Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P12931 (SRC_HUMAN)

Last modified November 3, 2009. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Proto-oncogene tyrosine-protein kinase Src
    EC=2.7.10.2
Alternative name(s):
    pp60c-src
      Short name=p60-Src
      Short name=c-Src
Gene names
Name: SRC
Synonyms: SRC1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

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. Interacts with CAV2 (tyrosine phosphorylated form).

Post-translational modification

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. Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABL1P005191EBI-621482,EBI-375543
ABL2P426841EBI-621482,EBI-1102694
ACAP1Q150271EBI-621482,EBI-751746
ACTN1P128142EBI-621482,EBI-351710
AIREO439181EBI-621482,EBI-1753081
AKAP2Q9Y2D51EBI-621482,EBI-1754555
AKAP6Q130231EBI-621482,EBI-1056102
ALS2CR12Q96Q351EBI-621482,EBI-1755548
APOL5Q9BWW91EBI-621482,EBI-1753592
Arap3Q8R5G73EBI-621482,EBI-621463From a different organism.
ASAP1Q9ULH11EBI-621482,EBI-346622
ASAP2O431501EBI-621482,EBI-310968
ASB16Q96NS51EBI-621482,EBI-1751918
Bcar1Q637671EBI-621482,EBI-1176801From a different organism.
CASTP208101EBI-621482,EBI-1268770
CD97P489601EBI-621482,EBI-1756009
CDKN1BP465271EBI-621482,EBI-519280
CELSR2Q9HCU41EBI-621482,EBI-724117
CKAP5Q140081EBI-621482,EBI-310585
CUL9Q8IWT31EBI-621482,EBI-311123
CYP4F2P783291EBI-621482,EBI-1752413
DAG1Q141181EBI-621482,EBI-1755945
DLGAP1O144901EBI-621482,EBI-1753207
DLGAP2Q9P1A61EBI-621482,EBI-1753397
DLGAP3O958861EBI-621482,EBI-1752541
DLGAP4Q9Y2H01EBI-621482,EBI-722139
DLX4Q929881EBI-621482,EBI-1752755
DOCK1Q141851EBI-621482,EBI-446740
DOCK3Q8IZD91EBI-621482,EBI-1752361
DUSP15Q9H1R21EBI-621482,EBI-1752795
EFSO432811EBI-621482,EBI-718488
EIF3DO153711EBI-621482,EBI-353818
EPB41L3Q9Y2J21EBI-621482,EBI-310986
EXTL3O439091EBI-621482,EBI-1754679
F2RL2O002541EBI-621482,EBI-1751853
FANCAO153601EBI-621482,EBI-81570
FASP254452EBI-621482,EBI-494743
FCGR2BP319941EBI-621482,EBI-724784
FCGR2CP319951EBI-621482,EBI-1396036
GLTSCR1Q9NZM41EBI-621482,EBI-1754943
GNSP155861EBI-621482,EBI-1752200
HCN2Q9UL511EBI-621482,EBI-1751885
HOXC8P312731EBI-621482,EBI-1752118
ID4P479281EBI-621482,EBI-1754719
IKBKGQ9Y6K91EBI-621482,EBI-81279
ISG20L2Q9H9L31EBI-621482,EBI-751335
Khdrbs1Q607491EBI-621482,EBI-519077From a different organism.
KIAA1219Q86X101EBI-621482,EBI-1755842
LIG3P499161EBI-621482,EBI-1753381
MAP4K1Q929181EBI-621482,EBI-881
MED28Q9H2041EBI-621482,EBI-514199
MEPEQ9NQ761EBI-621482,EBI-1753293
MKI67P460131EBI-621482,EBI-876367
NKX2-1P436991EBI-621482,EBI-1391923
NXPH3O951571EBI-621482,EBI-1752913
OGNP207741EBI-621482,EBI-1753690
PAX3P237601EBI-621482,EBI-1167564
PAX7P237591EBI-621482,EBI-1042757
PDIA2Q130871EBI-621482,EBI-1752525
PECAM1P162841EBI-621482,EBI-716404
PHACTR2O751671EBI-621482,EBI-1754409
POLD1P283401EBI-621482,EBI-716569
PRICKLE3O439001EBI-621482,EBI-1751761
PTK2Q053971EBI-621482,EBI-702142
RAPGEF1Q139051EBI-621482,EBI-976876
RIN3Q8TB241EBI-621482,EBI-1570523
RPL13P263731EBI-621482,EBI-356849
RPP38P783451EBI-621482,EBI-366493
RRASP103011EBI-621482,EBI-968703
RTN4Q9NQC31EBI-621482,EBI-715945
SEPN1Q9NZV51EBI-621482,EBI-1751965
SHANK2Q9UPX81EBI-621482,EBI-1570571
SHANK3Q9BYB01EBI-621482,EBI-1752330
SHROOM2Q137961EBI-621482,EBI-1644065
SNX17Q150361EBI-621482,EBI-1752620
SNX3O604931EBI-621482,EBI-727209
SOS1Q078891EBI-621482,EBI-297487
SOS2Q078901EBI-621482,EBI-298181
SP1P080471EBI-621482,EBI-298336
Stat3P422271EBI-621482,EBI-602878From a different organism.
TULP4Q9NRJ41EBI-621482,EBI-1753487
ZP2Q059961EBI-621482,EBI-1755919

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P12931-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P12931-2)

The sequence of this isoform differs from the canonical sequence as follows:
     117-117: T → TRKVDVR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 536535Proto-oncogene tyrosine-protein kinase Src
PRO_0000088141

Regions

Domain84 – 14562SH3
Domain151 – 24898SH2
Domain270 – 523254Protein kinase
Nucleotide binding276 – 2849ATP

Sites

Active site3891Proton acceptor
Binding site2981ATP

Amino acid modifications

Modified residue171Phosphoserine Ref.18 Ref.19
Modified residue691Phosphoserine Ref.18
Modified residue741Phosphothreonine Ref.19
Modified residue751Phosphoserine Ref.18 Ref.20
Modified residue1871Phosphotyrosine By similarity
Modified residue4191Phosphotyrosine; by autocatalysis Ref.18 Ref.19
Modified residue4391Phosphotyrosine Ref.17
Modified residue5301Phosphotyrosine; by CSK Ref.21
Lipidation21N-myristoyl glycine By similarity

Natural variations

Alternative sequence1171T → TRKVDVR in isoform 2.
VSP_012134
Natural variant1761L → F: dbSNP rs6018260.
VAR_051699
Natural variant2371A → T
VAR_041830

Secondary structure

............................................................................... 536
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C1908084683E5DE8

FASTA53659,835
        10         20         30         40         50         60 
MGSNKSKPKD ASQRRRSLEP AENVHGAGGG AFPASQTPSK PASADGHRGP SAAFAPAAAE 

        70         80         90        100        110        120 
PKLFGGFNSS DTVTSPQRAG PLAGGVTTFV ALYDYESRTE TDLSFKKGER LQIVNNTEGD 

       130        140        150        160        170        180 
WWLAHSLSTG QTGYIPSNYV APSDSIQAEE WYFGKITRRE SERLLLNAEN PRGTFLVRES 

       190        200        210        220        230        240 
ETTKGAYCLS VSDFDNAKGL NVKHYKIRKL DSGGFYITSR TQFNSLQQLV AYYSKHADGL 

       250        260        270        280        290        300 
CHRLTTVCPT SKPQTQGLAK DAWEIPRESL RLEVKLGQGC FGEVWMGTWN GTTRVAIKTL 

       310        320        330        340        350        360 
KPGTMSPEAF LQEAQVMKKL RHEKLVQLYA VVSEEPIYIV TEYMSKGSLL DFLKGETGKY 

       370        380        390        400        410        420 
LRLPQLVDMA AQIASGMAYV ERMNYVHRDL RAANILVGEN LVCKVADFGL ARLIEDNEYT 

       430        440        450        460        470        480 
ARQGAKFPIK WTAPEAALYG RFTIKSDVWS FGILLTELTT KGRVPYPGMV NREVLDQVER 

       490        500        510        520        530 
GYRMPCPPEC PESLHDLMCQ CWRKEPEERP TFEYLQAFLE DYFTSTEPQY QPGENL 

« Hide

Isoform 2.

Checksum: C12D30F8BCD5FF6B
Show »

FASTA54260,589

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung and Skin.
[3]"DNA sequence encoding the amino-terminal region of the human c-src protein: implications of sequence divergence among src-type kinase oncogenes."
Tanaka A., Gibbs C.P., Arthur R.R., Anderson S.K., Kung H.-J., Fujita D.J.
Mol. Cell. Biol. 7:1978-1983(1987) [PubMed: 3299057] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185 (ISOFORM 1).
[4]"Human cellular src gene: nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-src."
Anderson S.K., Gibbs C.P., Tanaka A., Kung H.-J., Fujita D.J.
Mol. Cell. Biol. 5:1122-1129(1985) [PubMed: 2582238] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-536 (ISOFORM 1).
[5]"Neuron-specific splicing of C-SRC RNA in human brain."
Pyper J.M., Bolen J.B.
J. Neurosci. Res. 24:89-96(1989) [PubMed: 2681803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 98-139 (ISOFORM 2).
[6]"Isolation of duplicated human c-src genes located on chromosomes 1 and 20."
Parker R.C., Mardon G., Lebo R.V., Varmus H.E., Bishop J.M.
Mol. Cell. Biol. 5:831-838(1985) [PubMed: 2581127] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-536 (ISOFORM 1).
[7]"Identification of a novel neuronal C-SRC exon expressed in human brain."
Pyper J.M., Bolen J.B.
Mol. Cell. Biol. 10:2035-2040(1990) [PubMed: 1691439] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[8]"Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral."
Rebhun J.F., Chen H., Quilliam L.A.
J. Biol. Chem. 275:13406-13410(2000) [PubMed: 10747847] [Abstract]
Cited for: INTERACTION WITH RALGPS1.
[9]"The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 beta and beta-catenin."
Li Y., Kuwahara H., Ren J., Wen G., Kufe D.
J. Biol. Chem. 276:6061-6064(2001) [PubMed: 11152665] [Abstract]
Cited for: INTERACTION WITH MUC1.
[10]"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK."
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.
J. Biol. Chem. 276:42389-42400(2001) [PubMed: 11518702] [Abstract]
Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
[11]"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."
Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
J. Biol. Chem. 277:34556-34567(2002) [PubMed: 12091389] [Abstract]
Cited for: INTERACTION WITH CAV2.
[12]"Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade."
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002) [PubMed: 12415108] [Abstract]
Cited for: INTERACTION WITH PELP1.
[13]"Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."
Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., Campos-Gonzalez R., Lisanti M.P.
Biochemistry 43:13694-13706(2004) [PubMed: 15504032] [Abstract]
Cited for: INTERACTION WITH CAV2.
[14]"The C2 domain of PKCdelta is a phosphotyrosine binding domain."
Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.
Cell 121:271-280(2005) [PubMed: 15851033] [Abstract]
Cited for: INTERACTION WITH CDCP1.
[15]"The adaptor protein Tom1L1 is a negative regulator of Src mitogenic signaling induced by growth factors."
Franco M., Furstoss O., Simon V., Benistant C., Hong W.J., Roche S.
Mol. Cell. Biol. 26:1932-1947(2006) [PubMed: 16479011] [Abstract]
Cited for: INTERACTION WITH TOM1L2.
[16]"Gonadotropin-releasing hormone functionally antagonizes testosterone activation of the human androgen receptor in prostate cells through focal adhesion complexes involving Hic-5."
Maudsley S., Davidson L., Pawson A.J., Freestone S.H., Lopez de Maturana R., Thomson A.A., Millar R.P.
Neuroendocrinology 84:285-300(2006) [PubMed: 17202804] [Abstract]
Cited for: INTERACTION WITH TGFB1I1.
[17]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
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. expand/collapse author list , 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.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, MASS SPECTROMETRY.
Tissue: Lung.
[18]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-69; SER-75 AND TYR-419, MASS SPECTROMETRY.
[19]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-74 AND TYR-419, MASS SPECTROMETRY.
Tissue: Platelet.
[20]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, MASS SPECTROMETRY.
[21]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-530, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[22]"Three-dimensional structure of the tyrosine kinase c-Src."
Xu W., Harrison S.C., Eck M.J.
Nature 385:595-602(1997) [PubMed: 9024657] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 86-536.
[23]"Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and structural study."
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.
Biochemistry 36:6283-6293(1997) [PubMed: 9174343] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 145-249.
[24]"Solution structure of the human pp60c-src SH2 domain complexed with a phosphorylated tyrosine pentapeptide."
Xu R.X., Word J.M., Davis D.G., Rink M.J., Willard D.H. Jr., Gampe R.T. Jr.
Biochemistry 34:2107-2121(1995) [PubMed: 7532003] [Abstract]
Cited for: STRUCTURE BY NMR OF 204-249.
[25]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-237.
+Additional computationally mapped references.

Cross-references

Sequence databases

AL133293 Genomic DNA. Translation: CAC34523.1.
BC011566 mRNA. Translation: AAH11566.1.
BC051270 mRNA. Translation: AAH51270.2.
K03218 expand/collapse EMBL AC list , M16237, M16243, M16244, M16245, K03212, K03213, K03214, K03215, K03216, K03217 Genomic DNA. Translation: AAA60584.1.
X02647 expand/collapse EMBL AC list , X03995, X03996, X03997, X03998, X03999, X04000 Genomic DNA. Translation: CAA26485.1.
IPIIPI00328867.
IPI00641230.
PIRTVHUSC. A26891.
RefSeqNP_005408.1.
NP_938033.1.
UniGeneHs.195659

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A07X-ray2.20A/B144-249[»]
1A08X-ray2.20A/B144-249[»]
1A09X-ray2.00A/B144-249[»]
1A1AX-ray2.00A/B144-249[»]
1A1BX-ray2.20A/B144-249[»]
1A1CX-ray2.40A/B144-249[»]
1A1EX-ray2.20A/B144-249[»]
1FMKX-ray1.50A86-536[»]
1HCSNMR-B144-249[»]
1HCTNMR-B144-249[»]
1KSWX-ray2.80A86-535[»]
1O41X-ray1.70A145-251[»]
1O42X-ray1.70A145-251[»]
1O43X-ray1.50A145-251[»]
1O44X-ray1.70A145-251[»]
1O45X-ray1.80A145-251[»]
1O46X-ray2.00A145-251[»]
1O47X-ray1.80A145-251[»]
1O48X-ray1.55A145-251[»]
1O49X-ray1.70A145-251[»]
1O4AX-ray1.50A145-251[»]
1O4BX-ray1.85A145-251[»]
1O4CX-ray1.80A145-251[»]
1O4DX-ray1.85A145-251[»]
1O4EX-ray2.00A145-251[»]
1O4FX-ray2.00A145-251[»]
1O4GX-ray1.55A145-251[»]
1O4HX-ray2.25A145-251[»]
1O4IX-ray1.75A145-251[»]
1O4JX-ray1.70A145-251[»]
1O4KX-ray1.57A145-251[»]
1O4LX-ray1.65A145-251[»]
1O4MX-ray1.60A145-251[»]
1O4NX-ray1.60A145-251[»]
1O4OX-ray1.70A145-251[»]
1O4PX-ray1.90A145-251[»]
1O4QX-ray1.70A145-251[»]
1O4RX-ray1.50A145-251[»]
1SHDX-ray2.00A144-248[»]
1Y57X-ray1.91A86-535[»]
1YI6X-ray2.00A/B261-535[»]
1YOJX-ray1.95A/B254-535[»]
1YOLX-ray2.30A/B254-535[»]
1YOMX-ray2.90A/B254-535[»]
2BDFX-ray2.10A/B258-535[»]
2BDJX-ray2.50A258-535[»]
2H8HX-ray2.20A2-535[»]
2SRCX-ray1.50A86-535[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1059N.
IntActP12931. 92 interactions.
STRINGP12931.

PTM databases

PhosphoSiteP12931.

2-D gel databases

OGPP12931.

Proteomic databases

PRIDEP12931.

Genome annotation databases

EnsemblENST00000358208; ENSP00000350941; ENSG00000197122; Homo sapiens. [Genome view]
ENST00000360723; ENSP00000353950; ENSG00000197122; Homo sapiens. [Genome view]
ENST00000373558; ENSP00000362659; ENSG00000197122; Homo sapiens. [Genome view]
ENST00000373567; ENSP00000362668; ENSG00000197122; Homo sapiens. [Genome view]
ENST00000373578; ENSP00000362680; ENSG00000197122; Homo sapiens. [Genome view]
ENST00000445403; ENSP00000408503; ENSG00000197122; Homo sapiens. [Genome view]
GeneID6714.
KEGGhsa:6714.
UCSCuc002xgx.1. human.

Organism-specific databases

CTD6714.
GeneCardsGC20P035406.
H-InvDBHIX0015793.
HGNCHGNC:11283. SRC.
HPACAB004023.
MIM190090. gene.
PharmGKBPA36111.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP12931.
OMAKVDVREG.

Enzyme and pathway databases

BRENDA2.7.10.2. 247.
Pathway_Interaction_DBalphasynuclein_pathway. Alpha-synuclein signaling.
amb2_neutrophils_pathway. amb2 Integrin signaling.
arf6cyclingpathway. Arf6 signaling events.
nfkappabatypicalpathway. Atypical NF-kappaB pathway.
pi3kcipathway. Class I PI3K signaling events.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
endothelinpathway. Endothelins.
epha_fwdpathway. EPHA forward signaling.
epha2_fwdpathway. EPHA2 forward signaling.
ephbfwdpathway. EPHB forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
fgf_pathway. FGF signaling pathway.
glypican_1pathway. Glypican 1 network.
avb3_integrin_pathway. Integrins in angiogenesis.
lysophospholipid_pathway. LPA receptor mediated events.
a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.
pdgfrbpathway. PDGFR-beta signaling pathway.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
ar_tf_pathway. Regulation of Androgen receptor activity.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
s1p_s1p3_pathway. S1P3 pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
prlsignalingeventspathway. Signaling events mediated by PRL.
ptp1bpathway. Signaling events mediated by PTP1B.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
syndecan_3_pathway. Syndecan-3-mediated signaling events.
txa2pathway. Thromboxane A2 receptor signaling.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.
ReactomeREACT_11061. Signalling by NGF.
REACT_13552. Integrin cell surface interactions.
REACT_16888. Signaling by PDGF.
REACT_18266. Axon guidance.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.
REACT_9417. Signaling by EGFR.
REACT_9480. Gap junction trafficking and regulation.

Gene expression databases

ArrayExpressP12931.
BgeeP12931.
CleanExHS_SRC.
GenevestigatorP12931.
GermOnlineENSG00000197122. Homo sapiens.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR020473. SH3_region.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01254. Dasatinib.
NextBio26186.
PMAP-CutDBP12931.
SOURCESearch...

Entry information

Entry nameSRC_HUMAN
AccessionPrimary (citable) accession number: P12931
Secondary accession number(s): Q86VB9, Q9H5A8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents