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Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)

 SRC_HUMAN               Reviewed;         536 AA.
P12931; E1P5V4; Q76P87; Q86VB9; Q9H5A8;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 224.
RecName: Full=Proto-oncogene tyrosine-protein kinase Src;
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};
AltName: Full=Proto-oncogene c-Src;
AltName: Full=pp60c-src;
Short=p60-Src;
Name=SRC; Synonyms=SRC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185 (ISOFORM 1).
PubMed=3299057; DOI=10.1128/MCB.7.5.1978;
Tanaka A., Gibbs C.P., Arthur R.R., Anderson S.K., Kung H.-J.,
Fujita D.J.;
"DNA sequence encoding the amino-terminal region of the human c-src
protein: implications of sequence divergence among src-type kinase
oncogenes.";
Mol. Cell. Biol. 7:1978-1983(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-536 (ISOFORM 1).
PubMed=2582238; DOI=10.1128/MCB.5.5.1122;
Anderson S.K., Gibbs C.P., Tanaka A., Kung H.-J., Fujita D.J.;
"Human cellular src gene: nucleotide sequence and derived amino acid
sequence of the region coding for the carboxy-terminal two-thirds of
pp60c-src.";
Mol. Cell. Biol. 5:1122-1129(1985).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 98-139 (ISOFORM 2).
PubMed=2681803; DOI=10.1002/jnr.490240113;
Pyper J.M., Bolen J.B.;
"Neuron-specific splicing of C-SRC RNA in human brain.";
J. Neurosci. Res. 24:89-96(1989).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-536 (ISOFORM 1).
PubMed=2581127; DOI=10.1128/MCB.5.4.831;
Parker R.C., Mardon G., Lebo R.V., Varmus H.E., Bishop J.M.;
"Isolation of duplicated human c-src genes located on chromosomes 1
and 20.";
Mol. Cell. Biol. 5:831-838(1985).
[8]
PHOSPHORYLATION AT TYR-419.
PubMed=6273838; DOI=10.1073/pnas.78.10.6013;
Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F.,
Erikson R.L., Bishop J.M.;
"Characterization of sites for tyrosine phosphorylation in the
transforming protein of Rous sarcoma virus (pp60v-src) and its normal
cellular homologue (pp60c-src).";
Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981).
[9]
ROLE IN TUMOR TISSUES.
PubMed=3093483;
Rosen N., Bolen J.B., Schwartz A.M., Cohen P., DeSeau V., Israel M.A.;
"Analysis of pp60c-src protein kinase activity in human tumor cell
lines and tissues.";
J. Biol. Chem. 261:13754-13759(1986).
[10]
ROLE IN COLON CARCINOMA.
PubMed=2498394; DOI=10.1172/JCI114113;
Cartwright C.A., Kamps M.P., Meisler A.I., Pipas J.M., Eckhart W.;
"pp60c-src activation in human colon carcinoma.";
J. Clin. Invest. 83:2025-2033(1989).
[11]
ALTERNATIVE SPLICING.
PubMed=1691439; DOI=10.1128/MCB.10.5.2035;
Pyper J.M., Bolen J.B.;
"Identification of a novel neuronal C-SRC exon expressed in human
brain.";
Mol. Cell. Biol. 10:2035-2040(1990).
[12]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-530, AND MYRISTOYLATION
AT GLY-2.
PubMed=7525268;
Kaplan K.B., Bibbins K.B., Swedlow J.R., Arnaud M., Morgan D.O.,
Varmus H.E.;
"Association of the amino-terminal half of c-Src with focal adhesions
alters their properties and is regulated by phosphorylation of
tyrosine 527.";
EMBO J. 13:4745-4756(1994).
[13]
CATALYTIC ACTIVITY, ENZYME REGULATION, AND PHOSPHORYLATION.
PubMed=7929427;
Stover D.R., Liebetanz J., Lydon N.B.;
"Cdc2-mediated modulation of pp60c-src activity.";
J. Biol. Chem. 269:26885-26889(1994).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=7853507;
David-Pfeuty T., Nouvian-Dooghe Y.;
"Highly specific antibody to Rous sarcoma virus src gene product
recognizes nuclear and nucleolar antigens in human cells.";
J. Virol. 69:1699-1713(1995).
[15]
INTERACTION WITH CEACAM1.
PubMed=7478590;
Bruemmer J., Neumaier M., Goepfert C., Wagener C.;
"Association of pp60c-src with biliary glycoprotein (CD66a), an
adhesion molecule of the carcinoembryonic antigen family downregulated
in colorectal carcinomas.";
Oncogene 11:1649-1655(1995).
[16]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND INTERACTION WITH
FCAMR.
PubMed=8759729;
Rabinowich H., Manciulea M., Metes D., Sulica A., Herberman R.B.,
Corey S.J., Whiteside T.L.;
"Physical and functional association of Fc mu receptor on human
natural killer cells with the zeta- and Fc epsilon RI gamma-chains and
with src family protein tyrosine kinases.";
J. Immunol. 157:1485-1491(1996).
[17]
FUNCTION IN HGF SIGNALING PATHWAY.
PubMed=8755529; DOI=10.1073/pnas.93.15.7644;
Grano M., Galimi F., Zambonin G., Colucci S., Cottone E.,
Zallone A.Z., Comoglio P.M.;
"Hepatocyte growth factor is a coupling factor for osteoclasts and
osteoblasts in vitro.";
Proc. Natl. Acad. Sci. U.S.A. 93:7644-7648(1996).
[18]
CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=9571170; DOI=10.1006/bbrc.1998.8452;
Yang E.B., Zhang K., Cheng L.Y., Mack P.;
"Butein, a specific protein tyrosine kinase inhibitor.";
Biochem. Biophys. Res. Commun. 245:435-438(1998).
[19]
INTERACTION WITH RACK1.
PubMed=9584165; DOI=10.1128/MCB.18.6.3245;
Chang B.Y., Conroy K.B., Machleder E.M., Cartwright C.A.;
"RACK1, a receptor for activated C kinase and a homolog of the beta
subunit of G proteins, inhibits activity of src tyrosine kinases and
growth of NIH 3T3 cells.";
Mol. Cell. Biol. 18:3245-3256(1998).
[20]
INTERACTION WITH ADRB2 AND ARRB1.
PubMed=9924018; DOI=10.1126/science.283.5402.655;
Luttrell L.M., Ferguson S.S.G., Daaka Y., Miller W.E., Maudsley S.,
Della Rocca G.J., Lin F.-T., Kawakatsu H., Owada K., Luttrell D.K.,
Caron M.G., Lefkowitz R.J.;
"Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src
protein kinase complexes.";
Science 283:655-661(1999).
[21]
INTERACTION WITH ARRB1 AND ARRB2.
PubMed=10753943; DOI=10.1074/jbc.275.15.11312;
Miller W.E., Maudsley S., Ahn S., Khan K.D., Luttrell L.M.,
Lefkowitz R.J.;
"beta-arrestin1 interacts with the catalytic domain of the tyrosine
kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in
receptor endocytosis.";
J. Biol. Chem. 275:11312-11319(2000).
[22]
INTERACTION WITH RALGPS1.
PubMed=10747847; DOI=10.1074/jbc.C000085200;
Rebhun J.F., Chen H., Quilliam L.A.;
"Identification and characterization of a new family of guanine
nucleotide exchange factors for the ras-related GTPase Ral.";
J. Biol. Chem. 275:13406-13410(2000).
[23]
FUNCTION IN PHOSPHORYLATION OF RASA1 AND RASGRF1.
PubMed=11389730; DOI=10.1046/j.1432-1327.2001.02230.x;
Giglione C., Gonfloni S., Parmeggiani A.;
"Differential actions of p60c-Src and Lck kinases on the Ras
regulators p120-GAP and GDP/GTP exchange factor CDC25Mm.";
Eur. J. Biochem. 268:3275-3283(2001).
[24]
INTERACTION WITH MUC1.
PubMed=11152665; DOI=10.1074/jbc.C000754200;
Li Y., Kuwahara H., Ren J., Wen G., Kufe D.;
"The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1
carcinoma-associated antigen with GSK3 beta and beta-catenin.";
J. Biol. Chem. 276:6061-6064(2001).
[25]
INTERACTION WITH RACK1.
PubMed=11279199; DOI=10.1074/jbc.M101375200;
Chang B.Y., Chiang M., Cartwright C.A.;
"The interaction of Src and RACK1 is enhanced by activation of protein
kinase C and tyrosine phosphorylation of RACK1.";
J. Biol. Chem. 276:20346-20356(2001).
[26]
INTERACTION WITH HEV ORF3 PROTEIN.
PubMed=11518702; DOI=10.1074/jbc.M101546200;
Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M.,
Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.;
"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains
and activates MAPK.";
J. Biol. Chem. 276:42389-42400(2001).
[27]
INTERACTION WITH CAV2.
PubMed=12091389; DOI=10.1074/jbc.M204367200;
Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E.,
Lisanti M.P.;
"Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-
caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains
associated with lipid rafts/caveolae, but no longer forms a high
molecular mass hetero-oligomer with caveolin-1.";
J. Biol. Chem. 277:34556-34567(2002).
[28]
INTERACTION WITH PELP1.
PubMed=12415108; DOI=10.1073/pnas.192569699;
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
"Estrogen receptor-interacting protein that modulates its nongenomic
activity-crosstalk with Src/Erk phosphorylation cascade.";
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
[29]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12615910; DOI=10.1083/jcb.200209098;
Miyazaki T., Neff L., Tanaka S., Horne W.C., Baron R.;
"Regulation of cytochrome c oxidase activity by c-Src in
osteoclasts.";
J. Cell Biol. 160:709-718(2003).
[30]
INTERACTION WITH EPHB1.
PubMed=12925710; DOI=10.1083/jcb.200302073;
Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.;
"EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote
chemotaxis.";
J. Cell Biol. 162:661-671(2003).
[31]
CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=14632929; DOI=10.1046/j.1399-3011.2003.00094.x;
Kamath J.R., Liu R., Enstrom A.M., Lou Q., Lam K.S.;
"Development and characterization of potent and specific peptide
inhibitors of p60c-src protein tyrosine kinase using pseudosubstrate-
based inhibitor design approach.";
J. Pept. Res. 62:260-268(2003).
[32]
FUNCTION IN PHOSPHORYLATION OF PDPK1, AND INTERACTION WITH PTK2B/PYK2.
PubMed=14585963; DOI=10.1128/MCB.23.22.8019-8029.2003;
Taniyama Y., Weber D.S., Rocic P., Hilenski L., Akers M.L., Park J.,
Hemmings B.A., Alexander R.W., Griendling K.K.;
"Pyk2- and Src-dependent tyrosine phosphorylation of PDK1 regulates
focal adhesions.";
Mol. Cell. Biol. 23:8019-8029(2003).
[33]
INTERACTION WITH CAV2.
PubMed=15504032; DOI=10.1021/bi049295+;
Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W.,
Campos-Gonzalez R., Lisanti M.P.;
"Tyrosine phosphorylation of caveolin-2 at residue 27: differences in
the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27).";
Biochemistry 43:13694-13706(2004).
[34]
INTERACTION WITH CBCLC, PHOSPHORYLATION AT TYR-419, AND MUTAGENESIS OF
LYS-298.
PubMed=14661060; DOI=10.1038/sj.onc.1207298;
Kim M., Tezuka T., Tanaka K., Yamamoto T.;
"Cbl-c suppresses v-Src-induced transformation through ubiquitin-
dependent protein degradation.";
Oncogene 23:1645-1655(2004).
[35]
INTERACTION WITH CDCP1.
PubMed=15851033; DOI=10.1016/j.cell.2005.02.019;
Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.;
"The C2 domain of PKCdelta is a phosphotyrosine binding domain.";
Cell 121:271-280(2005).
[36]
FUNCTION IN PHOSPHORYLATION OF DDR2.
PubMed=16186108; DOI=10.1074/jbc.M506921200;
Yang K., Kim J.H., Kim H.J., Park I.S., Kim I.Y., Yang B.S.;
"Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src
stimulates intramolecular autophosphorylation and Shc signaling
complex formation.";
J. Biol. Chem. 280:39058-39066(2005).
[37]
INTERACTION WITH TOM1L2.
PubMed=16479011; DOI=10.1128/MCB.26.5.1932-1947.2006;
Franco M., Furstoss O., Simon V., Benistant C., Hong W.J., Roche S.;
"The adaptor protein Tom1L1 is a negative regulator of Src mitogenic
signaling induced by growth factors.";
Mol. Cell. Biol. 26:1932-1947(2006).
[38]
INTERACTION WITH TGFB1I1.
PubMed=17202804; DOI=10.1159/000098402;
Maudsley S., Davidson L., Pawson A.J., Freestone S.H.,
Lopez de Maturana R., Thomson A.A., Millar R.P.;
"Gonadotropin-releasing hormone functionally antagonizes testosterone
activation of the human androgen receptor in prostate cells through
focal adhesion complexes involving Hic-5.";
Neuroendocrinology 84:285-300(2006).
[39]
INTERACTION WITH AMOTL2.
PubMed=17293535; DOI=10.1242/dev.02782;
Huang H., Lu F.I., Jia S., Meng S., Cao Y., Wang Y., Ma W., Yin K.,
Wen Z., Peng J., Thisse C., Thisse B., Meng A.;
"Amotl2 is essential for cell movements in zebrafish embryo and
regulates c-Src translocation.";
Development 134:979-988(2007).
[40]
INTERACTION WITH SRCIN1.
PubMed=17525734; DOI=10.1038/sj.emboj.7601724;
Di Stefano P., Damiano L., Cabodi S., Aramu S., Tordella L.,
Praduroux A., Piva R., Cavallo F., Forni G., Silengo L., Tarone G.,
Turco E., Defilippi P.;
"p140Cap protein suppresses tumour cell properties, regulating Csk and
Src kinase activity.";
EMBO J. 26:2843-2855(2007).
[41]
FUNCTION.
PubMed=18586953; DOI=10.1152/ajplung.90282.2008;
Jeulin C., Seltzer V., Bailbe D., Andreau K., Marano F.;
"EGF mediates calcium-activated chloride channel activation in the
human bronchial epithelial cell line 16HBE14o-: involvement of
tyrosine kinase p60c-src.";
Am. J. Physiol. 295:L489-L496(2008).
[42]
INTERACTION WITH PDPK1.
PubMed=18024423; DOI=10.1074/jbc.M706361200;
Yang K.J., Shin S., Piao L., Shin E., Li Y., Park K.A., Byun H.S.,
Won M., Hong J., Kweon G.R., Hur G.M., Seok J.H., Chun T.,
Brazil D.P., Hemmings B.A., Park J.;
"Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by
Src involves tyrosine phosphorylation of PDK1 and Src homology 2
domain binding.";
J. Biol. Chem. 283:1480-1491(2008).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[44]
INTERACTION WITH PTK2/FAK1; PI3KR1/2 AND ESR1.
PubMed=18657504; DOI=10.1016/j.molcel.2008.05.025;
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y.,
Sentis S., Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S.,
Corbo L.;
"Regulation of estrogen rapid signaling through arginine methylation
by PRMT1.";
Mol. Cell 31:212-221(2008).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[46]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[47]
INTERACTION WITH MPP2.
PubMed=19665017; DOI=10.1016/j.yexcr.2009.07.028;
Baumgartner M., Weiss A., Fritzius T., Heinrich J., Moelling K.;
"The PDZ protein MPP2 interacts with c-Src in epithelial cells.";
Exp. Cell Res. 315:2888-2898(2009).
[48]
FUNCTION, AND INTERACTION WITH TRAF3; MAVS; DDX58 AND TBK1.
PubMed=19419966; DOI=10.1074/jbc.M808233200;
Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A.,
Anthonsen M.W.;
"The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible
gene I)-elicited antiviral signaling.";
J. Biol. Chem. 284:19122-19131(2009).
[49]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PDLIM4, SUBCELLULAR
LOCATION, PHOSPHORYLATION AT TYR-419 AND TYR-530, AND MUTAGENESIS OF
PRO-302; PRO-307 AND TYR-419.
PubMed=19307596; DOI=10.1083/jcb.200810155;
Zhang Y., Tu Y., Zhao J., Chen K., Wu C.;
"Reversion-induced LIM interaction with Src reveals a novel Src
inactivation cycle.";
J. Cell Biol. 184:785-792(2009).
[50]
PHOSPHORYLATION AT TYR-419, AND DEPHOSPHORYLATION AT TYR-419 BY PTPRJ.
PubMed=18936167; DOI=10.1128/MCB.01374-08;
Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.;
"New role for the protein tyrosine phosphatase DEP-1 in Akt activation
and endothelial cell survival.";
Mol. Cell. Biol. 29:241-253(2009).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND TYR-530, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[52]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[53]
CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=21036157; DOI=10.1016/j.bbrc.2010.10.101;
Yao X., Balamurugan P., Arvey A., Leslie C., Zhang L.;
"Heme controls the regulation of protein tyrosine kinases Jak2 and
Src.";
Biochem. Biophys. Res. Commun. 403:30-35(2010).
[54]
FUNCTION, AND INTERACTION WITH RUNX3.
PubMed=20100835; DOI=10.1074/jbc.M109.071381;
Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W.,
Li Y.H., Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.;
"Src kinase phosphorylates RUNX3 at tyrosine residues and localizes
the protein in the cytoplasm.";
J. Biol. Chem. 285:10122-10129(2010).
[55]
FUNCTION IN CBLC PHOSPHORYLATION.
PubMed=20525694; DOI=10.1074/jbc.M109.091157;
Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.;
"The N terminus of Cbl-c regulates ubiquitin ligase activity by
modulating affinity for the ubiquitin-conjugating enzyme.";
J. Biol. Chem. 285:23687-23698(2010).
[56]
INTERACTION WITH NDFIP1 AND NDFIP2.
PubMed=20534535; DOI=10.1073/pnas.0911714107;
Mund T., Pelham H.R.;
"Regulation of PTEN/Akt and MAP kinase signaling pathways by the
ubiquitin ligase activators Ndfip1 and Ndfip2.";
Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010).
[57]
FUNCTION, AND INTERACTION WITH TNK2.
PubMed=21309750; DOI=10.1042/BJ20102156;
Chan W., Sit S.T., Manser E.;
"The Cdc42-associated kinase ACK1 is not auto-inhibited but requires
Src for activation.";
Biochem. J. 435:355-364(2011).
[58]
PHOSPHORYLATION AT SER-75.
PubMed=21442427; DOI=10.1007/s00018-011-0638-1;
Pan Q., Qiao F., Gao C., Norman B., Optican L., Zelenka P.S.;
"Cdk5 targets active Src for ubiquitin-dependent degradation by
phosphorylating Src(S75).";
Cell. Mol. Life Sci. 68:3425-3436(2011).
[59]
INTERACTION WITH PRR7.
PubMed=21460222; DOI=10.1074/jbc.M110.175117;
Hrdinka M., Draber P., Stepanek O., Ormsby T., Otahal P.,
Angelisova P., Brdicka T., Paces J., Horejsi V., Drbal K.;
"PRR7 is a transmembrane adaptor protein expressed in activated T
cells involved in regulation of T cell receptor signaling and
apoptosis.";
J. Biol. Chem. 286:19617-19629(2011).
[60]
FUNCTION IN FOCAL ADHESION DYNAMICS, AND INTERACTION WITH PTK2/FAK1
AND DNM2.
PubMed=21411625; DOI=10.1091/mbc.E10-09-0785;
Wang Y., Cao H., Chen J., McNiven M.A.;
"A direct interaction between the large GTPase dynamin-2 and FAK
regulates focal adhesion dynamics in response to active Src.";
Mol. Biol. Cell 22:1529-1538(2011).
[61]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-75, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[62]
FUNCTION IN PHOSPHORYLATION OF BCAR1.
PubMed=22710723; DOI=10.1038/onc.2012.220;
Zhang P., Guo A., Possemato A., Wang C., Beard L., Carlin C.,
Markowitz S.D., Polakiewicz R.D., Wang Z.;
"Identification and functional characterization of p130Cas as a
substrate of protein tyrosine phosphatase nonreceptor 14.";
Oncogene 32:2087-2095(2013).
[63]
INTERACTION WITH TRAP1.
PubMed=23564345; DOI=10.1073/pnas.1220659110;
Yoshida S., Tsutsumi S., Muhlebach G., Sourbier C., Lee M.J., Lee S.,
Vartholomaiou E., Tatokoro M., Beebe K., Miyajima N., Mohney R.P.,
Chen Y., Hasumi H., Xu W., Fukushima H., Nakamura K., Koga F.,
Kihara K., Trepel J., Picard D., Neckers L.;
"Molecular chaperone TRAP1 regulates a metabolic switch between
mitochondrial respiration and aerobic glycolysis.";
Proc. Natl. Acad. Sci. U.S.A. 110:E1604-E1612(2013).
[64]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[65]
PHOSPHORYLATION AT TYR-419 AND TYR-530, INVOLVEMENT IN THC6, VARIANT
THC6 LYS-527, AND CHARACTERIZATION OF VARIANT THC6 LYS-527.
PubMed=26936507; DOI=10.1126/scitranslmed.aad7666;
BRIDGE-BPD Consortium;
Turro E., Greene D., Wijgaerts A., Thys C., Lentaigne C.,
Bariana T.K., Westbury S.K., Kelly A.M., Selleslag D., Stephens J.C.,
Papadia S., Simeoni I., Penkett C.J., Ashford S., Attwood A.,
Austin S., Bakchoul T., Collins P., Deevi S.V., Favier R.,
Kostadima M., Lambert M.P., Mathias M., Millar C.M., Peerlinck K.,
Perry D.J., Schulman S., Whitehorn D., Wittevrongel C., De Maeyer M.,
Rendon A., Gomez K., Erber W.N., Mumford A.D., Nurden P., Stirrups K.,
Bradley J.R., Raymond F.L., Laffan M.A., Van Geet C., Richardson S.,
Freson K., Ouwehand W.H.;
"A dominant gain-of-function mutation in universal tyrosine kinase SRC
causes thrombocytopenia, myelofibrosis, bleeding, and bone
pathologies.";
Sci. Transl. Med. 8:328RA30-328RA30(2016).
[66]
REVIEW ON FUNCTION.
PubMed=8672527; DOI=10.1016/0304-419X(96)00003-0;
Brown M.T., Cooper J.A.;
"Regulation, substrates and functions of src.";
Biochim. Biophys. Acta 1287:121-149(1996).
[67]
REVIEW ON FUNCTION.
PubMed=9442882; DOI=10.1146/annurev.cellbio.13.1.513;
Thomas S.M., Brugge J.S.;
"Cellular functions regulated by Src family kinases.";
Annu. Rev. Cell Dev. Biol. 13:513-609(1997).
[68]
REVIEW ON FUNCTION.
PubMed=11964124; DOI=10.1007/s00018-002-8438-2;
Ma Y.C., Huang X.Y.;
"Novel regulation and function of Src tyrosine kinase.";
Cell. Mol. Life Sci. 59:456-462(2002).
[69]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 86-536.
PubMed=9024657; DOI=10.1038/385595a0;
Xu W., Harrison S.C., Eck M.J.;
"Three-dimensional structure of the tyrosine kinase c-Src.";
Nature 385:595-602(1997).
[70]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 145-249.
PubMed=9174343; DOI=10.1021/bi970019n;
Charifson P.S., Shewchuk L.M., Rocque W., Hummel C.W., Jordan S.R.,
Mohr C., Pacofsky G.J., Peel M.R., Rodriguez M., Sternbach D.D.,
Consler T.G.;
"Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and
structural study.";
Biochemistry 36:6283-6293(1997).
[71]
STRUCTURE BY NMR OF 204-249.
PubMed=7532003; DOI=10.1021/bi00007a003;
Xu R.X., Word J.M., Davis D.G., Rink M.J., Willard D.H. Jr.,
Gampe R.T. Jr.;
"Solution structure of the human pp60c-src SH2 domain complexed with a
phosphorylated tyrosine pentapeptide.";
Biochemistry 34:2107-2121(1995).
[72]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 412-424 IN COMPLEX WITH
CBLC, UBIQUITINATION, AND INTERACTION WITH CBLC.
PubMed=22888118; DOI=10.1093/jb/mvs085;
Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M.,
Yamanashi Y., Yamamoto T., Nakagawa A.;
"Structural flexibility regulates phosphopeptide-binding activity of
the tyrosine kinase binding domain of Cbl-c.";
J. Biochem. 152:487-495(2012).
[73]
VARIANT [LARGE SCALE ANALYSIS] THR-237.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Non-receptor protein tyrosine kinase which is activated
following engagement of many different classes of cellular
receptors including immune response receptors, integrins and other
adhesion receptors, receptor protein tyrosine kinases, G protein-
coupled receptors as well as cytokine receptors. Participates in
signaling pathways that control a diverse spectrum of biological
activities including gene transcription, immune response, cell
adhesion, cell cycle progression, apoptosis, migration, and
transformation. Due to functional redundancy between members of
the SRC kinase family, identification of the specific role of each
SRC kinase is very difficult. SRC appears to be one of the primary
kinases activated following engagement of receptors and plays a
role in the activation of other protein tyrosine kinase (PTK)
families. Receptor clustering or dimerization leads to recruitment
of SRC to the receptor complexes where it phosphorylates the
tyrosine residues within the receptor cytoplasmic domains. Plays
an important role in the regulation of cytoskeletal organization
through phosphorylation of specific substrates such as AFAP1.
Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1
and to localize to actin filaments. Cytoskeletal reorganization is
also controlled through the phosphorylation of cortactin (CTTN)
(Probable). When cells adhere via focal adhesions to the
extracellular matrix, signals are transmitted by integrins into
the cell resulting in tyrosine phosphorylation of a number of
focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN)
(PubMed:21411625). In addition to phosphorylating focal adhesion
proteins, SRC is also active at the sites of cell-cell contact
adherens junctions and phosphorylates substrates such as beta-
catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP).
Another type of cell-cell junction, the gap junction, is also a
target for SRC, which phosphorylates connexin-43 (GJA1). SRC is
implicated in regulation of pre-mRNA-processing and phosphorylates
RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role
in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3,
leading to increased DNA binding activity of these transcription
factors (By similarity). Involved in the RAS pathway through
phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a
role in EGF-mediated calcium-activated chloride channel activation
(PubMed:18586953). Required for epidermal growth factor receptor
(EGFR) internalization through phosphorylation of clathrin heavy
chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin
(ARRB1 and ARRB2) desensitization through phosphorylation and
activation of GRK2, leading to beta-arrestin phosphorylation and
internalization. Has a critical role in the stimulation of the
CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal
growth factor (Probable). Might be involved not only in mediating
the transduction of mitogenic signals at the level of the plasma
membrane but also in controlling progression through the cell
cycle via interaction with regulatory proteins in the nucleus
(PubMed:7853507). Plays an important role in osteoclastic bone
resorption in conjunction with PTK2B/PYK2. Both the formation of a
SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for
this function. Recruited to activated integrins by PTK2B/PYK2,
thereby phosphorylating CBL, which in turn induces the activation
and recruitment of phosphatidylinositol 3-kinase to the cell
membrane in a signaling pathway that is critical for osteoclast
function (PubMed:8755529, PubMed:14585963). Promotes energy
production in osteoclasts by activating mitochondrial cytochrome C
oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine
residues, thereby promoting its subsequent autophosphorylation
(PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine
residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835,
PubMed:21309750). Enhances DDX58/RIG-I-elicited antiviral
signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9',
'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at
'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple
tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3
activity (PubMed:20525694). Involved in anchorage-independent cell
growth (PubMed:19307596). Required for podosome formation (By
similarity). {ECO:0000250|UniProtKB:P05480,
ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:12615910,
ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:16186108,
ECO:0000269|PubMed:18586953, ECO:0000269|PubMed:19307596,
ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:20100835,
ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:21309750,
ECO:0000269|PubMed:21411625, ECO:0000269|PubMed:22710723,
ECO:0000269|PubMed:7853507, ECO:0000269|PubMed:8755529,
ECO:0000269|PubMed:8759729, ECO:0000305|PubMed:11964124,
ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:14632929,
ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:21036157,
ECO:0000269|PubMed:7929427, ECO:0000269|PubMed:8759729,
ECO:0000269|PubMed:9571170}.
-!- ENZYME REGULATION: Phosphorylation by CSK at Tyr-530 inhibits
kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced
by heme. Further phosphorylation by CDK1 partially reactivates
CSK-inactivated SRC and facilitates complete reactivation by
protein tyrosine phosphatase PTPRC. Integrin engagement stimulates
kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase
activity. Butein and pseudosubstrate-based peptide inhibitors like
CIYKYYF act as inhibitors. Phosphorylation at Tyr-419 increases
kinase activity. {ECO:0000269|PubMed:14632929,
ECO:0000269|PubMed:21036157, ECO:0000269|PubMed:7929427,
ECO:0000269|PubMed:8759729, ECO:0000269|PubMed:9571170}.
-!- SUBUNIT: Interacts with DDEF1/ASAP1; via the SH3 domain (By
similarity). Interacts with CCPG1 (By similarity). Identified in a
complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1,
GAP43 and CTTN (By similarity). Interacts with ERBB2, STAT1 and
PNN (By similarity). Interacts with DDR1, DDR2 and DAB2 (By
similarity). Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2
(PubMed:12415108, PubMed:15851033, PubMed:16479011,
PubMed:17202804). Interacts with the cytoplasmic domain of MUC1,
phosphorylates it and increases binding of MUC1 with beta-catenin
(PubMed:11152665). Interacts with RALGPS1; via the SH3 domain
(PubMed:10747847). Interacts with CAV2 (tyrosine phosphorylated
form) (PubMed:12091389, PubMed:15504032). Interacts (via the SH3
domain and the protein kinase domain) with ARRB1; the interaction
is independent of the phosphorylation state of SRC C-terminus (By
similarity). Interacts with ARRB1 and ARRB2 (PubMed:10753943,
PubMed:9924018). Interacts with SRCIN1 (PubMed:17525734).
Interacts with NDFIP2 and more weakly with NDFIP1
(PubMed:20534535). Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1
and ESR1 (dimethylated on arginine) (PubMed:18657504,
PubMed:21411625). Interacts with FASLG (PubMed:19807924).
Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form
of PTK2B/PYK2 (PubMed:14585963). Interacts (via SH2 domain) with
FLT3 (tyrosine phosphorylated) (By similarity). Interacts with
PDGFRA (tyrosine phosphorylated) (By similarity). Interacts with
CSF1R (By similarity). Interacts (via SH2 and SH3 domain) with
TNK2 (PubMed:21309750). Interacts (via protein kinase domain) with
the tyrosine phosphorylated form of RUNX3 (via runt domain)
(PubMed:20100835). Interacts with TRAF3 (via RING-type zinc finger
domain) (PubMed:19419966). Interacts with DDX58, MAVS and TBK1
(PubMed:19419966). Interacts (via SH2 domain) with RACK1; the
interaction is enhanced by tyrosine phosphorylation of RACK1 and
inhibits SRC activity (PubMed:9584165, PubMed:11279199). Interacts
with EPHB1; activates the MAPK/ERK cascade to regulate cell
migration (PubMed:12925710). Interacts with FCAMR
(PubMed:8759729). Interacts (via SH2 domain) with the 'Tyr-9'
phosphorylated form of PDPK1 (PubMed:18024423). Interacts with
AMOTL2; this interaction regulates the translocation of
phosphorylated SRC to peripheral cell-matrix adhesion sites
(PubMed:17293535). Interacts with TRAP1 (PubMed:23564345).
Interacts with CBLC; the interaction is enhanced when SRC is
phosphorylated at Tyr-419 (PubMed:14661060, PubMed:22888118).
Interacts with ARHGEF5 (By similarity). Interacts (via cytoplasmic
domain) with CEACAM1 (via SH2 domain); this interaction is
regulated by trans-homophilic cell adhesion (PubMed:7478590).
Interacts with MPP2 (PubMed:19665017). Interacts with PRR7
(PubMed:21460222). Interacts (via kinase domain and to a lesser
extent the SH2 domain) directly with PDLIM4; this interaction
results in PTPN13-mediated dephosphorylation of this protein
leading to its inactivation (PubMed:19307596).
{ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:Q9WUD9,
ECO:0000269|PubMed:10747847, ECO:0000269|PubMed:10753943,
ECO:0000269|PubMed:11152665, ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12091389, ECO:0000269|PubMed:12415108,
ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:14585963,
ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:15504032,
ECO:0000269|PubMed:15851033, ECO:0000269|PubMed:16479011,
ECO:0000269|PubMed:17202804, ECO:0000269|PubMed:17293535,
ECO:0000269|PubMed:17525734, ECO:0000269|PubMed:18024423,
ECO:0000269|PubMed:18657504, ECO:0000269|PubMed:19307596,
ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:19665017,
ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:20100835,
ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:21309750,
ECO:0000269|PubMed:21411625, ECO:0000269|PubMed:22888118,
ECO:0000269|PubMed:23564345, ECO:0000269|PubMed:7478590,
ECO:0000269|PubMed:8759729, ECO:0000269|PubMed:9584165,
ECO:0000269|PubMed:9924018}.
-!- SUBUNIT: (Microbial infection) Interacts with HEV ORF3 protein;
via the SH3 domain. {ECO:0000269|PubMed:11518702}.
-!- INTERACTION:
P00519:ABL1; NbExp=2; IntAct=EBI-621482, EBI-375543;
P42684:ABL2; NbExp=2; IntAct=EBI-621482, EBI-1102694;
P12814:ACTN1; NbExp=2; IntAct=EBI-621482, EBI-351710;
Q13444:ADAM15; NbExp=3; IntAct=EBI-621482, EBI-77818;
P07550:ADRB2; NbExp=3; IntAct=EBI-621482, EBI-491169;
P55196:AFDN; NbExp=7; IntAct=EBI-621482, EBI-365875;
P10275:AR; NbExp=7; IntAct=EBI-621482, EBI-608057;
Q8R5G7:Arap3 (xeno); NbExp=3; IntAct=EBI-621482, EBI-621463;
P49407:ARRB1; NbExp=3; IntAct=EBI-621482, EBI-743313;
P32121:ARRB2; NbExp=2; IntAct=EBI-621482, EBI-714559;
Q9ULH1:ASAP1; NbExp=3; IntAct=EBI-621482, EBI-346622;
P56945:BCAR1; NbExp=3; IntAct=EBI-621482, EBI-702093;
P22681:CBL; NbExp=8; IntAct=EBI-621482, EBI-518228;
Q9H5V8:CDCP1; NbExp=2; IntAct=EBI-621482, EBI-1019736;
P12830:CDH1; NbExp=2; IntAct=EBI-621482, EBI-727477;
P35222:CTNNB1; NbExp=2; IntAct=EBI-621482, EBI-491549;
P52800:Efnb2 (xeno); NbExp=2; IntAct=EBI-621482, EBI-1032676;
P00533:EGFR; NbExp=7; IntAct=EBI-621482, EBI-297353;
P04626:ERBB2; NbExp=11; IntAct=EBI-621482, EBI-641062;
P21860:ERBB3; NbExp=2; IntAct=EBI-621482, EBI-720706;
P03372:ESR1; NbExp=11; IntAct=EBI-621482, EBI-78473;
P03372-4:ESR1; NbExp=2; IntAct=EBI-621482, EBI-4309277;
P14921-1:ETS1; NbExp=2; IntAct=EBI-621482, EBI-913224;
P25445:FAS; NbExp=2; IntAct=EBI-621482, EBI-494743;
Q8NFZ0:FBXO18; NbExp=4; IntAct=EBI-621482, EBI-724767;
Q13480:GAB1; NbExp=12; IntAct=EBI-621482, EBI-517684;
P19367:HK1; NbExp=2; IntAct=EBI-621482, EBI-713162;
P61978:HNRNPK; NbExp=6; IntAct=EBI-621482, EBI-304185;
P97288:Htr4 (xeno); NbExp=2; IntAct=EBI-621482, EBI-7149283;
Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-621482, EBI-81279;
P35968:KDR; NbExp=2; IntAct=EBI-621482, EBI-1005487;
Q07666:KHDRBS1; NbExp=3; IntAct=EBI-621482, EBI-1364;
P10721:KIT; NbExp=5; IntAct=EBI-621482, EBI-1379503;
Q8TBB1:LNX1; NbExp=6; IntAct=EBI-621482, EBI-739832;
P07948:LYN; NbExp=2; IntAct=EBI-621482, EBI-79452;
Q9H204:MED28; NbExp=3; IntAct=EBI-621482, EBI-514199;
P08581:MET; NbExp=4; IntAct=EBI-621482, EBI-1039152;
Q13177:PAK2; NbExp=2; IntAct=EBI-621482, EBI-1045887;
P16284:PECAM1; NbExp=3; IntAct=EBI-621482, EBI-716404;
P27986:PIK3R1; NbExp=6; IntAct=EBI-621482, EBI-79464;
Q92569:PIK3R3; NbExp=3; IntAct=EBI-621482, EBI-79893;
Q05397:PTK2; NbExp=8; IntAct=EBI-621482, EBI-702142;
P34152:Ptk2 (xeno); NbExp=2; IntAct=EBI-621482, EBI-77070;
Q14289:PTK2B; NbExp=3; IntAct=EBI-621482, EBI-298640;
P18031:PTPN1; NbExp=14; IntAct=EBI-621482, EBI-968788;
Q16825:PTPN21; NbExp=2; IntAct=EBI-621482, EBI-2860264;
P18433:PTPRA; NbExp=4; IntAct=EBI-621482, EBI-2609645;
P18052:Ptpra (xeno); NbExp=3; IntAct=EBI-621482, EBI-6597520;
Q62884:Ptprj (xeno); NbExp=3; IntAct=EBI-621482, EBI-7459400;
Q13905:RAPGEF1; NbExp=2; IntAct=EBI-621482, EBI-976876;
Q01973:ROR1; NbExp=9; IntAct=EBI-621482, EBI-6082337;
P27635:RPL10; NbExp=6; IntAct=EBI-621482, EBI-352398;
O00560:SDCBP; NbExp=2; IntAct=EBI-621482, EBI-727004;
P35326:SPRR2A; NbExp=3; IntAct=EBI-621482, EBI-1047940;
Q9C0H9:SRCIN1; NbExp=3; IntAct=EBI-621482, EBI-1393949;
Q68CZ2:TNS3; NbExp=13; IntAct=EBI-621482, EBI-1220488;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7525268}.
Mitochondrion inner membrane {ECO:0000269|PubMed:12615910}.
Nucleus {ECO:0000269|PubMed:7853507}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:7525268}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:19307596}. Note=Localizes to focal adhesion
sites following integrin engagement. Localization to focal
adhesion sites requires myristoylation and the SH3 domain
(PubMed:7525268). Colocalizes with PDLIM4 at the perinuclear
region, but not at focal adhesions (PubMed:19307596).
{ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:7525268}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P12931-1; Sequence=Displayed;
Name=2;
IsoId=P12931-2; Sequence=VSP_012134;
-!- TISSUE SPECIFICITY: Expressed ubiquitously. Platelets, neurons and
osteoclasts express 5-fold to 200-fold higher levels than most
other tissues.
-!- DOMAIN: The SH2 and SH3 domains are important for the
intramolecular and intermolecular interactions that regulate
catalytic activity, localization, and substrate recruitment.
-!- PTM: Myristoylated at Gly-2, and this is essential for targeting
to membranes. {ECO:0000269|PubMed:7525268}.
-!- PTM: Dephosphorylated at Tyr-530 by PTPRJ (By similarity).
Phosphorylated on Tyr-530 by c-Src kinase (CSK). The
phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ
at Tyr-419. Normally maintained in an inactive conformation with
the SH2 domain engaged with Tyr-530, the SH3 domain engaged with
the SH2-kinase linker, and Tyr-419 dephosphorylated.
Dephosphorylation of Tyr-530 as a result of protein tyrosine
phosphatase (PTP) action disrupts the intramolecular interaction
between the SH2 domain and Tyr-530, Tyr-419 can then become
autophosphorylated, resulting in SRC activation. Phosphorylation
of Tyr-530 by CSK allows this interaction to reform, resulting in
SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets
SRC to ubiquitin-dependent degradation and thus leads to
cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this
enhances kinase activity. Phosphorylated by PTK2B/PYK2; this
enhances kinase activity. {ECO:0000250,
ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18936167,
ECO:0000269|PubMed:21442427, ECO:0000269|PubMed:22888118,
ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:7525268}.
-!- PTM: S-nitrosylation is important for activation of its kinase
activity. {ECO:0000250}.
-!- PTM: Ubiquitinated in response to CDK5-mediated phosphorylation.
Ubiquitination mediated by CBLC requires SRC autophosphorylation
at Tyr-419 and may lead to lysosomal degradation.
{ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18936167,
ECO:0000269|PubMed:22888118, ECO:0000269|PubMed:6273838}.
-!- DISEASE: Note=SRC kinase activity has been shown to be increased
in several tumor tissues and tumor cell lines such as colon
carcinoma cells. {ECO:0000269|PubMed:2498394,
ECO:0000269|PubMed:3093483}.
-!- DISEASE: Thrombocytopenia 6 (THC6) [MIM:616937]: A form of
thrombocytopenia, a hematologic disorder defined by a decrease in
the number of platelets in circulating blood, resulting in the
potential for increased bleeding and decreased ability for
clotting. THC6 is an autosomal dominant form. Affected individuals
may also have bone abnormalities and an increased risk for
myelofibrosis. {ECO:0000269|PubMed:26936507}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SRCID448ch20q11.html";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AL133293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW76065.1; -; Genomic_DNA.
EMBL; CH471077; EAW76064.1; -; Genomic_DNA.
EMBL; CH471077; EAW76066.1; -; Genomic_DNA.
EMBL; CH471077; EAW76067.1; -; Genomic_DNA.
EMBL; BC011566; AAH11566.1; -; mRNA.
EMBL; BC051270; AAH51270.2; -; mRNA.
EMBL; K03218; AAA60584.1; -; Genomic_DNA.
EMBL; M16237; AAA60584.1; JOINED; Genomic_DNA.
EMBL; M16243; AAA60584.1; JOINED; Genomic_DNA.
EMBL; M16244; AAA60584.1; JOINED; Genomic_DNA.
EMBL; M16245; AAA60584.1; JOINED; Genomic_DNA.
EMBL; K03212; AAA60584.1; JOINED; Genomic_DNA.
EMBL; K03213; AAA60584.1; JOINED; Genomic_DNA.
EMBL; K03214; AAA60584.1; JOINED; Genomic_DNA.
EMBL; K03215; AAA60584.1; JOINED; Genomic_DNA.
EMBL; K03216; AAA60584.1; JOINED; Genomic_DNA.
EMBL; K03217; AAA60584.1; JOINED; Genomic_DNA.
EMBL; X02647; CAA26485.1; -; Genomic_DNA.
EMBL; X03995; CAA26485.1; JOINED; Genomic_DNA.
EMBL; X03996; CAA26485.1; JOINED; Genomic_DNA.
EMBL; X03997; CAA26485.1; JOINED; Genomic_DNA.
EMBL; X03998; CAA26485.1; JOINED; Genomic_DNA.
EMBL; X03999; CAA26485.1; JOINED; Genomic_DNA.
EMBL; X04000; CAA26485.1; JOINED; Genomic_DNA.
CCDS; CCDS13294.1; -. [P12931-1]
PIR; A26891; TVHUSC.
RefSeq; NP_005408.1; NM_005417.4. [P12931-1]
RefSeq; NP_938033.1; NM_198291.2. [P12931-1]
RefSeq; XP_011527315.1; XM_011529013.2. [P12931-1]
RefSeq; XP_016883513.1; XM_017028024.1. [P12931-2]
RefSeq; XP_016883514.1; XM_017028025.1. [P12931-2]
RefSeq; XP_016883515.1; XM_017028026.1. [P12931-2]
RefSeq; XP_016883516.1; XM_017028027.1. [P12931-2]
UniGene; Hs.195659; -.
PDB; 1A07; X-ray; 2.20 A; A/B=144-249.
PDB; 1A08; X-ray; 2.20 A; A/B=144-249.
PDB; 1A09; X-ray; 2.00 A; A/B=144-249.
PDB; 1A1A; X-ray; 2.00 A; A/B=144-249.
PDB; 1A1B; X-ray; 2.20 A; A/B=144-249.
PDB; 1A1C; X-ray; 2.40 A; A/B=144-249.
PDB; 1A1E; X-ray; 2.20 A; A/B=144-249.
PDB; 1FMK; X-ray; 1.50 A; A=86-536.
PDB; 1HCS; NMR; -; B=144-249.
PDB; 1HCT; NMR; -; B=144-249.
PDB; 1KSW; X-ray; 2.80 A; A=86-536.
PDB; 1O41; X-ray; 1.70 A; A=145-252.
PDB; 1O42; X-ray; 1.70 A; A=145-252.
PDB; 1O43; X-ray; 1.50 A; A=145-252.
PDB; 1O44; X-ray; 1.70 A; A=145-252.
PDB; 1O45; X-ray; 1.80 A; A=145-252.
PDB; 1O46; X-ray; 2.00 A; A=145-252.
PDB; 1O47; X-ray; 1.80 A; A=145-252.
PDB; 1O48; X-ray; 1.55 A; A=145-252.
PDB; 1O49; X-ray; 1.70 A; A=145-252.
PDB; 1O4A; X-ray; 1.50 A; A=145-252.
PDB; 1O4B; X-ray; 1.85 A; A=145-252.
PDB; 1O4C; X-ray; 1.80 A; A=145-252.
PDB; 1O4D; X-ray; 1.85 A; A=145-252.
PDB; 1O4E; X-ray; 2.00 A; A=145-252.
PDB; 1O4F; X-ray; 2.00 A; A=145-252.
PDB; 1O4G; X-ray; 1.55 A; A=145-252.
PDB; 1O4H; X-ray; 2.25 A; A=145-252.
PDB; 1O4I; X-ray; 1.75 A; A=145-252.
PDB; 1O4J; X-ray; 1.70 A; A=145-252.
PDB; 1O4K; X-ray; 1.57 A; A=145-252.
PDB; 1O4L; X-ray; 1.65 A; A=145-252.
PDB; 1O4M; X-ray; 1.60 A; A=145-252.
PDB; 1O4N; X-ray; 1.60 A; A=145-252.
PDB; 1O4O; X-ray; 1.70 A; A=145-252.
PDB; 1O4P; X-ray; 1.90 A; A=145-252.
PDB; 1O4Q; X-ray; 1.70 A; A=145-252.
PDB; 1O4R; X-ray; 1.50 A; A=145-252.
PDB; 1SHD; X-ray; 2.00 A; A=144-249.
PDB; 1Y57; X-ray; 1.91 A; A=86-536.
PDB; 1YI6; X-ray; 2.00 A; A/B=261-536.
PDB; 1YOJ; X-ray; 1.95 A; A/B=254-536.
PDB; 1YOL; X-ray; 2.30 A; A/B=254-536.
PDB; 1YOM; X-ray; 2.90 A; A/B=254-536.
PDB; 2BDF; X-ray; 2.10 A; A/B=258-536.
PDB; 2BDJ; X-ray; 2.50 A; A=258-536.
PDB; 2H8H; X-ray; 2.20 A; A=2-536.
PDB; 2SRC; X-ray; 1.50 A; A=86-536.
PDB; 3VRO; X-ray; 1.80 A; B=412-424.
PDB; 3ZMP; X-ray; 2.62 A; C/D=527-536.
PDB; 3ZMQ; X-ray; 3.30 A; C=527-536.
PDB; 4F59; X-ray; 1.71 A; A=144-252.
PDB; 4F5A; X-ray; 1.80 A; A=144-252.
PDB; 4F5B; X-ray; 1.57 A; A=144-252.
PDB; 4HXJ; X-ray; 2.00 A; A/B=87-144.
PDB; 4K11; X-ray; 2.30 A; A=87-534.
PDB; 4MXO; X-ray; 2.10 A; A/B=254-536.
PDB; 4MXX; X-ray; 2.60 A; A/B=254-536.
PDB; 4MXY; X-ray; 2.58 A; A/B=254-536.
PDB; 4MXZ; X-ray; 2.58 A; A/B=254-536.
PDBsum; 1A07; -.
PDBsum; 1A08; -.
PDBsum; 1A09; -.
PDBsum; 1A1A; -.
PDBsum; 1A1B; -.
PDBsum; 1A1C; -.
PDBsum; 1A1E; -.
PDBsum; 1FMK; -.
PDBsum; 1HCS; -.
PDBsum; 1HCT; -.
PDBsum; 1KSW; -.
PDBsum; 1O41; -.
PDBsum; 1O42; -.
PDBsum; 1O43; -.
PDBsum; 1O44; -.
PDBsum; 1O45; -.
PDBsum; 1O46; -.
PDBsum; 1O47; -.
PDBsum; 1O48; -.
PDBsum; 1O49; -.
PDBsum; 1O4A; -.
PDBsum; 1O4B; -.
PDBsum; 1O4C; -.
PDBsum; 1O4D; -.
PDBsum; 1O4E; -.
PDBsum; 1O4F; -.
PDBsum; 1O4G; -.
PDBsum; 1O4H; -.
PDBsum; 1O4I; -.
PDBsum; 1O4J; -.
PDBsum; 1O4K; -.
PDBsum; 1O4L; -.
PDBsum; 1O4M; -.
PDBsum; 1O4N; -.
PDBsum; 1O4O; -.
PDBsum; 1O4P; -.
PDBsum; 1O4Q; -.
PDBsum; 1O4R; -.
PDBsum; 1SHD; -.
PDBsum; 1Y57; -.
PDBsum; 1YI6; -.
PDBsum; 1YOJ; -.
PDBsum; 1YOL; -.
PDBsum; 1YOM; -.
PDBsum; 2BDF; -.
PDBsum; 2BDJ; -.
PDBsum; 2H8H; -.
PDBsum; 2SRC; -.
PDBsum; 3VRO; -.
PDBsum; 3ZMP; -.
PDBsum; 3ZMQ; -.
PDBsum; 4F59; -.
PDBsum; 4F5A; -.
PDBsum; 4F5B; -.
PDBsum; 4HXJ; -.
PDBsum; 4K11; -.
PDBsum; 4MXO; -.
PDBsum; 4MXX; -.
PDBsum; 4MXY; -.
PDBsum; 4MXZ; -.
ProteinModelPortal; P12931; -.
SMR; P12931; -.
BioGrid; 112592; 284.
CORUM; P12931; -.
DIP; DIP-1059N; -.
ELM; P12931; -.
IntAct; P12931; 206.
MINT; MINT-93621; -.
STRING; 9606.ENSP00000350941; -.
BindingDB; P12931; -.
ChEMBL; CHEMBL267; -.
DrugBank; DB08564; (2E)-N-{4-[(3-bromophenyl)amino]quinazolin-6-yl}-4-(dimethylamino)but-2-enamide.
DrugBank; DB06882; 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-naphthalen-1-ylurea.
DrugBank; DB06883; 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-phenylurea.
DrugBank; DB08192; 2-(4-CARCOXY-5-ISOPROPYLTHIAZOLYL)BENZOPIPERIDINE.
DrugBank; DB04739; 4-[(4-METHYL-1-PIPERAZINYL)METHYL]-N-[3-[[4-(3-PYRIDINYL)-2-PYRIMIDINYL]AMINO]PHENYL]-BENZAMIDE.
DrugBank; DB07966; [4-({4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]quinazolin-2-yl}amino)phenyl]acetonitrile.
DrugBank; DB06616; Bosutinib.
DrugBank; DB04272; Citric Acid.
DrugBank; DB01254; Dasatinib.
DrugBank; DB03217; DPI59.
DrugBank; DB03628; ISO24.
DrugBank; DB02175; Malonic acid.
DrugBank; DB08462; N-(4-PHENYLAMINO-QUINAZOLIN-6-YL)-ACRYLAMIDE.
DrugBank; DB07662; N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE.
DrugBank; DB01893; N6-Benzyl Adenosine-5'-Diphosphate.
DrugBank; DB09079; Nintedanib.
DrugBank; DB03902; Oxalic Acid.
DrugBank; DB03114; PAS219.
DrugBank; DB03078; PASBN.
DrugBank; DB03298; Phenylphosphate.
DrugBank; DB01962; Phosphonotyrosine.
DrugBank; DB08901; Ponatinib.
DrugBank; DB04751; Purvalanol A.
DrugBank; DB04080; RU78191.
DrugBank; DB01947; RU78262.
DrugBank; DB03828; RU78299.
DrugBank; DB03306; RU78300.
DrugBank; DB02908; RU78783.
DrugBank; DB02762; RU79072.
DrugBank; DB03525; RU79073.
DrugBank; DB01866; RU79256.
DrugBank; DB04495; RU81843.
DrugBank; DB03104; RU82129.
DrugBank; DB03268; RU82197.
DrugBank; DB03591; RU82209.
DrugBank; DB02336; RU83876.
DrugBank; DB01678; RU84687.
DrugBank; DB03712; RU85053.
DrugBank; DB01908; RU85493.
DrugBank; DB02432; RU90395.
DrugBank; DB05184; XL228.
GuidetoPHARMACOLOGY; 2206; -.
iPTMnet; P12931; -.
PhosphoSitePlus; P12931; -.
SwissPalm; P12931; -.
DMDM; 125711; -.
OGP; P12931; -.
EPD; P12931; -.
MaxQB; P12931; -.
PaxDb; P12931; -.
PeptideAtlas; P12931; -.
PRIDE; P12931; -.
DNASU; 6714; -.
Ensembl; ENST00000358208; ENSP00000350941; ENSG00000197122. [P12931-1]
Ensembl; ENST00000373558; ENSP00000362659; ENSG00000197122. [P12931-2]
Ensembl; ENST00000373567; ENSP00000362668; ENSG00000197122. [P12931-1]
Ensembl; ENST00000373578; ENSP00000362680; ENSG00000197122. [P12931-1]
GeneID; 6714; -.
KEGG; hsa:6714; -.
UCSC; uc002xgy.5; human. [P12931-1]
CTD; 6714; -.
DisGeNET; 6714; -.
EuPathDB; HostDB:ENSG00000197122.11; -.
GeneCards; SRC; -.
HGNC; HGNC:11283; SRC.
HPA; CAB004023; -.
HPA; HPA030875; -.
MalaCards; SRC; -.
MIM; 190090; gene.
MIM; 616937; phenotype.
neXtProt; NX_P12931; -.
OpenTargets; ENSG00000197122; -.
PharmGKB; PA36111; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P12931; -.
KO; K05704; -.
OMA; CQCWRKD; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P12931; -.
TreeFam; TF351634; -.
BioCyc; MetaCyc:HS02256-MONOMER; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-1227986; Signaling by ERBB2.
Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-177929; Signaling by EGFR.
Reactome; R-HSA-180292; GAB1 signalosome.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-191647; c-src mediated regulation of Cx43 function and closure of gap junctions.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-389356; CD28 co-stimulation.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-391160; Signal regulatory protein family interactions.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-3928664; Ephrin signaling.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-HSA-418885; DCC mediated attractive signaling.
Reactome; R-HSA-418886; Netrin mediated repulsion signals.
Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells.
Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-HSA-8934903; Receptor Mediated Mitophagy.
Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
SignaLink; P12931; -.
SIGNOR; P12931; -.
ChiTaRS; SRC; human.
EvolutionaryTrace; P12931; -.
GeneWiki; Src_(gene); -.
GenomeRNAi; 6714; -.
PMAP-CutDB; P12931; -.
PRO; PR:P12931; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000197122; -.
CleanEx; HS_SRC; -.
Genevisible; P12931; HS.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0005901; C:caveola; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0002102; C:podosome; IEA:Ensembl.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0071253; F:connexin binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IEA:Ensembl.
GO; GO:0070851; F:growth factor receptor binding; IPI:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0051427; F:hormone receptor binding; IBA:GO_Central.
GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; TAS:BHF-UCL.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; TAS:BHF-UCL.
GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
GO; GO:0034332; P:adherens junction organization; IEA:Ensembl.
GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; ISS:BHF-UCL.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0045453; P:bone resorption; ISS:UniProtKB.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISS:BHF-UCL.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
GO; GO:0071393; P:cellular response to progesterone stimulus; ISS:BHF-UCL.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0035635; P:entry of bacterium into host cell; TAS:Reactome.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IDA:BHF-UCL.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:BHF-UCL.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IMP:UniProtKB.
GO; GO:0032463; P:negative regulation of protein homooligomerization; IMP:UniProtKB.
GO; GO:0051974; P:negative regulation of telomerase activity; IMP:BHF-UCL.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
GO; GO:0048477; P:oogenesis; IEA:Ensembl.
GO; GO:0036035; P:osteoclast development; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IEA:Ensembl.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0033625; P:positive regulation of integrin activation; TAS:BHF-UCL.
GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IMP:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:2000386; P:positive regulation of ovarian follicle development; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IC:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0010954; P:positive regulation of protein processing; IEA:Ensembl.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IMP:ParkinsonsUK-UCL.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0001545; P:primary ovarian follicle growth; IEA:Ensembl.
GO; GO:0050847; P:progesterone receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0045124; P:regulation of bone resorption; TAS:BHF-UCL.
GO; GO:2001286; P:regulation of caveolin-mediated endocytosis; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
GO; GO:0060491; P:regulation of cell projection assembly; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:UniProtKB.
GO; GO:2000641; P:regulation of early endosome to late endosome transport; IMP:UniProtKB.
GO; GO:0010632; P:regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
GO; GO:0071801; P:regulation of podosome assembly; IBA:GO_Central.
GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
GO; GO:0043114; P:regulation of vascular permeability; TAS:BHF-UCL.
GO; GO:0010447; P:response to acidic pH; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0051385; P:response to mineralocorticoid; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IEA:Ensembl.
GO; GO:0007172; P:signal complex assembly; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0045056; P:transcytosis; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:0060065; P:uterus development; IEA:Ensembl.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell adhesion;
Cell cycle; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Host-virus interaction; Immunity; Kinase;
Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed.
CHAIN 2 536 Proto-oncogene tyrosine-protein kinase
Src.
/FTId=PRO_0000088141.
DOMAIN 84 145 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 151 248 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 270 523 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 276 284 ATP.
ACT_SITE 389 389 Proton acceptor.
BINDING 298 298 ATP.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000269|PubMed:7929427}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000269|PubMed:7929427}.
MOD_RES 74 74 Phosphothreonine.
{ECO:0000269|PubMed:7929427}.
MOD_RES 75 75 Phosphoserine; by CDK5.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21442427}.
MOD_RES 187 187 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05480}.
MOD_RES 419 419 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14661060,
ECO:0000269|PubMed:18936167,
ECO:0000269|PubMed:19307596,
ECO:0000269|PubMed:26936507,
ECO:0000269|PubMed:6273838}.
MOD_RES 419 419 Phosphotyrosine; by FAK2. {ECO:0000250}.
MOD_RES 439 439 Phosphotyrosine.
{ECO:0000269|PubMed:7929427}.
MOD_RES 511 511 Phosphothreonine.
{ECO:0000269|PubMed:7929427}.
MOD_RES 522 522 Phosphotyrosine.
{ECO:0000269|PubMed:7929427}.
MOD_RES 530 530 Phosphotyrosine; by CSK.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:19307596,
ECO:0000269|PubMed:26936507,
ECO:0000269|PubMed:7525268}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:7525268}.
VAR_SEQ 117 117 T -> TRKVDVR (in isoform 2).
{ECO:0000303|PubMed:2681803}.
/FTId=VSP_012134.
VARIANT 176 176 L -> F (in dbSNP:rs6018260).
/FTId=VAR_051699.
VARIANT 237 237 A -> T (in dbSNP:rs34881773).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041830.
VARIANT 527 527 E -> K (in THC6; increased protein
tyrosine kinase activity; increased
autophosphorylation at Y-419; causes
defective megakaryopoiesis associated
with increased overall tyrosine
phosphorylation in megakaryocytes;
dbSNP:rs879255268).
{ECO:0000269|PubMed:26936507}.
/FTId=VAR_076919.
MUTAGEN 298 298 K->M: Kinase inactive. Abolishes
ubiquitination promoted by CBLC.
{ECO:0000269|PubMed:14661060}.
MUTAGEN 302 302 P->E: Kinase active. Interacts with
PDLIM4; when associated with E-307 and F-
419. {ECO:0000269|PubMed:19307596}.
MUTAGEN 307 307 P->E: Kinase active. Interacts with
PDLIM4; when associated with E-302 and F-
419. {ECO:0000269|PubMed:19307596}.
MUTAGEN 419 419 Y->F: Loss of kinase activity. Loss of
interaction with PDLIM4.
{ECO:0000269|PubMed:19307596}.
STRAND 87 93 {ECO:0000244|PDB:1FMK}.
STRAND 99 102 {ECO:0000244|PDB:1FMK}.
STRAND 110 114 {ECO:0000244|PDB:1FMK}.
STRAND 118 126 {ECO:0000244|PDB:1FMK}.
TURN 127 129 {ECO:0000244|PDB:1FMK}.
STRAND 132 136 {ECO:0000244|PDB:1FMK}.
HELIX 137 139 {ECO:0000244|PDB:1FMK}.
STRAND 140 142 {ECO:0000244|PDB:1FMK}.
HELIX 146 148 {ECO:0000244|PDB:1FMK}.
STRAND 152 154 {ECO:0000244|PDB:1FMK}.
HELIX 158 165 {ECO:0000244|PDB:1FMK}.
STRAND 167 170 {ECO:0000244|PDB:1SHD}.
STRAND 174 179 {ECO:0000244|PDB:1FMK}.
STRAND 181 183 {ECO:0000244|PDB:1FMK}.
STRAND 187 195 {ECO:0000244|PDB:1FMK}.
TURN 196 198 {ECO:0000244|PDB:1FMK}.
STRAND 199 209 {ECO:0000244|PDB:1FMK}.
STRAND 211 213 {ECO:0000244|PDB:2SRC}.
STRAND 215 218 {ECO:0000244|PDB:1FMK}.
STRAND 221 225 {ECO:0000244|PDB:1FMK}.
HELIX 226 233 {ECO:0000244|PDB:1FMK}.
STRAND 240 242 {ECO:0000244|PDB:1FMK}.
STRAND 256 259 {ECO:0000244|PDB:1FMK}.
HELIX 267 269 {ECO:0000244|PDB:1FMK}.
STRAND 270 278 {ECO:0000244|PDB:1FMK}.
STRAND 283 289 {ECO:0000244|PDB:1FMK}.
TURN 290 292 {ECO:0000244|PDB:1FMK}.
STRAND 293 299 {ECO:0000244|PDB:1FMK}.
TURN 302 304 {ECO:0000244|PDB:2BDF}.
HELIX 307 319 {ECO:0000244|PDB:1FMK}.
STRAND 328 332 {ECO:0000244|PDB:1FMK}.
STRAND 334 336 {ECO:0000244|PDB:1FMK}.
STRAND 338 341 {ECO:0000244|PDB:1FMK}.
HELIX 349 353 {ECO:0000244|PDB:1FMK}.
HELIX 355 358 {ECO:0000244|PDB:1FMK}.
HELIX 363 382 {ECO:0000244|PDB:1FMK}.
HELIX 392 394 {ECO:0000244|PDB:1FMK}.
STRAND 395 397 {ECO:0000244|PDB:1FMK}.
HELIX 399 401 {ECO:0000244|PDB:1FMK}.
STRAND 403 405 {ECO:0000244|PDB:1FMK}.
HELIX 410 413 {ECO:0000244|PDB:2SRC}.
HELIX 417 420 {ECO:0000244|PDB:2SRC}.
TURN 423 426 {ECO:0000244|PDB:1Y57}.
HELIX 429 431 {ECO:0000244|PDB:1FMK}.
HELIX 434 439 {ECO:0000244|PDB:1FMK}.
HELIX 444 459 {ECO:0000244|PDB:1FMK}.
TURN 460 462 {ECO:0000244|PDB:1FMK}.
HELIX 471 479 {ECO:0000244|PDB:1FMK}.
HELIX 492 501 {ECO:0000244|PDB:1FMK}.
HELIX 506 508 {ECO:0000244|PDB:1FMK}.
HELIX 512 520 {ECO:0000244|PDB:1FMK}.
TURN 521 523 {ECO:0000244|PDB:1FMK}.
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


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