[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185 (ISOFORM 1).
PubMed=3299057 [NCBI, ExPASy, EBI, Israel, Japan]
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).
|
[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-536 (ISOFORM 1).
PubMed=2582238 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[5]
|
NUCLEOTIDE SEQUENCE [MRNA] OF 98-139 (ISOFORM 2).
DOI=10.1002/jnr.490240113; PubMed=2681803 [NCBI, ExPASy, EBI, Israel, Japan]
Pyper J.M.,
Bolen J.B.;
"Neuron-specific splicing of C-SRC RNA in human brain.";
J. Neurosci. Res. 24:89-96(1989).
|
[6]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-536 (ISOFORM 1).
PubMed=2581127 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[7]
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ALTERNATIVE SPLICING.
PubMed=1691439 [NCBI, ExPASy, EBI, Israel, Japan]
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).
|
[8]
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INTERACTION WITH RALGPS1.
DOI=10.1074/jbc.C000085200; PubMed=10747847 [NCBI, ExPASy, EBI, Israel, Japan]
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).
|
[9]
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INTERACTION WITH MUC1.
DOI=10.1074/jbc.C000754200; PubMed=11152665 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[10]
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INTERACTION WITH HEV ORF3 PROTEIN.
DOI=10.1074/jbc.M101546200; PubMed=11518702 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[11]
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INTERACTION WITH PELP1.
DOI=10.1073/pnas.192569699; PubMed=12415108 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[12]
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INTERACTION WITH CDCP1.
DOI=10.1016/j.cell.2005.02.019; PubMed=15851033 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[13]
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INTERACTION WITH TOM1L2.
DOI=10.1128/MCB.26.5.1932-1947.2006; PubMed=16479011 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[14]
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INTERACTION WITH TGFB1I1.
DOI=10.1159/000098402; PubMed=17202804 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[15]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND MASS SPECTROMETRY.
TISSUE=Lung;
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K.,
Guo A.,
Zeng Q.,
Possemato A.,
Yu J.,
Haack H.,
Nardone J.,
Lee K.,
Reeves C.,
Li Y.,
Hu Y.,
Tan Z.,
Stokes M.,
Sullivan L.,
Mitchell J.,
Wetzel R.,
Macneill J.,
Ren J.M.,
Yuan J., ![]()
Bakalarski C.E.,
Villen J.,
Kornhauser J.M.,
Smith B.,
Li D.,
Zhou X.,
Gygi S.P.,
Gu T.-L.,
Polakiewicz R.D.,
Rush J.,
Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
|
[16]
|
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-69; SER-75 AND TYR-419, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J.,
Jaensch L.,
Nimtz M.,
Dieterich G.,
Hornberger R.,
Keri G.,
Wehland J.,
Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
|
[17]
|
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-74 AND TYR-419, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
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).
|
[18]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[19]
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X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 86-536.
DOI=10.1038/385595a0; PubMed=9024657 [NCBI, ExPASy, EBI, Israel, Japan]
Xu W.,
Harrison S.C.,
Eck M.J.;
"Three-dimensional structure of the tyrosine kinase c-Src.";
Nature 385:595-602(1997).
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[20]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 145-249.
DOI=10.1021/bi970019n; PubMed=9174343 [NCBI, ExPASy, EBI, Israel, Japan]
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).
|
[21]
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STRUCTURE BY NMR OF 204-249.
DOI=10.1021/bi00007a003; PubMed=7532003 [NCBI, ExPASy, EBI, Israel, Japan]
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).
|
[22]
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VARIANT [LARGE SCALE ANALYSIS] THR-237.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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|
- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
- SUBUNIT: Interacts with DDEF1/ASAP1; via the SH3 domain. Interacts with CCPG1 (By similarity). Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2. Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin. Interacts with RALGPS1; via the SH3 domain. Interacts with HEV ORF3 protein; via the SH3 domain.
- INTERACTION:
P00519:ABL1; NbExp=1; IntAct=EBI-621482, EBI-375543;
P42684:ABL2; NbExp=1; IntAct=EBI-621482, EBI-1102694;
Q15027:ACAP1; NbExp=1; IntAct=EBI-621482, EBI-751746;
P12814:ACTN1; NbExp=2; IntAct=EBI-621482, EBI-351710;
O43918:AIRE; NbExp=1; IntAct=EBI-621482, EBI-1753081;
Q9Y2D5:AKAP2; NbExp=1; IntAct=EBI-621482, EBI-1754555;
Q13023:AKAP6; NbExp=1; IntAct=EBI-621482, EBI-1056102;
Q96Q35:ALS2CR12; NbExp=1; IntAct=EBI-621482, EBI-1755548;
Q9BWW9:APOL5; NbExp=1; IntAct=EBI-621482, EBI-1753592;
Q8R5G7:Arap3 (xeno); NbExp=3; IntAct=EBI-621482, EBI-621463;
Q9ULH1:ASAP1; NbExp=1; IntAct=EBI-621482, EBI-346622;
O43150:ASAP2; NbExp=1; IntAct=EBI-621482, EBI-310968;
Q96NS5:ASB16; NbExp=1; IntAct=EBI-621482, EBI-1751918;
Q63767:Bcar1 (xeno); NbExp=1; IntAct=EBI-621482, EBI-1176801;
P20810:CAST; NbExp=1; IntAct=EBI-621482, EBI-1268770;
P48960:CD97; NbExp=1; IntAct=EBI-621482, EBI-1756009;
P46527:CDKN1B; NbExp=1; IntAct=EBI-621482, EBI-519280;
Q9HCU4:CELSR2; NbExp=1; IntAct=EBI-621482, EBI-724117;
Q14008:CKAP5; NbExp=1; IntAct=EBI-621482, EBI-310585;
Q8IWT3:CUL9; NbExp=1; IntAct=EBI-621482, EBI-311123;
P78329:CYP4F2; NbExp=1; IntAct=EBI-621482, EBI-1752413;
Q14118:DAG1; NbExp=1; IntAct=EBI-621482, EBI-1755945;
O14490:DLGAP1; NbExp=1; IntAct=EBI-621482, EBI-1753207;
Q9P1A6:DLGAP2; NbExp=1; IntAct=EBI-621482, EBI-1753397;
O95886:DLGAP3; NbExp=1; IntAct=EBI-621482, EBI-1752541;
Q9Y2H0:DLGAP4; NbExp=1; IntAct=EBI-621482, EBI-722139;
Q92988:DLX4; NbExp=1; IntAct=EBI-621482, EBI-1752755;
Q14185:DOCK1; NbExp=1; IntAct=EBI-621482, EBI-446740;
Q8IZD9:DOCK3; NbExp=1; IntAct=EBI-621482, EBI-1752361;
Q9H1R2:DUSP15; NbExp=1; IntAct=EBI-621482, EBI-1752795;
O43281:EFS; NbExp=1; IntAct=EBI-621482, EBI-718488;
O15371:EIF3D; NbExp=1; IntAct=EBI-621482, EBI-353818;
Q9Y2J2:EPB41L3; NbExp=1; IntAct=EBI-621482, EBI-310986;
O43909:EXTL3; NbExp=1; IntAct=EBI-621482, EBI-1754679;
O00254:F2RL2; NbExp=1; IntAct=EBI-621482, EBI-1751853;
O15360:FANCA; NbExp=1; IntAct=EBI-621482, EBI-81570;
P25445:FAS; NbExp=2; IntAct=EBI-621482, EBI-494743;
P31994:FCGR2B; NbExp=1; IntAct=EBI-621482, EBI-724784;
P31995:FCGR2C; NbExp=1; IntAct=EBI-621482, EBI-1396036;
Q9NZM4:GLTSCR1; NbExp=1; IntAct=EBI-621482, EBI-1754943;
P15586:GNS; NbExp=1; IntAct=EBI-621482, EBI-1752200;
Q9UL51:HCN2; NbExp=1; IntAct=EBI-621482, EBI-1751885;
P31273:HOXC8; NbExp=1; IntAct=EBI-621482, EBI-1752118;
P47928:ID4; NbExp=1; IntAct=EBI-621482, EBI-1754719;
Q9Y6K9:IKBKG; NbExp=1; IntAct=EBI-621482, EBI-81279;
Q9H9L3:ISG20L2; NbExp=1; IntAct=EBI-621482, EBI-751335;
Q60749:Khdrbs1 (xeno); NbExp=1; IntAct=EBI-621482, EBI-519077;
Q86X10:KIAA1219; NbExp=1; IntAct=EBI-621482, EBI-1755842;
P49916:LIG3; NbExp=1; IntAct=EBI-621482, EBI-1753381;
Q92918:MAP4K1; NbExp=1; IntAct=EBI-621482, EBI-881;
Q9H204:MED28; NbExp=1; IntAct=EBI-621482, EBI-514199;
Q9NQ76:MEPE; NbExp=1; IntAct=EBI-621482, EBI-1753293;
P46013:MKI67; NbExp=1; IntAct=EBI-621482, EBI-876367;
P43699:NKX2-1; NbExp=1; IntAct=EBI-621482, EBI-1391923;
O95157:NXPH3; NbExp=1; IntAct=EBI-621482, EBI-1752913;
P20774:OGN; NbExp=1; IntAct=EBI-621482, EBI-1753690;
P23760:PAX3; NbExp=1; IntAct=EBI-621482, EBI-1167564;
P23759:PAX7; NbExp=1; IntAct=EBI-621482, EBI-1042757;
Q13087:PDIA2; NbExp=1; IntAct=EBI-621482, EBI-1752525;
P16284:PECAM1; NbExp=1; IntAct=EBI-621482, EBI-716404;
O75167:PHACTR2; NbExp=1; IntAct=EBI-621482, EBI-1754409;
P28340:POLD1; NbExp=1; IntAct=EBI-621482, EBI-716569;
O43900:PRICKLE3; NbExp=1; IntAct=EBI-621482, EBI-1751761;
Q05397:PTK2; NbExp=1; IntAct=EBI-621482, EBI-702142;
Q13905:RAPGEF1; NbExp=1; IntAct=EBI-621482, EBI-976876;
Q8TB24:RIN3; NbExp=1; IntAct=EBI-621482, EBI-1570523;
P26373:RPL13; NbExp=1; IntAct=EBI-621482, EBI-356849;
P78345:RPP38; NbExp=1; IntAct=EBI-621482, EBI-366493;
P10301:RRAS; NbExp=1; IntAct=EBI-621482, EBI-968703;
Q9NQC3:RTN4; NbExp=1; IntAct=EBI-621482, EBI-715945;
Q9NZV5:SEPN1; NbExp=1; IntAct=EBI-621482, EBI-1751965;
Q9UPX8:SHANK2; NbExp=1; IntAct=EBI-621482, EBI-1570571;
Q9BYB0:SHANK3; NbExp=1; IntAct=EBI-621482, EBI-1752330;
Q13796:SHROOM2; NbExp=1; IntAct=EBI-621482, EBI-1644065;
Q15036:SNX17; NbExp=1; IntAct=EBI-621482, EBI-1752620;
O60493:SNX3; NbExp=1; IntAct=EBI-621482, EBI-727209;
Q07889:SOS1; NbExp=1; IntAct=EBI-621482, EBI-297487;
Q07890:SOS2; NbExp=1; IntAct=EBI-621482, EBI-298181;
P08047:SP1; NbExp=1; IntAct=EBI-621482, EBI-298336;
P42227:Stat3 (xeno); NbExp=1; IntAct=EBI-621482, EBI-602878;
Q9NRJ4:TULP4; NbExp=1; IntAct=EBI-621482, EBI-1753487;
Q05996:ZP2; NbExp=1; IntAct=EBI-621482, EBI-1755919;
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
|
| Name | 2 |
| Isoform ID | P12931-2 |
| Features which should be applied to build the isoform sequence: VSP_012134. |
|
|
- PTM: Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. The phosphorylated tail interacts with the SH2 domain thereby repressing kinase activity.
- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.
- SIMILARITY: Contains 1 protein kinase domain.
- SIMILARITY: Contains 1 SH2 domain.
- SIMILARITY: Contains 1 SH3 domain.
|
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