). Might be involved not CC only in mediating the transduction of mitogenic signals at the level of CC the plasma membrane but also in controlling progression through the CC cell cycle via interaction with regulatory proteins in the nucleus CC (PubMed:7853507). Plays an important role in osteoclastic bone CC resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC- CC PTK2B/PYK2 complex and SRC kinase activity are necessary for this CC function. Recruited to activated integrins by PTK2B/PYK2, thereby CC phosphorylating CBL, which in turn induces the activation and CC recruitment of phosphatidylinositol 3-kinase to the cell membrane in a CC signaling pathway that is critical for osteoclast function CC (PubMed:8755529, PubMed:14585963). Promotes energy production in CC osteoclasts by activating mitochondrial cytochrome C oxidase CC (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby CC promoting its subsequent autophosphorylation (PubMed:16186108). CC Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' CC and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances RIGI- CC elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at CC 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates CC BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple CC tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 CC activity (PubMed:20525694). Phosphorylates synaptic vesicle protein CC synaptophysin (SYP) (By similarity). Involved in anchorage-independent CC cell growth (PubMed:19307596). Required for podosome formation (By CC similarity). Mediates IL6 signaling by activating YAP1-NOTCH pathway to CC induce inflammation-induced epithelial regeneration (PubMed:25731159). CC Phosphorylates OTUB1, promoting deubiquitination of RPTOR CC (PubMed:35927303). Phosphorylates caspase CASP8 at 'Tyr-380' which CC negatively regulates CASP8 processing and activation, down-regulating CC CASP8 proapoptotic function (PubMed:16619028). CC {ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:Q9WUD9, CC ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:12615910, CC ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:16186108, CC ECO:0000269|PubMed:16619028, ECO:0000269|PubMed:18586953, CC ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:19419966, CC ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20525694, CC ECO:0000269|PubMed:21309750, ECO:0000269|PubMed:21411625, CC ECO:0000269|PubMed:22710723, ECO:0000269|PubMed:25731159, CC ECO:0000269|PubMed:35927303, ECO:0000269|PubMed:7853507, CC ECO:0000269|PubMed:8755529, ECO:0000269|PubMed:8759729, CC ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527, CC ECO:0000305|PubMed:9442882}. CC -!- FUNCTION: [Isoform 1]: Non-receptor protein tyrosine kinase which CC phosphorylates synaptophysin with high affinity. CC {ECO:0000250|UniProtKB:Q9WUD9}. CC -!- FUNCTION: [Isoform 2]: Non-receptor protein tyrosine kinase which shows CC higher basal kinase activity than isoform 1, possibly due to weakened CC intramolecular interactions which enhance autophosphorylation of Tyr- CC 419 and subsequent activation (By similarity). The SH3 domain shows CC reduced affinity with the linker sequence between the SH2 and kinase CC domains which may account for the increased basal activity (By CC similarity). Displays altered substrate specificity compared to isoform CC 1, showing weak affinity for synaptophysin and for peptide substrates CC containing class I or class II SH3 domain-binding motifs (By CC similarity). Plays a role in L1CAM-mediated neurite elongation, CC possibly by acting downstream of L1CAM to drive cytoskeletal CC rearrangements involved in neurite outgrowth (By similarity). CC {ECO:0000250|UniProtKB:Q9WUD9}. CC -!- FUNCTION: [Isoform 3]: Non-receptor protein tyrosine kinase which shows CC higher basal kinase activity than isoform 1, possibly due to weakened CC intramolecular interactions which enhance autophosphorylation of Tyr- CC 419 and subsequent activation (By similarity). The SH3 domain shows CC reduced affinity with the linker sequence between the SH2 and kinase CC domains which may account for the increased basal activity (By CC similarity). Displays altered substrate specificity compared to isoform CC 1, showing weak affinity for synaptophysin and for peptide substrates CC containing class I or class II SH3 domain-binding motifs (By CC similarity). Plays a role in neurite elongation (By similarity). CC {ECO:0000250|UniProtKB:Q9WUD9}. 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 ECO:0000269|PubMed:14632929, ECO:0000269|PubMed:19307596, CC ECO:0000269|PubMed:21036157, ECO:0000269|PubMed:35927303, CC ECO:0000269|PubMed:7929427, ECO:0000269|PubMed:8759729, CC ECO:0000269|PubMed:9571170}; CC -!- CATALYTIC ACTIVITY: [Isoform 1]: 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:0000250|UniProtKB:Q9WUD9}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: 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:0000250|UniProtKB:Q9WUD9}; CC -!- CATALYTIC ACTIVITY: [Isoform 3]: 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:0000250|UniProtKB:Q9WUD9}; CC -!- ACTIVITY REGULATION: Phosphorylation by CSK at Tyr-530 inhibits kinase CC activity. Inhibitory phosphorylation at Tyr-530 is enhanced by heme. CC Further phosphorylation by CDK1 partially reactivates CSK-inactivated CC SRC and facilitates complete reactivation by protein tyrosine CC phosphatase PTPRC. Integrin engagement stimulates kinase activity. CC Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and CC pseudosubstrate-based peptide inhibitors like CIYKYYF act as CC inhibitors. Phosphorylation at Tyr-419 increases kinase activity. CC {ECO:0000269|PubMed:14632929, ECO:0000269|PubMed:21036157, CC ECO:0000269|PubMed:7929427, ECO:0000269|PubMed:8759729, CC ECO:0000269|PubMed:9571170}. CC -!- SUBUNIT: Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 CC domain) and SRC; the formation of the complex is dependent on integrin CC mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373). Interacts CC with DDEF1/ASAP1; via the SH3 domain (By similarity). Interacts with CC CCPG1 (By similarity). Identified in a complex containing FGFR4, NCAM1, CC CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN (By similarity). Interacts CC with ERBB2, STAT1 and PNN (By similarity). Interacts with DDR1, DDR2 CC and DAB2 (By similarity). Interacts with CDCP1, TGFB1I1 and TOM1L2 CC (PubMed:15851033, PubMed:16479011, PubMed:17202804). Interacts with the CC cytoplasmic domain of MUC1, phosphorylates it and increases binding of CC MUC1 with beta-catenin (PubMed:11152665). Interacts with RALGPS1; via CC the SH3 domain (PubMed:10747847). Interacts with CAV2 (tyrosine CC phosphorylated form) (PubMed:12091389, PubMed:15504032). Interacts (via CC the SH3 domain and the protein kinase domain) with ARRB1; the CC interaction is independent of the phosphorylation state of SRC C- CC terminus (By similarity). Interacts with ARRB1 and ARRB2 CC (PubMed:10753943, PubMed:9924018). Interacts with SRCIN1 CC (PubMed:17525734). Interacts with NDFIP2 and more weakly with NDFIP1 CC (PubMed:20534535). Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and CC ESR1 (dimethylated on arginine) (PubMed:18657504, PubMed:21411625). CC Interacts with FASLG (PubMed:19807924). Interacts (via SH2 domain) with CC the 'Tyr-402' phosphorylated form of PTK2B/PYK2 (PubMed:14585963). CC Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated) (By CC similarity). Interacts with PDGFRA (tyrosine phosphorylated) (By CC similarity). Interacts with CSF1R (By similarity). Interacts (via SH2 CC and SH3 domain) with TNK2 (PubMed:21309750). Interacts (via protein CC kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt CC domain) (PubMed:20100835). Interacts with TRAF3 (via RING-type zinc CC finger domain) (PubMed:19419966). Interacts with RIGI, MAVS and TBK1 CC (PubMed:19419966). Interacts (via SH2 domain) with RACK1; the CC interaction is enhanced by tyrosine phosphorylation of RACK1 and CC inhibits SRC activity (PubMed:9584165, PubMed:11279199). Interacts with CC EPHB1; activates the MAPK/ERK cascade to regulate cell migration CC (PubMed:12925710). Interacts with FCAMR (PubMed:8759729). Interacts CC (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1 CC (PubMed:18024423). Interacts with AMOTL2; this interaction regulates CC the translocation of phosphorylated SRC to peripheral cell-matrix CC adhesion sites (PubMed:17293535). Interacts with TRAP1 CC (PubMed:23564345). Interacts with CBLC; the interaction is enhanced CC when SRC is phosphorylated at Tyr-419 (PubMed:14661060, CC PubMed:22888118). Interacts with ARHGEF5 (By similarity). Interacts CC (via cytoplasmic domain) with CEACAM1 (via SH2 domain); this CC interaction is regulated by trans-homophilic cell adhesion CC (PubMed:7478590). Interacts with MPP2 (PubMed:19665017). Interacts with CC PRR7 (PubMed:21460222). Interacts (via kinase domain and to a lesser CC extent the SH2 domain) directly with PDLIM4; this interaction results CC in PTPN13-mediated dephosphorylation of this protein leading to its CC inactivation (PubMed:19307596). Interacts with P85 (PIK3R1 or PIK3R2) CC (PubMed:28903391). Interacts with HNRNPA2B1 (PubMed:31320558). CC Interacts with IL6ST/gp130 (PubMed:25731159). Interacts (via SH3 CC domain) with PELP1 in the presence of 17-beta-estradiol. Interacts with CC AMBRA1 (By similarity). {ECO:0000250|UniProtKB:P05480, CC ECO:0000250|UniProtKB:Q9WUD9, ECO:0000269|PubMed:10747847, CC ECO:0000269|PubMed:10753943, ECO:0000269|PubMed:11152665, CC ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12091389, CC ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:14585963, CC ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:14963108, CC ECO:0000269|PubMed:15504032, ECO:0000269|PubMed:15851033, CC ECO:0000269|PubMed:16479011, ECO:0000269|PubMed:17202804, CC ECO:0000269|PubMed:17293535, ECO:0000269|PubMed:17525734, CC ECO:0000269|PubMed:18024423, ECO:0000269|PubMed:18657504, CC ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:19419966, CC ECO:0000269|PubMed:19665017, ECO:0000269|PubMed:19807924, CC ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20534535, CC ECO:0000269|PubMed:21309750, ECO:0000269|PubMed:21411625, CC ECO:0000269|PubMed:22801373, ECO:0000269|PubMed:22888118, CC ECO:0000269|PubMed:23564345, ECO:0000269|PubMed:25731159, CC ECO:0000269|PubMed:28903391, ECO:0000269|PubMed:31320558, CC ECO:0000269|PubMed:7478590, ECO:0000269|PubMed:8759729, CC ECO:0000269|PubMed:9584165, ECO:0000269|PubMed:9924018}. CC -!- SUBUNIT: (Microbial infection) Interacts with HEV ORF3 protein; via the CC SH3 domain. {ECO:0000269|PubMed:11518702}. CC -!- SUBUNIT: (Microbial infection) Interacts (via SH2 domain) with HCV non- CC structural protein 5A (via N-terminus). {ECO:0000269|PubMed:30862675}. CC -!- INTERACTION: CC P12931; P00519: ABL1; NbExp=2; IntAct=EBI-621482, EBI-375543; CC P12931; P42684: ABL2; NbExp=2; IntAct=EBI-621482, EBI-1102694; CC P12931; P12814: ACTN1; NbExp=2; IntAct=EBI-621482, EBI-351710; CC P12931; O14672: ADAM10; NbExp=3; IntAct=EBI-621482, EBI-1536151; CC P12931; O43184: ADAM12; NbExp=2; IntAct=EBI-621482, EBI-2625825; CC P12931; Q13444: ADAM15; NbExp=4; IntAct=EBI-621482, EBI-77818; CC P12931; P07550: ADRB2; NbExp=3; IntAct=EBI-621482, EBI-491169; CC P12931; P55196: AFDN; NbExp=7; IntAct=EBI-621482, EBI-365875; CC P12931; P10275: AR; NbExp=7; IntAct=EBI-621482, EBI-608057; CC P12931; P49407: ARRB1; NbExp=3; IntAct=EBI-621482, EBI-743313; CC P12931; P32121: ARRB2; NbExp=2; IntAct=EBI-621482, EBI-714559; CC P12931; Q9ULH1: ASAP1; NbExp=3; IntAct=EBI-621482, EBI-346622; CC P12931; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-621482, EBI-10254793; CC P12931; P56945: BCAR1; NbExp=3; IntAct=EBI-621482, EBI-702093; CC P12931; Q14457: BECN1; NbExp=3; IntAct=EBI-621482, EBI-949378; CC P12931; P22681: CBL; NbExp=8; IntAct=EBI-621482, EBI-518228; CC P12931; Q16543: CDC37; NbExp=5; IntAct=EBI-621482, EBI-295634; CC P12931; Q9H5V8: CDCP1; NbExp=3; IntAct=EBI-621482, EBI-1019736; CC P12931; P12830: CDH1; NbExp=2; IntAct=EBI-621482, EBI-727477; CC P12931; P68400: CSNK2A1; NbExp=2; IntAct=EBI-621482, EBI-347804; CC P12931; P35222: CTNNB1; NbExp=2; IntAct=EBI-621482, EBI-491549; CC P12931; P00533: EGFR; NbExp=9; IntAct=EBI-621482, EBI-297353; CC P12931; P04626: ERBB2; NbExp=11; IntAct=EBI-621482, EBI-641062; CC P12931; P21860: ERBB3; NbExp=2; IntAct=EBI-621482, EBI-720706; CC P12931; P03372: ESR1; NbExp=12; IntAct=EBI-621482, EBI-78473; CC P12931; P03372-4: ESR1; NbExp=2; IntAct=EBI-621482, EBI-4309277; CC P12931; P14921-1: ETS1; NbExp=2; IntAct=EBI-621482, EBI-913224; CC P12931; P25445: FAS; NbExp=2; IntAct=EBI-621482, EBI-494743; CC P12931; Q8NFZ0: FBH1; NbExp=4; IntAct=EBI-621482, EBI-724767; CC P12931; P06241: FYN; NbExp=3; IntAct=EBI-621482, EBI-515315; CC P12931; Q13480: GAB1; NbExp=12; IntAct=EBI-621482, EBI-517684; CC P12931; Q13322-4: GRB10; NbExp=3; IntAct=EBI-621482, EBI-12353035; CC P12931; P19367: HK1; NbExp=2; IntAct=EBI-621482, EBI-713162; CC P12931; P61978: HNRNPK; NbExp=6; IntAct=EBI-621482, EBI-304185; CC P12931; P07900: HSP90AA1; NbExp=3; IntAct=EBI-621482, EBI-296047; CC P12931; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-621482, EBI-81279; CC P12931; P35968: KDR; NbExp=6; IntAct=EBI-621482, EBI-1005487; CC P12931; Q07666: KHDRBS1; NbExp=3; IntAct=EBI-621482, EBI-1364; CC P12931; P10721: KIT; NbExp=5; IntAct=EBI-621482, EBI-1379503; CC P12931; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-621482, EBI-2796400; CC P12931; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-621482, EBI-739832; CC P12931; Q14693: LPIN1; NbExp=3; IntAct=EBI-621482, EBI-5278370; CC P12931; P07948: LYN; NbExp=4; IntAct=EBI-621482, EBI-79452; CC P12931; Q9H204: MED28; NbExp=3; IntAct=EBI-621482, EBI-514199; CC P12931; P08581: MET; NbExp=7; IntAct=EBI-621482, EBI-1039152; CC P12931; Q13177: PAK2; NbExp=2; IntAct=EBI-621482, EBI-1045887; CC P12931; P16284: PECAM1; NbExp=3; IntAct=EBI-621482, EBI-716404; CC P12931; P27986: PIK3R1; NbExp=7; IntAct=EBI-621482, EBI-79464; CC P12931; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-621482, EBI-9090282; CC P12931; Q92569: PIK3R3; NbExp=3; IntAct=EBI-621482, EBI-79893; CC P12931; Q05397: PTK2; NbExp=9; IntAct=EBI-621482, EBI-702142; CC P12931; Q14289: PTK2B; NbExp=3; IntAct=EBI-621482, EBI-298640; CC P12931; P18031: PTPN1; NbExp=14; IntAct=EBI-621482, EBI-968788; CC P12931; Q16825: PTPN21; NbExp=2; IntAct=EBI-621482, EBI-2860264; CC P12931; P18433: PTPRA; NbExp=4; IntAct=EBI-621482, EBI-2609645; CC P12931; Q15907: RAB11B; NbExp=3; IntAct=EBI-621482, EBI-722234; CC P12931; Q13905: RAPGEF1; NbExp=2; IntAct=EBI-621482, EBI-976876; CC P12931; Q01973: ROR1; NbExp=9; IntAct=EBI-621482, EBI-6082337; CC P12931; P27635: RPL10; NbExp=6; IntAct=EBI-621482, EBI-352398; CC P12931; O00560: SDCBP; NbExp=2; IntAct=EBI-621482, EBI-727004; CC P12931; O60880: SH2D1A; NbExp=3; IntAct=EBI-621482, EBI-6983382; CC P12931; O14796: SH2D1B; NbExp=3; IntAct=EBI-621482, EBI-3923013; CC P12931; P35326: SPRR2A; NbExp=3; IntAct=EBI-621482, EBI-1047940; CC P12931; Q9C0H9: SRCIN1; NbExp=3; IntAct=EBI-621482, EBI-1393949; CC P12931; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-621482, EBI-2505861; CC P12931; Q68CZ2: TNS3; NbExp=13; IntAct=EBI-621482, EBI-1220488; CC P12931; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-621482, EBI-749023; CC P12931; Q8R5G7: Arap3; Xeno; NbExp=3; IntAct=EBI-621482, EBI-621463; CC P12931; P52800: Efnb2; Xeno; NbExp=2; IntAct=EBI-621482, EBI-1032676; CC P12931; P97288: Htr4; Xeno; NbExp=2; IntAct=EBI-621482, EBI-7149283; CC P12931; P34152: Ptk2; Xeno; NbExp=2; IntAct=EBI-621482, EBI-77070; CC P12931; P18052: Ptpra; Xeno; NbExp=3; IntAct=EBI-621482, EBI-6597520; CC P12931; Q62884; Xeno; NbExp=3; IntAct=EBI-621482, EBI-7459400; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7525268}; CC Lipid-anchor {ECO:0000269|PubMed:22801373}. Mitochondrion inner CC membrane {ECO:0000269|PubMed:12615910}. Nucleus CC {ECO:0000269|PubMed:7853507}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:7525268}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:19307596}. Cell junction, focal adhesion CC {ECO:0000269|PubMed:22801373}. Note=Localizes to focal adhesion sites CC following integrin engagement (PubMed:22801373). Localization to focal CC adhesion sites requires myristoylation and the SH3 domain CC (PubMed:7525268). Colocalizes with PDLIM4 at the perinuclear region, CC but not at focal adhesions (PubMed:19307596). CC {ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:22801373, CC ECO:0000269|PubMed:7525268}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=c-src {ECO:0000303|PubMed:8319227}; CC IsoId=P12931-1; Sequence=Displayed; CC Name=2; Synonyms=c-srcN1 {ECO:0000303|PubMed:8319227}, N1-Src CC {ECO:0000250|UniProtKB:Q9WUD9}; CC IsoId=P12931-2; Sequence=VSP_012134; CC Name=3; Synonyms=c-srcN2 {ECO:0000303|PubMed:8319227}, N2-Src CC {ECO:0000250|UniProtKB:Q9WUD9}; CC IsoId=P12931-3; Sequence=VSP_061494; CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. Platelets, neurons and CC osteoclasts express 5-fold to 200-fold higher levels than most other CC tissues. CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in spleen and liver. CC {ECO:0000269|PubMed:8319227}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in brain. CC {ECO:0000269|PubMed:8319227}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in brain. CC {ECO:0000269|PubMed:8319227}. CC -!- DEVELOPMENTAL STAGE: [Isoform 1]: Expressed at higher levels in fetal CC liver than in adult liver. {ECO:0000269|PubMed:1691439}. CC -!- DEVELOPMENTAL STAGE: [Isoform 2]: Expressed at higher levels in fetal CC brain than in adult brain. {ECO:0000269|PubMed:1691439}. CC -!- DEVELOPMENTAL STAGE: [Isoform 3]: Expressed at similar levels in adult CC and fetal brain. {ECO:0000269|PubMed:1691439}. CC -!- DOMAIN: The SH2 and SH3 domains are important for the intramolecular CC and intermolecular interactions that regulate catalytic activity, CC localization, and substrate recruitment. CC -!- PTM: Myristoylated at Gly-2, and this is essential for targeting to CC membranes. {ECO:0000269|PubMed:7525268}. CC -!- PTM: Dephosphorylated at Tyr-530 by PTPRJ (By similarity). CC Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated CC form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-419. CC Normally maintained in an inactive conformation with the SH2 domain CC engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase CC linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a CC result of protein tyrosine phosphatase (PTP) action disrupts the CC intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 CC can then become autophosphorylated, resulting in SRC activation. CC Phosphorylation of Tyr-530 by CSK allows this interaction to reform, CC resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 CC targets SRC to ubiquitin-dependent degradation and thus leads to CC cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances CC kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase CC activity. Upon activation of IL6ST by IL6, Tyr-419 is phosphorylated CC and Tyr-530 dephosphorylated (PubMed:25731159). {ECO:0000250, CC ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18936167, CC ECO:0000269|PubMed:21442427, ECO:0000269|PubMed:22888118, CC ECO:0000269|PubMed:25731159, ECO:0000269|PubMed:6273838, CC ECO:0000269|PubMed:7525268}. CC -!- PTM: [Isoform 1]: Displays reduced levels of autophosphorylation at CC Tyr-419 compared to isoforms 2 and 3. {ECO:0000250|UniProtKB:Q9WUD9}. CC -!- PTM: [Isoform 2]: Displays enhanced levels of autophosphorylation at CC Tyr-419 compared to isoform 1. {ECO:0000250|UniProtKB:Q9WUD9}. CC -!- PTM: [Isoform 3]: Displays enhanced levels of autophosphorylation at CC Tyr-419 compared to isoform 1 (By similarity). Shows reduced CC phosphorylation at Tyr-527 compared to isoforms 1 and 2 (By CC similarity). {ECO:0000250|UniProtKB:Q9WUD9}. CC -!- PTM: S-nitrosylation is important for activation of its kinase CC activity. {ECO:0000250}. CC -!- PTM: Ubiquitinated in response to CDK5-mediated phosphorylation. CC Ubiquitination mediated by CBLC requires SRC autophosphorylation at CC Tyr-419 and may lead to lysosomal degradation. CC {ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18936167, CC ECO:0000269|PubMed:22888118, ECO:0000269|PubMed:6273838}. CC -!- DISEASE: Note=SRC kinase activity has been shown to be increased in CC several tumor tissues and tumor cell lines such as colon carcinoma CC cells. {ECO:0000269|PubMed:2498394, ECO:0000269|PubMed:3093483}. CC -!- DISEASE: Thrombocytopenia 6 (THC6) [MIM:616937]: A form of CC thrombocytopenia, a hematologic disorder defined by a decrease in the CC number of platelets in circulating blood, resulting in the potential CC for increased bleeding and decreased ability for clotting. THC6 is an CC autosomal dominant form. Affected individuals may also have bone CC abnormalities and an increased risk for myelofibrosis. CC {ECO:0000269|PubMed:26936507}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/448/SRC"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL133293; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW76065.1; -; Genomic_DNA. DR EMBL; CH471077; EAW76064.1; -; Genomic_DNA. DR EMBL; CH471077; EAW76066.1; -; Genomic_DNA. DR EMBL; CH471077; EAW76067.1; -; Genomic_DNA. DR EMBL; BC011566; AAH11566.1; -; mRNA. DR EMBL; BC051270; AAH51270.2; -; mRNA. DR EMBL; K03218; AAA60584.1; -; Genomic_DNA. DR EMBL; M16237; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; M16243; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; M16244; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; M16245; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; K03212; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; K03213; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; K03214; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; K03215; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; K03216; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; K03217; AAA60584.1; JOINED; Genomic_DNA. DR EMBL; X02647; CAA26485.1; -; Genomic_DNA. DR EMBL; X03995; CAA26485.1; JOINED; Genomic_DNA. DR EMBL; X03996; CAA26485.1; JOINED; Genomic_DNA. DR EMBL; X03997; CAA26485.1; JOINED; Genomic_DNA. DR EMBL; X03998; CAA26485.1; JOINED; Genomic_DNA. DR EMBL; X03999; CAA26485.1; JOINED; Genomic_DNA. DR EMBL; X04000; CAA26485.1; JOINED; Genomic_DNA. DR CCDS; CCDS13294.1; -. [P12931-1] DR PIR; A26891; TVHUSC. DR RefSeq; NP_005408.1; NM_005417.4. [P12931-1] DR RefSeq; NP_938033.1; NM_198291.2. [P12931-1] DR RefSeq; XP_011527315.1; XM_011529013.2. DR RefSeq; XP_016883513.1; XM_017028024.1. DR RefSeq; XP_016883514.1; XM_017028025.1. DR RefSeq; XP_016883515.1; XM_017028026.1. [P12931-2] DR RefSeq; XP_016883516.1; XM_017028027.1. DR PDB; 1A07; X-ray; 2.20 A; A/B=144-249. DR PDB; 1A08; X-ray; 2.20 A; A/B=144-249. DR PDB; 1A09; X-ray; 2.00 A; A/B=144-249. DR PDB; 1A1A; X-ray; 2.00 A; A/B=144-249. DR PDB; 1A1B; X-ray; 2.20 A; A/B=144-249. DR PDB; 1A1C; X-ray; 2.40 A; A/B=144-249. DR PDB; 1A1E; X-ray; 2.20 A; A/B=144-249. DR PDB; 1FMK; X-ray; 1.50 A; A=86-536. DR PDB; 1HCS; NMR; -; B=144-249. DR PDB; 1HCT; NMR; -; B=144-249. DR PDB; 1KSW; X-ray; 2.80 A; A=86-536. DR PDB; 1O41; X-ray; 1.70 A; A=145-252. DR PDB; 1O42; X-ray; 1.70 A; A=145-252. DR PDB; 1O43; X-ray; 1.50 A; A=145-252. DR PDB; 1O44; X-ray; 1.70 A; A=145-252. DR PDB; 1O45; X-ray; 1.80 A; A=145-252. DR PDB; 1O46; X-ray; 2.00 A; A=145-252. DR PDB; 1O47; X-ray; 1.80 A; A=145-252. DR PDB; 1O48; X-ray; 1.55 A; A=145-252. DR PDB; 1O49; X-ray; 1.70 A; A=145-252. DR PDB; 1O4A; X-ray; 1.50 A; A=145-252. DR PDB; 1O4B; X-ray; 1.85 A; A=145-252. DR PDB; 1O4C; X-ray; 1.80 A; A=145-252. DR PDB; 1O4D; X-ray; 1.85 A; A=145-252. DR PDB; 1O4E; X-ray; 2.00 A; A=145-252. DR PDB; 1O4F; X-ray; 2.00 A; A=145-252. DR PDB; 1O4G; X-ray; 1.55 A; A=145-252. DR PDB; 1O4H; X-ray; 2.25 A; A=145-252. DR PDB; 1O4I; X-ray; 1.75 A; A=145-252. DR PDB; 1O4J; X-ray; 1.70 A; A=145-252. DR PDB; 1O4K; X-ray; 1.57 A; A=145-252. DR PDB; 1O4L; X-ray; 1.65 A; A=145-252. DR PDB; 1O4M; X-ray; 1.60 A; A=145-252. DR PDB; 1O4N; X-ray; 1.60 A; A=145-252. DR PDB; 1O4O; X-ray; 1.70 A; A=145-252. DR PDB; 1O4P; X-ray; 1.90 A; A=145-252. DR PDB; 1O4Q; X-ray; 1.70 A; A=145-252. DR PDB; 1O4R; X-ray; 1.50 A; A=145-252. DR PDB; 1SHD; X-ray; 2.00 A; A=144-249. DR PDB; 1Y57; X-ray; 1.91 A; A=86-536. DR PDB; 1YI6; X-ray; 2.00 A; A/B=261-536. DR PDB; 1YOJ; X-ray; 1.95 A; A/B=254-536. DR PDB; 1YOL; X-ray; 2.30 A; A/B=254-536. DR PDB; 1YOM; X-ray; 2.90 A; A/B=254-536. DR PDB; 2BDF; X-ray; 2.10 A; A/B=258-536. DR PDB; 2BDJ; X-ray; 2.50 A; A=258-536. DR PDB; 2H8H; X-ray; 2.20 A; A=2-536. DR PDB; 2SRC; X-ray; 1.50 A; A=86-536. DR PDB; 3VRO; X-ray; 1.80 A; B=412-424. DR PDB; 3ZMP; X-ray; 2.62 A; C/D=527-536. DR PDB; 3ZMQ; X-ray; 3.30 A; C=527-536. DR PDB; 4F59; X-ray; 1.71 A; A=144-252. DR PDB; 4F5A; X-ray; 1.80 A; A=144-252. DR PDB; 4F5B; X-ray; 1.57 A; A=144-252. DR PDB; 4HXJ; X-ray; 2.00 A; A/B=87-144. DR PDB; 4K11; X-ray; 2.30 A; A=87-534. DR PDB; 4MXO; X-ray; 2.10 A; A/B=254-536. DR PDB; 4MXX; X-ray; 2.60 A; A/B=254-536. DR PDB; 4MXY; X-ray; 2.58 A; A/B=254-536. DR PDB; 4MXZ; X-ray; 2.58 A; A/B=254-536. DR PDB; 6ATE; X-ray; 2.40 A; A=254-536. DR PDB; 6C4S; X-ray; 1.50 A; A/B=87-144. DR PDB; 6E6E; X-ray; 2.15 A; A/B/C/D/E/F/G/H=261-536. DR PDB; 6EHJ; X-ray; 2.10 A; D/F=2-9. DR PDB; 7NG7; X-ray; 1.50 A; A=254-536. DR PDB; 7OTE; X-ray; 2.49 A; A/B=254-536. DR PDB; 7T1U; X-ray; 2.65 A; A/B=147-251. DR PDB; 7YQE; X-ray; 3.50 A; A/B=85-247. DR PDB; 8HAQ; X-ray; 2.27 A; A/B=260-536. DR PDBsum; 1A07; -. DR PDBsum; 1A08; -. DR PDBsum; 1A09; -. DR PDBsum; 1A1A; -. DR PDBsum; 1A1B; -. DR PDBsum; 1A1C; -. DR PDBsum; 1A1E; -. DR PDBsum; 1FMK; -. DR PDBsum; 1HCS; -. DR PDBsum; 1HCT; -. DR PDBsum; 1KSW; -. DR PDBsum; 1O41; -. DR PDBsum; 1O42; -. DR PDBsum; 1O43; -. DR PDBsum; 1O44; -. DR PDBsum; 1O45; -. DR PDBsum; 1O46; -. DR PDBsum; 1O47; -. DR PDBsum; 1O48; -. DR PDBsum; 1O49; -. DR PDBsum; 1O4A; -. DR PDBsum; 1O4B; -. DR PDBsum; 1O4C; -. DR PDBsum; 1O4D; -. DR PDBsum; 1O4E; -. DR PDBsum; 1O4F; -. DR PDBsum; 1O4G; -. DR PDBsum; 1O4H; -. DR PDBsum; 1O4I; -. DR PDBsum; 1O4J; -. DR PDBsum; 1O4K; -. DR PDBsum; 1O4L; -. DR PDBsum; 1O4M; -. DR PDBsum; 1O4N; -. DR PDBsum; 1O4O; -. DR PDBsum; 1O4P; -. DR PDBsum; 1O4Q; -. DR PDBsum; 1O4R; -. DR PDBsum; 1SHD; -. DR PDBsum; 1Y57; -. DR PDBsum; 1YI6; -. DR PDBsum; 1YOJ; -. DR PDBsum; 1YOL; -. DR PDBsum; 1YOM; -. DR PDBsum; 2BDF; -. DR PDBsum; 2BDJ; -. DR PDBsum; 2H8H; -. DR PDBsum; 2SRC; -. DR PDBsum; 3VRO; -. DR PDBsum; 3ZMP; -. DR PDBsum; 3ZMQ; -. DR PDBsum; 4F59; -. DR PDBsum; 4F5A; -. DR PDBsum; 4F5B; -. DR PDBsum; 4HXJ; -. DR PDBsum; 4K11; -. DR PDBsum; 4MXO; -. DR PDBsum; 4MXX; -. DR PDBsum; 4MXY; -. DR PDBsum; 4MXZ; -. DR PDBsum; 6ATE; -. DR PDBsum; 6C4S; -. DR PDBsum; 6E6E; -. DR PDBsum; 6EHJ; -. DR PDBsum; 7NG7; -. DR PDBsum; 7OTE; -. DR PDBsum; 7T1U; -. DR PDBsum; 7YQE; -. DR PDBsum; 8HAQ; -. DR AlphaFoldDB; P12931; -. DR BMRB; P12931; -. DR SASBDB; P12931; -. DR SMR; P12931; -. DR BioGRID; 112592; 582. DR CORUM; P12931; -. DR DIP; DIP-1059N; -. DR ELM; P12931; -. DR IntAct; P12931; 392. DR MINT; P12931; -. DR STRING; 9606.ENSP00000362680; -. DR BindingDB; P12931; -. DR ChEMBL; CHEMBL267; -. DR DrugBank; DB08564; (2E)-N-{4-[(3-bromophenyl)amino]quinazolin-6-yl}-4-(dimethylamino)but-2-enamide. DR DrugBank; DB08054; 1-(1-methylethyl)-3-quinolin-6-yl-1H-pyrazolo[3,4-d]pyrimidin-4-amine. DR DrugBank; DB06882; 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-naphthalen-1-ylurea. DR DrugBank; DB06883; 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-phenylurea. DR DrugBank; DB08053; 1-cyclobutyl-3-(3,4-dimethoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine. DR DrugBank; DB03023; 1-Tert-Butyl-3-(4-Chloro-Phenyl)-1h-Pyrazolo[3,4-D]Pyrimidin-4-Ylamine. DR DrugBank; DB08192; 2-(4-CARCOXY-5-ISOPROPYLTHIAZOLYL)BENZOPIPERIDINE. DR DrugBank; DB03104; 2-[4-[(Z)-2-Acetamido-3-oxo-3-[[(3S)-2-oxo-1-[(4-phenylphenyl)methyl]azepan-3-yl]amino]prop-1-enyl]-2-formylphenyl]acetic acid. DR DrugBank; DB07335; 3-[4-AMINO-1-(1-METHYLETHYL)-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL]PHENOL. DR DrugBank; DB04739; 4-[(4-METHYL-1-PIPERAZINYL)METHYL]-N-[3-[[4-(3-PYRIDINYL)-2-PYRIMIDINYL]AMINO]PHENYL]-BENZAMIDE. DR DrugBank; DB07966; [4-({4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]quinazolin-2-yl}amino)phenyl]acetonitrile. DR DrugBank; DB06616; Bosutinib. DR DrugBank; DB04272; Citric acid. DR DrugBank; DB01254; Dasatinib. DR DrugBank; DB03217; DPI59. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB03628; ISO24. DR DrugBank; DB02175; Malonic acid. DR DrugBank; DB08462; N-(4-PHENYLAMINO-QUINAZOLIN-6-YL)-ACRYLAMIDE. DR DrugBank; DB01893; N6-Benzyl Adenosine-5'-Diphosphate. DR DrugBank; DB09079; Nintedanib. DR DrugBank; DB03902; Oxalic Acid. DR DrugBank; DB04495; Paratoulene phosphate. DR DrugBank; DB03114; PAS219. DR DrugBank; DB03078; PASBN. DR DrugBank; DB07662; PD-168393. DR DrugBank; DB03298; Phenylphosphate. DR DrugBank; DB01962; Phosphonotyrosine. DR DrugBank; DB08901; Ponatinib. DR DrugBank; DB08052; PP-121. DR DrugBank; DB04751; Purvalanol A. DR DrugBank; DB04080; RU78191. DR DrugBank; DB01947; RU78262. DR DrugBank; DB03828; RU78299. DR DrugBank; DB03306; RU78300. DR DrugBank; DB02908; RU78783. DR DrugBank; DB02762; RU79072. DR DrugBank; DB03525; RU79073. DR DrugBank; DB01866; RU79256. DR DrugBank; DB03268; RU82197. DR DrugBank; DB03591; RU82209. DR DrugBank; DB02336; RU83876. DR DrugBank; DB01678; RU84687. DR DrugBank; DB03712; RU85053. DR DrugBank; DB01908; RU85493. DR DrugBank; DB02432; RU90395. DR DrugBank; DB06137; Tirbanibulin. DR DrugBank; DB05184; XL228. DR DrugCentral; P12931; -. DR GuidetoPHARMACOLOGY; 2206; -. DR MoonDB; P12931; Predicted. DR TCDB; 8.A.23.1.12; the basigin (basigin) family. DR GlyGen; P12931; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P12931; -. DR PhosphoSitePlus; P12931; -. DR SwissPalm; P12931; -. DR BioMuta; SRC; -. DR DMDM; 125711; -. DR OGP; P12931; -. DR CPTAC; CPTAC-3071; -. DR CPTAC; CPTAC-3072; -. DR CPTAC; CPTAC-905; -. DR EPD; P12931; -. DR jPOST; P12931; -. DR MassIVE; P12931; -. DR MaxQB; P12931; -. DR PaxDb; 9606-ENSP00000362680; -. DR PeptideAtlas; P12931; -. DR ProteomicsDB; 52884; -. [P12931-1] DR ProteomicsDB; 52885; -. [P12931-2] DR Pumba; P12931; -. DR ABCD; P12931; 8 sequenced antibodies. DR Antibodypedia; 3409; 2335 antibodies from 47 providers. DR DNASU; 6714; -. DR Ensembl; ENST00000358208.9; ENSP00000350941.5; ENSG00000197122.13. [P12931-3] DR Ensembl; ENST00000373558.2; ENSP00000362659.2; ENSG00000197122.13. [P12931-2] DR Ensembl; ENST00000373567.6; ENSP00000362668.2; ENSG00000197122.13. [P12931-1] DR Ensembl; ENST00000373578.7; ENSP00000362680.2; ENSG00000197122.13. [P12931-1] DR Ensembl; ENST00000692112.1; ENSP00000508666.1; ENSG00000197122.13. [P12931-1] DR Ensembl; ENST00000692423.1; ENSP00000509325.1; ENSG00000197122.13. [P12931-1] DR Ensembl; ENST00000709392.1; ENSP00000517666.1; ENSG00000291971.1. [P12931-1] DR Ensembl; ENST00000709394.1; ENSP00000517668.1; ENSG00000291971.1. [P12931-1] DR Ensembl; ENST00000709395.1; ENSP00000517669.1; ENSG00000291971.1. [P12931-1] DR Ensembl; ENST00000709396.1; ENSP00000517670.1; ENSG00000291971.1. [P12931-1] DR Ensembl; ENST00000709397.1; ENSP00000517671.1; ENSG00000291971.1. [P12931-2] DR Ensembl; ENST00000709398.1; ENSP00000517672.1; ENSG00000291971.1. [P12931-3] DR GeneID; 6714; -. DR KEGG; hsa:6714; -. DR MANE-Select; ENST00000373578.7; ENSP00000362680.2; NM_198291.3; NP_938033.1. DR UCSC; uc002xgy.5; human. [P12931-1] DR AGR; HGNC:11283; -. DR CTD; 6714; -. DR DisGeNET; 6714; -. DR GeneCards; SRC; -. DR HGNC; HGNC:11283; SRC. DR HPA; ENSG00000197122; Low tissue specificity. DR MalaCards; SRC; -. DR MIM; 190090; gene. DR MIM; 616937; phenotype. DR neXtProt; NX_P12931; -. DR OpenTargets; ENSG00000197122; -. DR Orphanet; 480851; Hereditary thrombocytopenia with early-onset myelofibrosis. DR PharmGKB; PA36111; -. DR VEuPathDB; HostDB:ENSG00000197122; -. DR eggNOG; KOG0197; Eukaryota. DR GeneTree; ENSGT00940000158250; -. DR HOGENOM; CLU_000288_7_2_1; -. DR InParanoid; P12931; -. DR OMA; NYIAPVK; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P12931; -. DR TreeFam; TF351634; -. DR BioCyc; MetaCyc:HS02256-MONOMER; -. DR BRENDA; 2.7.10.2; 2681. DR PathwayCommons; P12931; -. DR Reactome; R-HSA-1227986; Signaling by ERBB2. DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4. DR Reactome; R-HSA-1253288; Downregulation of ERBB4 signaling. DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling. DR Reactome; R-HSA-1295596; Spry regulation of FGF signaling. [P12931-1] DR Reactome; R-HSA-1433557; Signaling by SCF-KIT. [P12931-1] DR Reactome; R-HSA-1433559; Regulation of KIT signaling. [P12931-1] DR Reactome; R-HSA-171007; p38MAPK events. [P12931-1] DR Reactome; R-HSA-177929; Signaling by EGFR. [P12931-1] DR Reactome; R-HSA-180292; GAB1 signalosome. DR Reactome; R-HSA-186763; Downstream signal transduction. DR Reactome; R-HSA-191650; Regulation of gap junction activity. [P12931-2] DR Reactome; R-HSA-201556; Signaling by ALK. [P12931-1] DR Reactome; R-HSA-2029481; FCGR activation. [P12931-1] DR Reactome; R-HSA-210990; PECAM1 interactions. [P12931-1] DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer. DR Reactome; R-HSA-2682334; EPH-Ephrin signaling. [P12931-1] DR Reactome; R-HSA-354192; Integrin signaling. DR Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins. DR Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins. DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth. [P12931-1] DR Reactome; R-HSA-389356; CD28 co-stimulation. [P12931-1] DR Reactome; R-HSA-389513; CTLA4 inhibitory signaling. [P12931-1] DR Reactome; R-HSA-391160; Signal regulatory protein family interactions. [P12931-1] DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling. [P12931-1] DR Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse. [P12931-1] DR Reactome; R-HSA-3928664; Ephrin signaling. [P12931-1] DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells. [P12931-1] DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1. [P12931-1] DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-418885; DCC mediated attractive signaling. DR Reactome; R-HSA-418886; Netrin mediated repulsion signals. DR Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO. DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling. [P12931-1] DR Reactome; R-HSA-437239; Recycling pathway of L1. [P12931-1] DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway. [P12931-1] DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs). [P12931-1] DR Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation. [P12931-1] DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling. [P12931-1] DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. [P12931-1] DR Reactome; R-HSA-5673000; RAF activation. DR Reactome; R-HSA-5674135; MAP2K and MAPK activation. DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants. DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants. DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions. DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF. DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-HSA-69231; Cyclin D associated events in G1. [P12931-1] DR Reactome; R-HSA-8853659; RET signaling. [P12931-1] DR Reactome; R-HSA-8874081; MET activates PTK2 signaling. DR Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells. DR Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity. DR Reactome; R-HSA-8934903; Receptor Mediated Mitophagy. [P12931-1] DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation. DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-HSA-9013420; RHOU GTPase cycle. DR Reactome; R-HSA-9032500; Activated NTRK2 signals through FYN. DR Reactome; R-HSA-9603381; Activated NTRK3 signals through PI3K. DR Reactome; R-HSA-9620244; Long-term potentiation. DR Reactome; R-HSA-9634597; GPER1 signaling. DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants. DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants. DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis. [P12931-1] DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis. [P12931-1] DR Reactome; R-HSA-9670439; Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants. [P12931-1] DR Reactome; R-HSA-9680350; Signaling by CSF1 (M-CSF) in myeloid cells. DR SignaLink; P12931; -. DR SIGNOR; P12931; -. DR BioGRID-ORCS; 6714; 33 hits in 1206 CRISPR screens. DR ChiTaRS; SRC; human. DR EvolutionaryTrace; P12931; -. DR GeneWiki; Src_(gene); -. DR GenomeRNAi; 6714; -. DR Pharos; P12931; Tclin. DR PRO; PR:P12931; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P12931; Protein. DR Bgee; ENSG00000197122; Expressed in body of stomach and 163 other cell types or tissues. DR GO; GO:0005884; C:actin filament; IEA:Ensembl. DR GO; GO:0005901; C:caveola; IDA:BHF-UCL. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:1902737; C:dendritic filopodium; IEA:Ensembl. DR GO; GO:0044294; C:dendritic growth cone; IEA:Ensembl. 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; ISS:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005770; C:late endosome; IDA:UniProtKB. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0045121; C:membrane raft; ISS:ARUK-UCL. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0002102; C:podosome; IEA:Ensembl. DR GO; GO:0099091; C:postsynaptic specialization, intracellular component; IEA:Ensembl. DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl. DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0051117; F:ATPase binding; ISS:ARUK-UCL. DR GO; GO:0070700; F:BMP receptor binding; IPI:ARUK-UCL. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0071253; F:connexin binding; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB. DR GO; GO:0020037; F:heme binding; IDA:UniProtKB. DR GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl. DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:ARUK-UCL. DR GO; GO:0030331; F:nuclear estrogen receptor binding; IEA:Ensembl. DR GO; GO:0016004; F:phospholipase activator activity; IDA:ARUK-UCL. DR GO; GO:0043274; F:phospholipase binding; IPI:ARUK-UCL. DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl. DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL. DR GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL. DR GO; GO:0034332; P:adherens junction organization; IEA:Ensembl. DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISS:BHF-UCL. DR GO; GO:0045453; P:bone resorption; ISS:UniProtKB. DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl. DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl. DR GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISS:BHF-UCL. DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl. DR GO; GO:0071393; P:cellular response to progesterone stimulus; ISS:BHF-UCL. DR GO; GO:1990646; P:cellular response to prolactin; IEA:Ensembl. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:Ensembl. DR GO; GO:0035635; P:entry of bacterium into host cell; TAS:Reactome. DR GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central. DR GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome. DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome. DR GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB. DR GO; GO:0030900; P:forebrain development; IEA:Ensembl. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0060576; P:intestinal epithelial cell development; IDA:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; IDA:ARUK-UCL. DR GO; GO:0007611; P:learning or memory; IEA:Ensembl. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0016236; P:macroautophagy; TAS:Reactome. DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl. DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:BHF-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase. DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; TAS:Reactome. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IMP:UniProtKB. DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IMP:UniProtKB. DR GO; GO:0051974; P:negative regulation of telomerase activity; IMP:BHF-UCL. DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:Ensembl. DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl. DR GO; GO:0048477; P:oogenesis; IEA:Ensembl. DR GO; GO:0036035; P:osteoclast development; IBA:GO_Central. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl. DR GO; GO:0035306; P:positive regulation of dephosphorylation; IDA:ARUK-UCL. DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0010907; P:positive regulation of glucose metabolic process; IEA:Ensembl. DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0033625; P:positive regulation of integrin activation; TAS:BHF-UCL. DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IMP:UniProtKB. DR GO; GO:2000256; P:positive regulation of male germ cell proliferation; IEA:Ensembl. DR GO; GO:1903997; P:positive regulation of non-membrane spanning protein tyrosine kinase activity; NAS:ARUK-UCL. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB. DR GO; GO:2000386; P:positive regulation of ovarian follicle development; IEA:Ensembl. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:ARUK-UCL. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:UniProtKB. DR GO; GO:2000588; P:positive regulation of platelet-derived growth factor receptor-beta signaling pathway; IEA:Ensembl. DR GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl. DR GO; GO:0010954; P:positive regulation of protein processing; IEA:Ensembl. DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0051222; P:positive regulation of protein transport; IEA:Ensembl. DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl. DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IMP:ParkinsonsUK-UCL. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IDA:UniProt. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0001545; P:primary ovarian follicle growth; IEA:Ensembl. DR GO; GO:0050847; P:progesterone receptor signaling pathway; ISS:BHF-UCL. DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl. DR GO; GO:0045124; P:regulation of bone resorption; TAS:BHF-UCL. DR GO; GO:2001286; P:regulation of caveolin-mediated endocytosis; IMP:UniProtKB. DR GO; GO:0060491; P:regulation of cell projection assembly; IEA:Ensembl. DR GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:UniProtKB. DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; IMP:UniProtKB. DR GO; GO:0010632; P:regulation of epithelial cell migration; IMP:UniProtKB. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL. DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl. DR GO; GO:0034139; P:regulation of toll-like receptor 3 signaling pathway; IDA:UniProt. DR GO; GO:0043114; P:regulation of vascular permeability; TAS:BHF-UCL. DR GO; GO:0010447; P:response to acidic pH; IEA:Ensembl. DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl. DR GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0051385; P:response to mineralocorticoid; IEA:Ensembl. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0007172; P:signal complex assembly; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0014856; P:skeletal muscle cell proliferation; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome. DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0045056; P:transcytosis; IEA:Ensembl. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0060065; P:uterus development; IEA:Ensembl. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome. DR CDD; cd05071; PTKc_Src; 1. DR CDD; cd10365; SH2_Src_Src; 1. DR CDD; cd12008; SH3_Src; 1. DR DisProt; DP01570; -. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR IDEAL; IID00708; -. 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 PANTHER; PTHR24418:SF53; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC; 1. DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. 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; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 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. DR Genevisible; P12931; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell adhesion; Cell cycle; KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Disease variant; KW Host-virus interaction; Immunity; Kinase; Lipoprotein; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Myristate; Nucleotide-binding; KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; KW SH3 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..536 FT /note="Proto-oncogene tyrosine-protein kinase Src" FT /id="PRO_0000088141" FT DOMAIN 84..145 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 151..248 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 270..523 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 389 FT /note="Proton acceptor" FT BINDING 276..284 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 298 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 75 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000269|PubMed:21442427, FT ECO:0007744|PubMed:23186163" FT MOD_RES 187 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P05480" FT MOD_RES 419 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:14661060, FT ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:19307596, FT ECO:0000269|PubMed:25731159, ECO:0000269|PubMed:26936507, FT ECO:0000269|PubMed:6273838" FT MOD_RES 419 FT /note="Phosphotyrosine; by FAK2" FT /evidence="ECO:0000250" FT MOD_RES 530 FT /note="Phosphotyrosine; by CSK" FT /evidence="ECO:0000269|PubMed:19307596, FT ECO:0000269|PubMed:26936507, ECO:0000269|PubMed:7525268, FT ECO:0000269|PubMed:7929427, ECO:0007744|PubMed:19369195" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:7525268" FT VAR_SEQ 117 FT /note="T -> TRKVDVR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:2681803" FT /id="VSP_012134" FT VAR_SEQ 117 FT /note="T -> TRKVDVSQTWFTFRWLQR (in isoform 3)" FT /id="VSP_061494" FT VARIANT 176 FT /note="L -> F (in dbSNP:rs6018260)" FT /id="VAR_051699" FT VARIANT 237 FT /note="A -> T (in dbSNP:rs34881773)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041830" FT VARIANT 527 FT /note="E -> K (in THC6; increased protein tyrosine kinase FT activity; increased autophosphorylation at Y-419; causes FT defective megakaryopoiesis associated with increased FT overall tyrosine phosphorylation in megakaryocytes; FT dbSNP:rs879255268)" FT /evidence="ECO:0000269|PubMed:26936507" FT /id="VAR_076919" FT MUTAGEN 298 FT /note="K->M: Kinase inactive. Abolishes ubiquitination FT promoted by CBLC." FT /evidence="ECO:0000269|PubMed:14661060" FT MUTAGEN 302 FT /note="P->E: Kinase active. Interacts with PDLIM4; when FT associated with E-307 and F-419." FT /evidence="ECO:0000269|PubMed:19307596" FT MUTAGEN 307 FT /note="P->E: Kinase active. Interacts with PDLIM4; when FT associated with E-302 and F-419." FT /evidence="ECO:0000269|PubMed:19307596" FT MUTAGEN 419 FT /note="Y->F: Loss of kinase activity. Loss of interaction FT with PDLIM4." FT /evidence="ECO:0000269|PubMed:19307596" FT STRAND 87..93 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 118..126 FT /evidence="ECO:0007829|PDB:1FMK" FT TURN 127..129 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 132..136 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 158..165 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:1SHD" FT STRAND 174..179 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 187..195 FT /evidence="ECO:0007829|PDB:1FMK" FT TURN 196..198 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 199..209 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:2SRC" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 221..225 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 226..233 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 270..278 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 280..282 FT /evidence="ECO:0007829|PDB:6ATE" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:1FMK" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 293..299 FT /evidence="ECO:0007829|PDB:1FMK" FT TURN 302..304 FT /evidence="ECO:0007829|PDB:2BDF" FT HELIX 307..319 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 328..332 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 338..341 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 345..348 FT /evidence="ECO:0007829|PDB:6ATE" FT HELIX 349..353 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 355..358 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 363..382 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 392..394 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 399..401 FT /evidence="ECO:0007829|PDB:1FMK" FT STRAND 403..405 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 410..413 FT /evidence="ECO:0007829|PDB:2SRC" FT HELIX 417..420 FT /evidence="ECO:0007829|PDB:2SRC" FT TURN 423..426 FT /evidence="ECO:0007829|PDB:1Y57" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 434..439 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 444..459 FT /evidence="ECO:0007829|PDB:1FMK" FT TURN 460..462 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 471..479 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 492..501 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 506..508 FT /evidence="ECO:0007829|PDB:1FMK" FT HELIX 512..520 FT /evidence="ECO:0007829|PDB:1FMK" FT TURN 521..523 FT /evidence="ECO:0007829|PDB:1FMK" SQ SEQUENCE 536 AA; 59835 MW; C1908084683E5DE8 CRC64; MGSNKSKPKD ASQRRRSLEP AENVHGAGGG AFPASQTPSK PASADGHRGP SAAFAPAAAE PKLFGGFNSS DTVTSPQRAG PLAGGVTTFV ALYDYESRTE TDLSFKKGER LQIVNNTEGD WWLAHSLSTG QTGYIPSNYV APSDSIQAEE WYFGKITRRE SERLLLNAEN PRGTFLVRES ETTKGAYCLS VSDFDNAKGL NVKHYKIRKL DSGGFYITSR TQFNSLQQLV AYYSKHADGL CHRLTTVCPT SKPQTQGLAK DAWEIPRESL RLEVKLGQGC FGEVWMGTWN GTTRVAIKTL KPGTMSPEAF LQEAQVMKKL RHEKLVQLYA VVSEEPIYIV TEYMSKGSLL DFLKGETGKY LRLPQLVDMA AQIASGMAYV ERMNYVHRDL RAANILVGEN LVCKVADFGL ARLIEDNEYT ARQGAKFPIK WTAPEAALYG RFTIKSDVWS FGILLTELTT KGRVPYPGMV NREVLDQVER GYRMPCPPEC PESLHDLMCQ CWRKEPEERP TFEYLQAFLE DYFTSTEPQY QPGENL //