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UniProtKB/Swiss-Prot entry P12931


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SRC_HUMAN
Primary accession number P12931
Secondary accession numbers Q86VB9 Q9H5A8
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 115)
Name and origin of the protein
Protein name Proto-oncogene tyrosine-protein kinase Src
Synonyms EC 2.7.10.2
pp60c-src
p60-Src
c-Src
Gene name
Name: SRC
Synonyms: SRC1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
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).
[2]
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).
[3]
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]
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 98-139 (ISOFORM 2).
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]
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).
[7]
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]
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]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL133293; CAC34523.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011566; AAH11566.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC051270; AAH51270.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03218; AAA60584.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16237; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16243; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16244; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16245; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03212; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03213; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03214; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03215; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03216; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03217; AAA60584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02647; CAA26485.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03995; CAA26485.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03996; CAA26485.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03997; CAA26485.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03998; CAA26485.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03999; CAA26485.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04000; CAA26485.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26891; TVHUSC.
RefSeq NP_005408.1; -.
NP_938033.1; -.
UniGene Hs.195659
3D structure databases
PDB
1A07; X-ray; 2.20 A; A/B=144-249.[ExPASy / RCSB / EBI]
1A08; X-ray; 2.20 A; A/B=144-249.[ExPASy / RCSB / EBI]
1A09; X-ray; 2.00 A; A/B=144-249.[ExPASy / RCSB / EBI]
1A1A; X-ray; 2.00 A; A/B=144-249.[ExPASy / RCSB / EBI]
1A1B; X-ray; 2.20 A; A/B=144-249.[ExPASy / RCSB / EBI]
1A1C; X-ray; 2.40 A; A/B=144-249.[ExPASy / RCSB / EBI]
1A1E; X-ray; 2.20 A; A/B=144-249.[ExPASy / RCSB / EBI]
1FMK; X-ray; 1.50 A; A=86-536.[ExPASy / RCSB / EBI]
1HCS; NMR; -; B=144-249.[ExPASy / RCSB / EBI]
1HCT; NMR; -; B=144-249.[ExPASy / RCSB / EBI]
1KSW; X-ray; 2.80 A; A=86-536.[ExPASy / RCSB / EBI]
1O41; X-ray; 1.70 A; A=145-252.[ExPASy / RCSB / EBI]
1O42; X-ray; 1.70 A; A=145-252.[ExPASy / RCSB / EBI]
1O43; X-ray; 1.50 A; A=145-252.[ExPASy / RCSB / EBI]
1O44; X-ray; 1.70 A; A=145-252.[ExPASy / RCSB / EBI]
1O45; X-ray; 1.80 A; A=145-252.[ExPASy / RCSB / EBI]
1O46; X-ray; 2.00 A; A=145-252.[ExPASy / RCSB / EBI]
1O47; X-ray; 1.80 A; A=145-252.[ExPASy / RCSB / EBI]
1O48; X-ray; 1.55 A; A=145-252.[ExPASy / RCSB / EBI]
1O49; X-ray; 1.70 A; A=145-252.[ExPASy / RCSB / EBI]
1O4A; X-ray; 1.50 A; A=145-252.[ExPASy / RCSB / EBI]
1O4B; X-ray; 1.85 A; A=145-252.[ExPASy / RCSB / EBI]
1O4C; X-ray; 1.80 A; A=145-252.[ExPASy / RCSB / EBI]
1O4D; X-ray; 1.85 A; A=145-252.[ExPASy / RCSB / EBI]
1O4E; X-ray; 2.00 A; A=145-252.[ExPASy / RCSB / EBI]
1O4F; X-ray; 2.00 A; A=145-252.[ExPASy / RCSB / EBI]
1O4G; X-ray; 1.55 A; A=145-252.[ExPASy / RCSB / EBI]
1O4H; X-ray; 2.25 A; A=145-252.[ExPASy / RCSB / EBI]
1O4I; X-ray; 1.75 A; A=145-252.[ExPASy / RCSB / EBI]
1O4J; X-ray; 1.70 A; A=145-252.[ExPASy / RCSB / EBI]
1O4K; X-ray; 1.57 A; A=145-252.[ExPASy / RCSB / EBI]
1O4L; X-ray; 1.65 A; A=145-252.[ExPASy / RCSB / EBI]
1O4M; X-ray; 1.60 A; A=145-252.[ExPASy / RCSB / EBI]
1O4N; X-ray; 1.60 A; A=145-252.[ExPASy / RCSB / EBI]
1O4O; X-ray; 1.70 A; A=145-252.[ExPASy / RCSB / EBI]
1O4P; X-ray; 1.90 A; A=145-252.[ExPASy / RCSB / EBI]
1O4Q; X-ray; 1.70 A; A=145-252.[ExPASy / RCSB / EBI]
1O4R; X-ray; 1.50 A; A=145-252.[ExPASy / RCSB / EBI]
1SHD; X-ray; 2.00 A; A=144-249.[ExPASy / RCSB / EBI]
1Y57; X-ray; 1.91 A; A=86-536.[ExPASy / RCSB / EBI]
1YI6; X-ray; 2.00 A; A/B=261-536.[ExPASy / RCSB / EBI]
1YOJ; X-ray; 1.95 A; A/B=254-536.[ExPASy / RCSB / EBI]
1YOL; X-ray; 2.30 A; A/B=254-536.[ExPASy / RCSB / EBI]
1YOM; X-ray; 2.90 A; A/B=254-536.[ExPASy / RCSB / EBI]
2BDF; X-ray; 2.10 A; A/B=258-536.[ExPASy / RCSB / EBI]
2BDJ; X-ray; 2.50 A; A=258-536.[ExPASy / RCSB / EBI]
2H8H; X-ray; 2.20 A; A=2-536.[ExPASy / RCSB / EBI]
2SRC; X-ray; 1.50 A; A=86-536.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A07; -.
1A08; -.
1A09; -.
1A1A; -.
1A1B; -.
1A1C; -.
1A1E; -.
1FMK; -.
1HCS; -.
1HCT; -.
1KSW; -.
1O41; -.
1O42; -.
1O43; -.
1O44; -.
1O45; -.
1O46; -.
1O47; -.
1O48; -.
1O49; -.
1O4A; -.
1O4B; -.
1O4C; -.
1O4D; -.
1O4E; -.
1O4F; -.
1O4G; -.
1O4H; -.
1O4I; -.
1O4J; -.
1O4K; -.
1O4L; -.
1O4M; -.
1O4N; -.
1O4O; -.
1O4P; -.
1O4Q; -.
1O4R; -.
1SHD; -.
1Y57; -.
1YI6; -.
1YOJ; -.
1YOL; -.
1YOM; -.
2BDF; -.
2BDJ; -.
2H8H; -.
2SRC; -.
ModBase P12931.
Protein-protein interaction databases
DIP DIP:1059N; -.
IntAct P12931; -.
PTM databases
PhosphoSite P12931; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
REACT_9417; Signaling by EGFR.
REACT_9480; Gap junction trafficking and regulation.
2D gel databases
OGP P12931; -.
Organism-specific databases
H-InvDB HIX0015793; -.
HGNC HGNC:11283; SRC.
GenAtlas SRC.
HPA CAB004023; -.
MIM 190090; gene. [NCBI / EBI]
PharmGKB PA36111; -.
GeneCards P12931.
Gene expression databases
ArrayExpress P12931; -.
CleanEx HS_SRC; -.
GermOnline ENSG00000197122; Homo sapiens.
Ontologies
GO
GO:0005901; Cellular component: caveola (inferred from direct assay from UniProtKB).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0004713; Molecular function: protein tyrosine kinase activity (traceable author statement from ProtInc).
GO:0042169; Molecular function: SH2 domain binding (inferred from physical interaction from UniProtKB).
GO:0005070; Molecular function: SH3/SH2 adaptor activity (traceable author statement from ProtInc).
GO:0007243; Biological process: protein kinase cascade (traceable author statement from ProtInc).
GO:0007265; Biological process: Ras protein signal transduction (inferred from experiment from Reactome).
GO:0007172; Biological process: signal complex assembly (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000980; SH2.
IPR001452; SH3.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.
Gene3D G3DSA:3.30.505.10; SH2; 1.
Pfam PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
PD000093; SH2; 1.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P12931.
Genome annotation databases
Ensembl ENSG00000197122; Homo sapiens. [Contig view]
GeneID 6714; -.
KEGG hsa:6714; -.
Phylogenomic databases
HOVERGEN P12931; -.
Other
DrugBank DB01254; Dasatinib.
LinkHub P12931; -.
SOURCE SRC; Homo sapiens.
ProtoNet P12931.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Host-virus interaction; Kinase; Lipoprotein; Myristate; Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   536  535     Proto-oncogene tyrosine-protein kinase Src. PRO_0000088141
DOMAIN   84   145  62     SH3. 
DOMAIN   151   248  98     SH2. 
DOMAIN   270   523  254     Protein kinase. 
NP_BIND   276   284  9     ATP. 
ACT_SITE   389   389        Proton acceptor. 
BINDING   298   298        ATP. 
MOD_RES   17    17        Phosphoserine. 
MOD_RES   69    69        Phosphoserine. 
MOD_RES   74    74        Phosphothreonine. 
MOD_RES   75    75        Phosphoserine. 
MOD_RES   187   187        Phosphotyrosine (By similarity). 
MOD_RES   419   419        Phosphotyrosine; by autocatalysis. 
MOD_RES   530   530        Phosphotyrosine; by CSK. 
LIPID   2     2        N-myristoyl glycine (By similarity). 
VAR_SEQ   117   117        T -> TRKVDVR (in isoform 2). VSP_012134
VARIANT   237   237  1     A -> T. VAR_041830 
STRAND   87    93  7      
STRAND   99   102  4      
STRAND   110   114  5      
STRAND   118   126  9      
TURN   127   129  3      
STRAND   132   136  5      
HELIX   137   139  3      
STRAND   140   142  3      
HELIX   146   148  3      
HELIX   158   165  8      
STRAND   174   179  6      
STRAND   181   183  3      
STRAND   187   195  9