Reviewed, UniProtKB/Swiss-Prot P12931 (SRC_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	536 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Host-virus interaction
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	Ras protein signal transduction Inferred from Experiment. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW protein kinase cascade Traceable author statement. Source: ProtInc response to interleukin-1 Inferred from mutant phenotype. Source: UniProtKB signal complex assembly Traceable author statement. Source: ProtInc
Cellular component	caveola Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SH2 domain binding Inferred from physical interaction. Source: UniProtKB SH3/SH2 adaptor activity Traceable author statement. Source: ProtInc non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	1	EBI-621482,EBI-375543
ABL2	P42684	1	EBI-621482,EBI-1102694
ACAP1	Q15027	1	EBI-621482,EBI-751746
ACTN1	P12814	2	EBI-621482,EBI-351710
AIRE	O43918	1	EBI-621482,EBI-1753081
AKAP2	Q9Y2D5	1	EBI-621482,EBI-1754555
AKAP6	Q13023	1	EBI-621482,EBI-1056102
ALS2CR12	Q96Q35	1	EBI-621482,EBI-1755548
APOL5	Q9BWW9	1	EBI-621482,EBI-1753592
Arap3	Q8R5G7	3	EBI-621482,EBI-621463	From a different organism.
ASAP1	Q9ULH1	1	EBI-621482,EBI-346622
ASAP2	O43150	1	EBI-621482,EBI-310968
ASB16	Q96NS5	1	EBI-621482,EBI-1751918
Bcar1	Q63767	1	EBI-621482,EBI-1176801	From a different organism.
CAST	P20810	1	EBI-621482,EBI-1268770
CD97	P48960	1	EBI-621482,EBI-1756009
CDKN1B	P46527	1	EBI-621482,EBI-519280
CELSR2	Q9HCU4	1	EBI-621482,EBI-724117
CKAP5	Q14008	1	EBI-621482,EBI-310585
CUL9	Q8IWT3	1	EBI-621482,EBI-311123
CYP4F2	P78329	1	EBI-621482,EBI-1752413
DAG1	Q14118	1	EBI-621482,EBI-1755945
DLGAP1	O14490	1	EBI-621482,EBI-1753207
DLGAP2	Q9P1A6	1	EBI-621482,EBI-1753397
DLGAP3	O95886	1	EBI-621482,EBI-1752541
DLGAP4	Q9Y2H0	1	EBI-621482,EBI-722139
DLX4	Q92988	1	EBI-621482,EBI-1752755
DOCK1	Q14185	1	EBI-621482,EBI-446740
DOCK3	Q8IZD9	1	EBI-621482,EBI-1752361
DUSP15	Q9H1R2	1	EBI-621482,EBI-1752795
EFS	O43281	1	EBI-621482,EBI-718488
EIF3D	O15371	1	EBI-621482,EBI-353818
EPB41L3	Q9Y2J2	1	EBI-621482,EBI-310986
EXTL3	O43909	1	EBI-621482,EBI-1754679
F2RL2	O00254	1	EBI-621482,EBI-1751853
FANCA	O15360	1	EBI-621482,EBI-81570
FAS	P25445	2	EBI-621482,EBI-494743
FCGR2B	P31994	1	EBI-621482,EBI-724784
FCGR2C	P31995	1	EBI-621482,EBI-1396036
GLTSCR1	Q9NZM4	1	EBI-621482,EBI-1754943
GNS	P15586	1	EBI-621482,EBI-1752200
HCN2	Q9UL51	1	EBI-621482,EBI-1751885
HOXC8	P31273	1	EBI-621482,EBI-1752118
ID4	P47928	1	EBI-621482,EBI-1754719
IKBKG	Q9Y6K9	1	EBI-621482,EBI-81279
ISG20L2	Q9H9L3	1	EBI-621482,EBI-751335
Khdrbs1	Q60749	1	EBI-621482,EBI-519077	From a different organism.
KIAA1219	Q86X10	1	EBI-621482,EBI-1755842
LIG3	P49916	1	EBI-621482,EBI-1753381
MAP4K1	Q92918	1	EBI-621482,EBI-881
MED28	Q9H204	1	EBI-621482,EBI-514199
MEPE	Q9NQ76	1	EBI-621482,EBI-1753293
MKI67	P46013	1	EBI-621482,EBI-876367
NKX2-1	P43699	1	EBI-621482,EBI-1391923
NXPH3	O95157	1	EBI-621482,EBI-1752913
OGN	P20774	1	EBI-621482,EBI-1753690
PAX3	P23760	1	EBI-621482,EBI-1167564
PAX7	P23759	1	EBI-621482,EBI-1042757
PDIA2	Q13087	1	EBI-621482,EBI-1752525
PECAM1	P16284	1	EBI-621482,EBI-716404
PHACTR2	O75167	1	EBI-621482,EBI-1754409
POLD1	P28340	1	EBI-621482,EBI-716569
PRICKLE3	O43900	1	EBI-621482,EBI-1751761
PTK2	Q05397	1	EBI-621482,EBI-702142
RAPGEF1	Q13905	1	EBI-621482,EBI-976876
RIN3	Q8TB24	1	EBI-621482,EBI-1570523
RPL13	P26373	1	EBI-621482,EBI-356849
RPP38	P78345	1	EBI-621482,EBI-366493
RRAS	P10301	1	EBI-621482,EBI-968703
RTN4	Q9NQC3	1	EBI-621482,EBI-715945
SEPN1	Q9NZV5	1	EBI-621482,EBI-1751965
SHANK2	Q9UPX8	1	EBI-621482,EBI-1570571
SHANK3	Q9BYB0	1	EBI-621482,EBI-1752330
SHROOM2	Q13796	1	EBI-621482,EBI-1644065
SNX17	Q15036	1	EBI-621482,EBI-1752620
SNX3	O60493	1	EBI-621482,EBI-727209
SOS1	Q07889	1	EBI-621482,EBI-297487
SOS2	Q07890	1	EBI-621482,EBI-298181
SP1	P08047	1	EBI-621482,EBI-298336
Stat3	P42227	1	EBI-621482,EBI-602878	From a different organism.
TULP4	Q9NRJ4	1	EBI-621482,EBI-1753487
ZP2	Q05996	1	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 536

535

Proto-oncogene tyrosine-protein kinase Src

PRO_0000088141

Regions

Domain

84 – 145

62

SH3

Domain

151 – 248

98

SH2

Domain

270 – 523

254

Protein kinase

Nucleotide binding

276 – 284

9

ATP

Sites

Active site

389

1

Proton acceptor

Binding site

298

1

ATP

Amino acid modifications

Modified residue

17

1

Phosphoserine Ref.18 Ref.19

Modified residue

69

1

Phosphoserine Ref.18

Modified residue

74

1

Phosphothreonine Ref.19

Modified residue

75

1

Phosphoserine Ref.18 Ref.20

Modified residue

187

1

Phosphotyrosine By similarity

Modified residue

419

1

Phosphotyrosine; by autocatalysis Ref.18 Ref.19

Modified residue

439

1

Phosphotyrosine Ref.17

Modified residue

530

1

Phosphotyrosine; by CSK Ref.21

Lipidation

2

1

N-myristoyl glycine By similarity

Natural variations

Alternative sequence

117

1

T → TRKVDVR in isoform 2.

VSP_012134

Natural variant

176

1

L → F: dbSNP rs6018260.

VAR_051699

Natural variant

237

1

A → T

VAR_041830

Secondary structure

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536

Helix Strand Turn

Details...

Beta strand

87 – 93

7

Beta strand

99 – 102

4

Beta strand

110 – 114

5

Beta strand

118 – 126

9

Turn

127 – 129

3

Beta strand

132 – 136

5

Helix

137 – 139

3

Beta strand

140 – 142

3

Helix

146 – 148

3

Helix

158 – 165

8

Beta strand

174 – 179

6

Beta strand

181 – 183

3

Beta strand

187 – 195

9

Turn

196 – 198

3

Beta strand

199 – 209

11

Beta strand

215 – 218

4

Beta strand

221 – 225

5

Helix

226 – 235

10

Beta strand

240 – 242

3

Beta strand

256 – 259

4

Helix

267 – 269

3

Beta strand

270 – 278

9

Beta strand

283 – 289

7

Turn

290 – 292

3

Beta strand

293 – 299

7

Helix

307 – 319

13

Beta strand

328 – 332

5

Beta strand

334 – 336

3

Beta strand

338 – 341

4

Helix

349 – 353

5

Helix

355 – 358

4

Helix

363 – 382

20

Helix

392 – 394

3

Beta strand

395 – 397

3

Helix

399 – 401

3

Beta strand

403 – 405

3

Helix

429 – 431

3

Helix

434 – 439

6

Helix

444 – 459

16

Turn

460 – 462

3

Helix

471 – 479

9

Helix

492 – 501

10

Helix

506 – 508

3

Helix

512 – 520

9

Turn

521 – 523

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C1908084683E5DE8	FASTA	536	59,835
	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
	Isoform 2. Checksum: C12D30F8BCD5FF6B	FASTA	542	60,589
	10 20 30 40 50 60 MGSNKSKPKD ASQRRRSLEP AENVHGAGGG AFPASQTPSK PASADGHRGP SAAFAPAAAE 70 80 90 100 110 120 PKLFGGFNSS DTVTSPQRAG PLAGGVTTFV ALYDYESRTE TDLSFKKGER LQIVNNTRKV 130 140 150 160 170 180 DVREGDWWLA HSLSTGQTGY IPSNYVAPSD SIQAEEWYFG KITRRESERL LLNAENPRGT 190 200 210 220 230 240 FLVRESETTK GAYCLSVSDF DNAKGLNVKH YKIRKLDSGG FYITSRTQFN SLQQLVAYYS 250 260 270 280 290 300 KHADGLCHRL TTVCPTSKPQ TQGLAKDAWE IPRESLRLEV KLGQGCFGEV WMGTWNGTTR 310 320 330 340 350 360 VAIKTLKPGT MSPEAFLQEA QVMKKLRHEK LVQLYAVVSE EPIYIVTEYM SKGSLLDFLK 370 380 390 400 410 420 GETGKYLRLP QLVDMAAQIA SGMAYVERMN YVHRDLRAAN ILVGENLVCK VADFGLARLI 430 440 450 460 470 480 EDNEYTARQG AKFPIKWTAP EAALYGRFTI KSDVWSFGIL LTELTTKGRV PYPGMVNREV 490 500 510 520 530 540 LDQVERGYRM PCPPECPESL HDLMCQCWRK EPEERPTFEY LQAFLEDYFT STEPQYQPGE NL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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

EMBLGenBankDDBJ

AL133293 Genomic DNA. Translation: CAC34523.1.
BC011566 mRNA. Translation: AAH11566.1.
BC051270 mRNA. Translation: AAH51270.2.
K03218 , M16237, M16243, M16244, M16245, K03212, K03213, K03214, K03215, K03216, K03217 Genomic DNA. Translation: AAA60584.1.
X02647 , X03995, X03996, X03997, X03998, X03999, X04000 Genomic DNA. Translation: CAA26485.1.

IPI

IPI00328867.
IPI00641230.

PIR

TVHUSC. A26891.

RefSeq

NP_005408.1.
NP_938033.1.

UniGene

Hs.195659

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A07	X-ray	2.20	A/B	144-249	[»]
1A08	X-ray	2.20	A/B	144-249	[»]
1A09	X-ray	2.00	A/B	144-249	[»]
1A1A	X-ray	2.00	A/B	144-249	[»]
1A1B	X-ray	2.20	A/B	144-249	[»]
1A1C	X-ray	2.40	A/B	144-249	[»]
1A1E	X-ray	2.20	A/B	144-249	[»]
1FMK	X-ray	1.50	A	86-536	[»]
1HCS	NMR	-	B	144-249	[»]
1HCT	NMR	-	B	144-249	[»]
1KSW	X-ray	2.80	A	86-535	[»]
1O41	X-ray	1.70	A	145-251	[»]
1O42	X-ray	1.70	A	145-251	[»]
1O43	X-ray	1.50	A	145-251	[»]
1O44	X-ray	1.70	A	145-251	[»]
1O45	X-ray	1.80	A	145-251	[»]
1O46	X-ray	2.00	A	145-251	[»]
1O47	X-ray	1.80	A	145-251	[»]
1O48	X-ray	1.55	A	145-251	[»]
1O49	X-ray	1.70	A	145-251	[»]
1O4A	X-ray	1.50	A	145-251	[»]
1O4B	X-ray	1.85	A	145-251	[»]
1O4C	X-ray	1.80	A	145-251	[»]
1O4D	X-ray	1.85	A	145-251	[»]
1O4E	X-ray	2.00	A	145-251	[»]
1O4F	X-ray	2.00	A	145-251	[»]
1O4G	X-ray	1.55	A	145-251	[»]
1O4H	X-ray	2.25	A	145-251	[»]
1O4I	X-ray	1.75	A	145-251	[»]
1O4J	X-ray	1.70	A	145-251	[»]
1O4K	X-ray	1.57	A	145-251	[»]
1O4L	X-ray	1.65	A	145-251	[»]
1O4M	X-ray	1.60	A	145-251	[»]
1O4N	X-ray	1.60	A	145-251	[»]
1O4O	X-ray	1.70	A	145-251	[»]
1O4P	X-ray	1.90	A	145-251	[»]
1O4Q	X-ray	1.70	A	145-251	[»]
1O4R	X-ray	1.50	A	145-251	[»]
1SHD	X-ray	2.00	A	144-248	[»]
1Y57	X-ray	1.91	A	86-535	[»]
1YI6	X-ray	2.00	A/B	261-535	[»]
1YOJ	X-ray	1.95	A/B	254-535	[»]
1YOL	X-ray	2.30	A/B	254-535	[»]
1YOM	X-ray	2.90	A/B	254-535	[»]
2BDF	X-ray	2.10	A/B	258-535	[»]
2BDJ	X-ray	2.50	A	258-535	[»]
2H8H	X-ray	2.20	A	2-535	[»]
2SRC	X-ray	1.50	A	86-535	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1059N.

IntAct

P12931. 92 interactions.

STRING

P12931.

PTM databases

PhosphoSite

P12931.

2-D gel databases

OGP

P12931.

Proteomic databases

PRIDE

P12931.

Genome annotation databases

Ensembl

ENST00000358208; 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]

GeneID

6714.

KEGG

hsa:6714.

UCSC

uc002xgx.1. human.

Organism-specific databases

CTD

6714.

GeneCards

GC20P035406.

H-InvDB

HIX0015793.

HGNC

HGNC:11283. SRC.

HPA

CAB004023.

MIM

190090. gene.

PharmGKB

PA36111.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P12931.

OMA

KVDVREG.

Enzyme and pathway databases

BRENDA

2.7.10.2. 247.

Pathway_Interaction_DB

alphasynuclein_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.

Reactome

REACT_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

ArrayExpress

P12931.

Bgee

P12931.

CleanEx

HS_SRC.

Genevestigator

P12931.

GermOnline

ENSG00000197122. Homo sapiens.

Family and domain databases

InterPro

IPR000719. 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]

Gene3D

G3DSA:3.30.505.10. SH2. 1 hit.

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.

ProDom

PD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS00107. 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]

ProtoNet

Search...

Other Resources

DrugBank

DB01254. Dasatinib.

NextBio

26186.

PMAP-CutDB

P12931.

SOURCE

Search...

Entry information

Entry name

SRC_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.