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P12931

- SRC_HUMAN

UniProt

P12931 - SRC_HUMAN

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Protein

Proto-oncogene tyrosine-protein kinase Src

Gene

SRC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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). 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). 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. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. 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 ADRBK1, 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. 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. 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. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-128'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity.16 Publications

Catalytic activityi

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

Enzyme regulationi

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.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei298 – 2981ATP
Active sitei389 – 3891Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi276 – 2849ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: UniProtKB
  3. ephrin receptor binding Source: UniProtKB
  4. growth factor receptor binding Source: UniProtKB
  5. heme binding Source: UniProtKB
  6. integrin binding Source: BHF-UCL
  7. ion channel binding Source: BHF-UCL
  8. kinase activity Source: Reactome
  9. non-membrane spanning protein tyrosine kinase activity Source: BHF-UCL
  10. phosphoprotein binding Source: UniProtKB
  11. protein kinase activity Source: UniProtKB
  12. protein tyrosine kinase activity Source: UniProtKB
  13. receptor binding Source: UniProtKB
  14. SH2 domain binding Source: UniProtKB
  15. SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. blood coagulation Source: Reactome
  3. bone resorption Source: UniProtKB
  4. branching involved in mammary gland duct morphogenesis Source: Ensembl
  5. cell adhesion Source: UniProtKB-KW
  6. cell cycle Source: UniProtKB-KW
  7. cellular response to progesterone stimulus Source: BHF-UCL
  8. epidermal growth factor receptor signaling pathway Source: Reactome
  9. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  10. fibroblast growth factor receptor signaling pathway Source: Reactome
  11. forebrain development Source: Ensembl
  12. innate immune response Source: Reactome
  13. integrin-mediated signaling pathway Source: UniProtKB
  14. intracellular signal transduction Source: BHF-UCL
  15. leukocyte migration Source: Reactome
  16. membrane organization Source: Reactome
  17. negative regulation of anoikis Source: UniProtKB
  18. negative regulation of apoptotic process Source: UniProtKB
  19. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  20. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  21. negative regulation of focal adhesion assembly Source: BHF-UCL
  22. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  23. negative regulation of mitochondrial depolarization Source: UniProtKB
  24. negative regulation of protein homooligomerization Source: UniProtKB
  25. neurotrophin TRK receptor signaling pathway Source: Reactome
  26. oogenesis Source: Ensembl
  27. peptidyl-tyrosine phosphorylation Source: MGI
  28. platelet activation Source: Reactome
  29. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  30. positive regulation of integrin activation Source: BHF-UCL
  31. positive regulation of podosome assembly Source: Ensembl
  32. positive regulation of protein kinase B signaling Source: UniProtKB
  33. progesterone receptor signaling pathway Source: BHF-UCL
  34. protein autophosphorylation Source: UniProtKB
  35. Ras protein signal transduction Source: Reactome
  36. regulation of bone resorption Source: BHF-UCL
  37. regulation of caveolin-mediated endocytosis Source: UniProtKB
  38. regulation of cell-cell adhesion Source: UniProtKB
  39. regulation of early endosome to late endosome transport Source: UniProtKB
  40. regulation of epithelial cell migration Source: UniProtKB
  41. regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
  42. regulation of protein binding Source: Ensembl
  43. regulation of vascular permeability Source: BHF-UCL
  44. response to interleukin-1 Source: BHF-UCL
  45. signal complex assembly Source: ProtInc
  46. signal transduction Source: ProtInc
  47. stress fiber assembly Source: UniProtKB
  48. T cell costimulation Source: Reactome
  49. transforming growth factor beta receptor signaling pathway Source: UniProtKB
  50. uterus development Source: Ensembl
  51. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell adhesion, Cell cycle, Host-virus interaction, Immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02256-MONOMER.
BRENDAi2.7.10.2. 2681.
ReactomeiREACT_11043. c-src mediated regulation of Cx43 function and closure of gap junctions.
REACT_111040. Signaling by SCF-KIT.
REACT_111080. Spry regulation of FGF signaling.
REACT_111225. Regulation of KIT signaling.
REACT_115755. Signaling by ERBB2.
REACT_12065. p38MAPK events.
REACT_12519. PECAM1 interactions.
REACT_12578. GAB1 signalosome.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_160274. FCGR activation.
REACT_17025. Downstream signal transduction.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_19140. ADP signalling through P2Y purinoceptor 1.
REACT_19183. CD28 co-stimulation.
REACT_19405. CTLA4 inhibitory signaling.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
REACT_22351. DCC mediated attractive signaling.
REACT_22365. Recycling pathway of L1.
REACT_22384. Netrin mediated repulsion signals.
REACT_228024. VEGFR2 mediated cell proliferation.
REACT_228063. EPHA-mediated growth cone collapse.
REACT_228085. EPHB-mediated forward signaling.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_228226. Ephrin signaling.
REACT_23847. GP1b-IX-V activation signalling.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
REACT_9417. Signaling by EGFR.
SignaLinkiP12931.

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene tyrosine-protein kinase Src (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Src
pp60c-src
Short name:
p60-Src
Gene namesi
Name:SRC
Synonyms:SRC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:11283. SRC.

Subcellular locationi

Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasmcytoskeleton
Note: Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain.

GO - Cellular componenti

  1. caveola Source: BHF-UCL
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-KW
  4. cytosol Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. late endosome Source: UniProtKB
  7. lysosome Source: UniProtKB
  8. mitochondrial inner membrane Source: UniProtKB
  9. mitochondrion Source: UniProtKB
  10. nucleus Source: UniProtKB-KW
  11. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

SRC kinase activity has been shown to be increased in several tumor tissues and tumor cell lines such as colon carcinoma cells.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi298 – 2981K → M: Kinase inactive. Abolishes ubiquitination promoted by CBLC. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA36111.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 536535Proto-oncogene tyrosine-protein kinase SrcPRO_0000088141Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei17 – 171Phosphoserine2 Publications
Modified residuei35 – 351Phosphoserine1 Publication
Modified residuei69 – 691Phosphoserine1 Publication
Modified residuei74 – 741Phosphothreonine1 Publication
Modified residuei75 – 751Phosphoserine; by CDK51 Publication
Modified residuei187 – 1871PhosphotyrosineBy similarity
Modified residuei419 – 4191Phosphotyrosine; by autocatalysis; alternate3 Publications
Modified residuei419 – 4191Phosphotyrosine; by FAK2; alternateBy similarity
Modified residuei439 – 4391Phosphotyrosine1 Publication
Modified residuei511 – 5111Phosphothreonine1 Publication
Modified residuei522 – 5221Phosphotyrosine1 Publication
Modified residuei530 – 5301Phosphotyrosine; by CSK2 Publications

Post-translational modificationi

Myristoylated at Gly-2, and this is essential for targeting to membranes.1 Publication
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.By similarity7 Publications
S-nitrosylation is important for activation of its kinase activity.By similarity
Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation.4 Publications

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP12931.
PaxDbiP12931.
PRIDEiP12931.

2D gel databases

OGPiP12931.

PTM databases

PhosphoSiteiP12931.

Miscellaneous databases

PMAP-CutDBP12931.

Expressioni

Tissue specificityi

Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues.

Gene expression databases

BgeeiP12931.
CleanExiHS_SRC.
ExpressionAtlasiP12931. baseline and differential.
GenevestigatoriP12931.

Organism-specific databases

HPAiCAB004023.
HPA030875.

Interactioni

Subunit structurei

Interacts with DDEF1/ASAP1; via the SH3 domain. Interacts with CCPG1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ERBB2, STAT1 and PNN. Interacts with DDR1, DDR2 and DAB2. 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). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with ARRB1 and ARRB2. Interacts with SRCIN1. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and ESR1 (dimethylated on arginine). Interacts with FASLG. Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with PDGFRA (tyrosine phosphorylated). Interacts with CSF1R. Interacts (via SH2 and SH3 domain) with TNK2. Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain). Interacts with TRAF3 (via RING-type zinc finger domain). Interacts with DDX58, MAVS and TBK1. Interacts (via SH2 domain) with GNB2L1/RACK1; the interaction is enhanced by tyrosine phosphorylation of GNB2L1 and inhibits SRC activity. Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration. Interacts with FCAMR. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Interacts with TRAP1. Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at Tyr-419.29 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-621482,EBI-375543
ABL2P426842EBI-621482,EBI-1102694
ACTN1P128142EBI-621482,EBI-351710
ADAM15Q134443EBI-621482,EBI-77818
ADRB2P075503EBI-621482,EBI-491169
ARP102757EBI-621482,EBI-608057
Arap3Q8R5G73EBI-621482,EBI-621463From a different organism.
ASAP1Q9ULH13EBI-621482,EBI-346622
BCAR1P569453EBI-621482,EBI-702093
CBLP226818EBI-621482,EBI-518228
CDH1P128302EBI-621482,EBI-727477
Efnb2P528002EBI-621482,EBI-1032676From a different organism.
EGFRP005337EBI-621482,EBI-297353
ERBB2P0462611EBI-621482,EBI-641062
ERBB3P218602EBI-621482,EBI-720706
ESR1P033729EBI-621482,EBI-78473
ESR1P03372-42EBI-621482,EBI-4309277
ETS1P14921-12EBI-621482,EBI-913224
FASP254452EBI-621482,EBI-494743
FBXO18Q8NFZ04EBI-621482,EBI-724767
GAB1Q1348012EBI-621482,EBI-517684
HNRNPKP619786EBI-621482,EBI-304185
Htr4P972882EBI-621482,EBI-7149283From a different organism.
IKBKGQ9Y6K93EBI-621482,EBI-81279
KDRP359682EBI-621482,EBI-1005487
KHDRBS1Q076663EBI-621482,EBI-1364
KITP107215EBI-621482,EBI-1379503
LNX1Q8TBB16EBI-621482,EBI-739832
MED28Q9H2043EBI-621482,EBI-514199
METP085814EBI-621482,EBI-1039152
MLLT4P551967EBI-621482,EBI-365875
PAK2Q131772EBI-621482,EBI-1045887
PECAM1P162843EBI-621482,EBI-716404
PIK3R1P279866EBI-621482,EBI-79464
PTK2Q053977EBI-621482,EBI-702142
Ptk2P341522EBI-621482,EBI-77070From a different organism.
PTK2BQ142893EBI-621482,EBI-298640
PTPN1P1803114EBI-621482,EBI-968788
PTPN21Q168252EBI-621482,EBI-2860264
PTPRAP184334EBI-621482,EBI-2609645
PtpraP180523EBI-621482,EBI-6597520From a different organism.
PtprjQ628843EBI-621482,EBI-7459400From a different organism.
RAPGEF1Q139052EBI-621482,EBI-976876
ROR1Q019739EBI-621482,EBI-6082337
RPL10P276356EBI-621482,EBI-352398
SPRR2AP353263EBI-621482,EBI-1047940
SRCIN1Q9C0H93EBI-621482,EBI-1393949
TNS3Q68CZ213EBI-621482,EBI-1220488

Protein-protein interaction databases

BioGridi112592. 252 interactions.
DIPiDIP-1059N.
IntActiP12931. 172 interactions.
MINTiMINT-93621.
STRINGi9606.ENSP00000350941.

Structurei

Secondary structure

1
536
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi87 – 937Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi110 – 1145Combined sources
Beta strandi118 – 1269Combined sources
Turni127 – 1293Combined sources
Beta strandi132 – 1365Combined sources
Helixi137 – 1393Combined sources
Beta strandi140 – 1423Combined sources
Helixi146 – 1483Combined sources
Beta strandi152 – 1543Combined sources
Helixi158 – 1658Combined sources
Beta strandi167 – 1704Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi187 – 1959Combined sources
Turni196 – 1983Combined sources
Beta strandi199 – 20911Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi215 – 2184Combined sources
Beta strandi221 – 2255Combined sources
Helixi226 – 2338Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi256 – 2594Combined sources
Helixi267 – 2693Combined sources
Beta strandi270 – 2789Combined sources
Beta strandi283 – 2897Combined sources
Turni290 – 2923Combined sources
Beta strandi293 – 2997Combined sources
Turni302 – 3043Combined sources
Helixi307 – 31913Combined sources
Beta strandi328 – 3325Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi338 – 3414Combined sources
Helixi349 – 3535Combined sources
Helixi355 – 3584Combined sources
Helixi363 – 38220Combined sources
Helixi392 – 3943Combined sources
Beta strandi395 – 3973Combined sources
Helixi399 – 4013Combined sources
Beta strandi403 – 4053Combined sources
Helixi410 – 4134Combined sources
Helixi417 – 4204Combined sources
Turni423 – 4264Combined sources
Helixi429 – 4313Combined sources
Helixi434 – 4396Combined sources
Helixi444 – 45916Combined sources
Turni460 – 4623Combined sources
Helixi471 – 4799Combined sources
Helixi492 – 50110Combined sources
Helixi506 – 5083Combined sources
Helixi512 – 5209Combined sources
Turni521 – 5233Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray2.80A86-536[»]
1O41X-ray1.70A145-252[»]
1O42X-ray1.70A145-252[»]
1O43X-ray1.50A145-252[»]
1O44X-ray1.70A145-252[»]
1O45X-ray1.80A145-252[»]
1O46X-ray2.00A145-252[»]
1O47X-ray1.80A145-252[»]
1O48X-ray1.55A145-252[»]
1O49X-ray1.70A145-252[»]
1O4AX-ray1.50A145-252[»]
1O4BX-ray1.85A145-252[»]
1O4CX-ray1.80A145-252[»]
1O4DX-ray1.85A145-252[»]
1O4EX-ray2.00A145-252[»]
1O4FX-ray2.00A145-252[»]
1O4GX-ray1.55A145-252[»]
1O4HX-ray2.25A145-252[»]
1O4IX-ray1.75A145-252[»]
1O4JX-ray1.70A145-252[»]
1O4KX-ray1.57A145-252[»]
1O4LX-ray1.65A145-252[»]
1O4MX-ray1.60A145-252[»]
1O4NX-ray1.60A145-252[»]
1O4OX-ray1.70A145-252[»]
1O4PX-ray1.90A145-252[»]
1O4QX-ray1.70A145-252[»]
1O4RX-ray1.50A145-252[»]
1SHDX-ray2.00A144-249[»]
1Y57X-ray1.91A86-536[»]
1YI6X-ray2.00A/B261-536[»]
1YOJX-ray1.95A/B254-536[»]
1YOLX-ray2.30A/B254-536[»]
1YOMX-ray2.90A/B254-536[»]
2BDFX-ray2.10A/B258-536[»]
2BDJX-ray2.50A258-536[»]
2H8HX-ray2.20A2-536[»]
2SRCX-ray1.50A86-536[»]
3VROX-ray1.80B412-424[»]
3ZMPX-ray2.62C/D527-536[»]
3ZMQX-ray3.30C527-536[»]
4F59X-ray1.71A144-252[»]
4F5AX-ray1.80A144-252[»]
4F5BX-ray1.57A144-252[»]
4HXJX-ray2.00A/B87-144[»]
4K11X-ray2.30A87-534[»]
4MXOX-ray2.10A/B254-536[»]
4MXXX-ray2.60A/B254-536[»]
4MXYX-ray2.58A/B254-536[»]
4MXZX-ray2.58A/B254-536[»]
ProteinModelPortaliP12931.
SMRiP12931. Positions 86-536.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12931.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 14562SH3PROSITE-ProRule annotationAdd
BLAST
Domaini151 – 24898SH2PROSITE-ProRule annotationAdd
BLAST
Domaini270 – 523254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The SH2 and SH3 domains are important for the intramolecular and intermolecular interactions that regulate catalytic activity, localization, and substrate recruitment.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP12931.
KOiK05704.
OMAiCQCWRKD.
OrthoDBiEOG7GTT2V.
PhylomeDBiP12931.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P12931-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGSNKSKPKD ASQRRRSLEP AENVHGAGGG AFPASQTPSK PASADGHRGP
60 70 80 90 100
SAAFAPAAAE PKLFGGFNSS DTVTSPQRAG PLAGGVTTFV ALYDYESRTE
110 120 130 140 150
TDLSFKKGER LQIVNNTEGD WWLAHSLSTG QTGYIPSNYV APSDSIQAEE
160 170 180 190 200
WYFGKITRRE SERLLLNAEN PRGTFLVRES ETTKGAYCLS VSDFDNAKGL
210 220 230 240 250
NVKHYKIRKL DSGGFYITSR TQFNSLQQLV AYYSKHADGL CHRLTTVCPT
260 270 280 290 300
SKPQTQGLAK DAWEIPRESL RLEVKLGQGC FGEVWMGTWN GTTRVAIKTL
310 320 330 340 350
KPGTMSPEAF LQEAQVMKKL RHEKLVQLYA VVSEEPIYIV TEYMSKGSLL
360 370 380 390 400
DFLKGETGKY LRLPQLVDMA AQIASGMAYV ERMNYVHRDL RAANILVGEN
410 420 430 440 450
LVCKVADFGL ARLIEDNEYT ARQGAKFPIK WTAPEAALYG RFTIKSDVWS
460 470 480 490 500
FGILLTELTT KGRVPYPGMV NREVLDQVER GYRMPCPPEC PESLHDLMCQ
510 520 530
CWRKEPEERP TFEYLQAFLE DYFTSTEPQY QPGENL
Length:536
Mass (Da):59,835
Last modified:January 23, 2007 - v3
Checksum:iC1908084683E5DE8
GO
Isoform 2 (identifier: P12931-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:542
Mass (Da):60,589
Checksum:iC12D30F8BCD5FF6B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti176 – 1761L → F.
Corresponds to variant rs6018260 [ dbSNP | Ensembl ].
VAR_051699
Natural varianti237 – 2371A → T.1 Publication
Corresponds to variant rs34881773 [ dbSNP | Ensembl ].
VAR_041830

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei117 – 1171T → TRKVDVR in isoform 2. 1 PublicationVSP_012134

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL133293 Genomic DNA. Translation: CAC10573.1.
AL133293 Genomic DNA. Translation: CAC34523.1.
CH471077 Genomic DNA. Translation: EAW76065.1.
CH471077 Genomic DNA. Translation: EAW76064.1.
CH471077 Genomic DNA. Translation: EAW76066.1.
CH471077 Genomic DNA. Translation: EAW76067.1.
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.
CCDSiCCDS13294.1. [P12931-1]
PIRiA26891. TVHUSC.
RefSeqiNP_005408.1. NM_005417.4. [P12931-1]
NP_938033.1. NM_198291.2. [P12931-1]
UniGeneiHs.195659.

Genome annotation databases

EnsembliENST00000358208; ENSP00000350941; ENSG00000197122. [P12931-1]
ENST00000373558; ENSP00000362659; ENSG00000197122. [P12931-2]
ENST00000373567; ENSP00000362668; ENSG00000197122. [P12931-1]
ENST00000373578; ENSP00000362680; ENSG00000197122. [P12931-1]
GeneIDi6714.
KEGGihsa:6714.
UCSCiuc002xgx.3. human. [P12931-1]

Polymorphism databases

DMDMi125711.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL133293 Genomic DNA. Translation: CAC10573.1 .
AL133293 Genomic DNA. Translation: CAC34523.1 .
CH471077 Genomic DNA. Translation: EAW76065.1 .
CH471077 Genomic DNA. Translation: EAW76064.1 .
CH471077 Genomic DNA. Translation: EAW76066.1 .
CH471077 Genomic DNA. Translation: EAW76067.1 .
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 .
CCDSi CCDS13294.1. [P12931-1 ]
PIRi A26891. TVHUSC.
RefSeqi NP_005408.1. NM_005417.4. [P12931-1 ]
NP_938033.1. NM_198291.2. [P12931-1 ]
UniGenei Hs.195659.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 86-536 [» ]
1O41 X-ray 1.70 A 145-252 [» ]
1O42 X-ray 1.70 A 145-252 [» ]
1O43 X-ray 1.50 A 145-252 [» ]
1O44 X-ray 1.70 A 145-252 [» ]
1O45 X-ray 1.80 A 145-252 [» ]
1O46 X-ray 2.00 A 145-252 [» ]
1O47 X-ray 1.80 A 145-252 [» ]
1O48 X-ray 1.55 A 145-252 [» ]
1O49 X-ray 1.70 A 145-252 [» ]
1O4A X-ray 1.50 A 145-252 [» ]
1O4B X-ray 1.85 A 145-252 [» ]
1O4C X-ray 1.80 A 145-252 [» ]
1O4D X-ray 1.85 A 145-252 [» ]
1O4E X-ray 2.00 A 145-252 [» ]
1O4F X-ray 2.00 A 145-252 [» ]
1O4G X-ray 1.55 A 145-252 [» ]
1O4H X-ray 2.25 A 145-252 [» ]
1O4I X-ray 1.75 A 145-252 [» ]
1O4J X-ray 1.70 A 145-252 [» ]
1O4K X-ray 1.57 A 145-252 [» ]
1O4L X-ray 1.65 A 145-252 [» ]
1O4M X-ray 1.60 A 145-252 [» ]
1O4N X-ray 1.60 A 145-252 [» ]
1O4O X-ray 1.70 A 145-252 [» ]
1O4P X-ray 1.90 A 145-252 [» ]
1O4Q X-ray 1.70 A 145-252 [» ]
1O4R X-ray 1.50 A 145-252 [» ]
1SHD X-ray 2.00 A 144-249 [» ]
1Y57 X-ray 1.91 A 86-536 [» ]
1YI6 X-ray 2.00 A/B 261-536 [» ]
1YOJ X-ray 1.95 A/B 254-536 [» ]
1YOL X-ray 2.30 A/B 254-536 [» ]
1YOM X-ray 2.90 A/B 254-536 [» ]
2BDF X-ray 2.10 A/B 258-536 [» ]
2BDJ X-ray 2.50 A 258-536 [» ]
2H8H X-ray 2.20 A 2-536 [» ]
2SRC X-ray 1.50 A 86-536 [» ]
3VRO X-ray 1.80 B 412-424 [» ]
3ZMP X-ray 2.62 C/D 527-536 [» ]
3ZMQ X-ray 3.30 C 527-536 [» ]
4F59 X-ray 1.71 A 144-252 [» ]
4F5A X-ray 1.80 A 144-252 [» ]
4F5B X-ray 1.57 A 144-252 [» ]
4HXJ X-ray 2.00 A/B 87-144 [» ]
4K11 X-ray 2.30 A 87-534 [» ]
4MXO X-ray 2.10 A/B 254-536 [» ]
4MXX X-ray 2.60 A/B 254-536 [» ]
4MXY X-ray 2.58 A/B 254-536 [» ]
4MXZ X-ray 2.58 A/B 254-536 [» ]
ProteinModelPortali P12931.
SMRi P12931. Positions 86-536.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112592. 252 interactions.
DIPi DIP-1059N.
IntActi P12931. 172 interactions.
MINTi MINT-93621.
STRINGi 9606.ENSP00000350941.

Chemistry

BindingDBi P12931.
ChEMBLi CHEMBL2363074.
DrugBanki DB06616. Bosutinib.
DB01254. Dasatinib.
DB08901. Ponatinib.
GuidetoPHARMACOLOGYi 2206.

PTM databases

PhosphoSitei P12931.

Polymorphism databases

DMDMi 125711.

2D gel databases

OGPi P12931.

Proteomic databases

MaxQBi P12931.
PaxDbi P12931.
PRIDEi P12931.

Protocols and materials databases

DNASUi 6714.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358208 ; ENSP00000350941 ; ENSG00000197122 . [P12931-1 ]
ENST00000373558 ; ENSP00000362659 ; ENSG00000197122 . [P12931-2 ]
ENST00000373567 ; ENSP00000362668 ; ENSG00000197122 . [P12931-1 ]
ENST00000373578 ; ENSP00000362680 ; ENSG00000197122 . [P12931-1 ]
GeneIDi 6714.
KEGGi hsa:6714.
UCSCi uc002xgx.3. human. [P12931-1 ]

Organism-specific databases

CTDi 6714.
GeneCardsi GC20P035973.
HGNCi HGNC:11283. SRC.
HPAi CAB004023.
HPA030875.
MIMi 190090. gene.
neXtProti NX_P12931.
PharmGKBi PA36111.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118938.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi P12931.
KOi K05704.
OMAi CQCWRKD.
OrthoDBi EOG7GTT2V.
PhylomeDBi P12931.
TreeFami TF351634.

Enzyme and pathway databases

BioCyci MetaCyc:HS02256-MONOMER.
BRENDAi 2.7.10.2. 2681.
Reactomei REACT_11043. c-src mediated regulation of Cx43 function and closure of gap junctions.
REACT_111040. Signaling by SCF-KIT.
REACT_111080. Spry regulation of FGF signaling.
REACT_111225. Regulation of KIT signaling.
REACT_115755. Signaling by ERBB2.
REACT_12065. p38MAPK events.
REACT_12519. PECAM1 interactions.
REACT_12578. GAB1 signalosome.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_160274. FCGR activation.
REACT_17025. Downstream signal transduction.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_19140. ADP signalling through P2Y purinoceptor 1.
REACT_19183. CD28 co-stimulation.
REACT_19405. CTLA4 inhibitory signaling.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
REACT_22351. DCC mediated attractive signaling.
REACT_22365. Recycling pathway of L1.
REACT_22384. Netrin mediated repulsion signals.
REACT_228024. VEGFR2 mediated cell proliferation.
REACT_228063. EPHA-mediated growth cone collapse.
REACT_228085. EPHB-mediated forward signaling.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_228226. Ephrin signaling.
REACT_23847. GP1b-IX-V activation signalling.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
REACT_9417. Signaling by EGFR.
SignaLinki P12931.

Miscellaneous databases

ChiTaRSi SRC. human.
EvolutionaryTracei P12931.
GeneWikii Src_(gene).
GenomeRNAii 6714.
NextBioi 26186.
PMAP-CutDB P12931.
PROi P12931.
SOURCEi Search...

Gene expression databases

Bgeei P12931.
CleanExi HS_SRC.
ExpressionAtlasi P12931. baseline and differential.
Genevestigatori P12931.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Skin.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185 (ISOFORM 1).
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-536 (ISOFORM 1).
  6. "Neuron-specific splicing of C-SRC RNA in human brain."
    Pyper J.M., Bolen J.B.
    J. Neurosci. Res. 24:89-96(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 98-139 (ISOFORM 2).
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-536 (ISOFORM 1).
  8. "Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src)."
    Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F., Erikson R.L., Bishop J.M.
    Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-419.
  9. "Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues."
    Rosen N., Bolen J.B., Schwartz A.M., Cohen P., DeSeau V., Israel M.A.
    J. Biol. Chem. 261:13754-13759(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN TUMOR TISSUES.
  10. Cited for: ROLE IN COLON CARCINOMA.
  11. "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] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  12. "Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527."
    Kaplan K.B., Bibbins K.B., Swedlow J.R., Arnaud M., Morgan D.O., Varmus H.E.
    EMBO J. 13:4745-4756(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-530, MYRISTOYLATION AT GLY-2.
  13. "Cdc2-mediated modulation of pp60c-src activity."
    Stover D.R., Liebetanz J., Lydon N.B.
    J. Biol. Chem. 269:26885-26889(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, ENZYME REGULATION.
  14. "Highly specific antibody to Rous sarcoma virus src gene product recognizes nuclear and nucleolar antigens in human cells."
    David-Pfeuty T., Nouvian-Dooghe Y.
    J. Virol. 69:1699-1713(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  15. "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."
    Rabinowich H., Manciulea M., Metes D., Sulica A., Herberman R.B., Corey S.J., Whiteside T.L.
    J. Immunol. 157:1485-1491(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCAMR, ENZYME REGULATION, FUNCTION.
  16. "Hepatocyte growth factor is a coupling factor for osteoclasts and osteoblasts in vitro."
    Grano M., Galimi F., Zambonin G., Colucci S., Cottone E., Zallone A.Z., Comoglio P.M.
    Proc. Natl. Acad. Sci. U.S.A. 93:7644-7648(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HGF SIGNALING PATHWAY.
  17. Cited for: ENZYME REGULATION.
  18. "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."
    Chang B.Y., Conroy K.B., Machleder E.M., Cartwright C.A.
    Mol. Cell. Biol. 18:3245-3256(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GNB2L1.
  19. Cited for: INTERACTION WITH ADRB2 AND ARRB1.
  20. "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."
    Miller W.E., Maudsley S., Ahn S., Khan K.D., Luttrell L.M., Lefkowitz R.J.
    J. Biol. Chem. 275:11312-11319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB1 AND ARRB2.
  21. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALGPS1.
  22. "Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm."
    Giglione C., Gonfloni S., Parmeggiani A.
    Eur. J. Biochem. 268:3275-3283(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RASA1 AND RASGRF1.
  23. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MUC1.
  24. "The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1."
    Chang B.Y., Chiang M., Cartwright C.A.
    J. Biol. Chem. 276:20346-20356(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GNB2L1.
  25. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
  26. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV2.
  27. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PELP1.
  28. "Regulation of cytochrome c oxidase activity by c-Src in osteoclasts."
    Miyazaki T., Neff L., Tanaka S., Horne W.C., Baron R.
    J. Cell Biol. 160:709-718(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  29. "EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis."
    Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.
    J. Cell Biol. 162:661-671(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPHB1.
  30. "Development and characterization of potent and specific peptide inhibitors of p60c-src protein tyrosine kinase using pseudosubstrate-based inhibitor design approach."
    Kamath J.R., Liu R., Enstrom A.M., Lou Q., Lam K.S.
    J. Pept. Res. 62:260-268(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  31. "Pyk2- and Src-dependent tyrosine phosphorylation of PDK1 regulates focal adhesions."
    Taniyama Y., Weber D.S., Rocic P., Hilenski L., Akers M.L., Park J., Hemmings B.A., Alexander R.W., Griendling K.K.
    Mol. Cell. Biol. 23:8019-8029(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PDPK1, INTERACTION WITH PTK2B/PYK2.
  32. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV2.
  33. "Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation."
    Kim M., Tezuka T., Tanaka K., Yamamoto T.
    Oncogene 23:1645-1655(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBCLC, PHOSPHORYLATION AT TYR-419, MUTAGENESIS OF LYS-298.
  34. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDCP1.
  35. "Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src stimulates intramolecular autophosphorylation and Shc signaling complex formation."
    Yang K., Kim J.H., Kim H.J., Park I.S., Kim I.Y., Yang B.S.
    J. Biol. Chem. 280:39058-39066(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DDR2.
  36. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOM1L2.
  37. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  38. "Amotl2 is essential for cell movements in zebrafish embryo and regulates c-Src translocation."
    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.
    Development 134:979-988(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AMOTL2.
  39. "p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity."
    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.
    EMBO J. 26:2843-2855(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRCIN1.
  40. "EGF mediates calcium-activated chloride channel activation in the human bronchial epithelial cell line 16HBE14o-: involvement of tyrosine kinase p60c-src."
    Jeulin C., Seltzer V., Bailbe D., Andreau K., Marano F.
    Am. J. Physiol. 295:L489-L496(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  41. "Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding."
    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.
    J. Biol. Chem. 283:1480-1491(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDPK1.
  42. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  43. Cited for: INTERACTION WITH PTK2/FAK1; PI3KR1/2 AND ESR1.
  44. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  45. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  46. "The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling."
    Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.
    J. Biol. Chem. 284:19122-19131(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRAF3; MAVS; DDX58 AND TBK1.
  47. "New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival."
    Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.
    Mol. Cell. Biol. 29:241-253(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-419, DEPHOSPHORYLATION AT TYR-419 BY PTPRJ.
  48. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND TYR-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  49. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  50. "Heme controls the regulation of protein tyrosine kinases Jak2 and Src."
    Yao X., Balamurugan P., Arvey A., Leslie C., Zhang L.
    Biochem. Biophys. Res. Commun. 403:30-35(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  51. "Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm."
    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.
    J. Biol. Chem. 285:10122-10129(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RUNX3.
  52. "The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme."
    Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.
    J. Biol. Chem. 285:23687-23698(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CBLC PHOSPHORYLATION.
  53. "Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2."
    Mund T., Pelham H.R.
    Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NDFIP1 AND NDFIP2.
  54. "The Cdc42-associated kinase ACK1 is not auto-inhibited but requires Src for activation."
    Chan W., Sit S.T., Manser E.
    Biochem. J. 435:355-364(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TNK2.
  55. "Cdk5 targets active Src for ubiquitin-dependent degradation by phosphorylating Src(S75)."
    Pan Q., Qiao F., Gao C., Norman B., Optican L., Zelenka P.S.
    Cell. Mol. Life Sci. 68:3425-3436(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-75.
  56. Cited for: REVIEW ON FUNCTION.
  57. "Cellular functions regulated by Src family kinases."
    Thomas S.M., Brugge J.S.
    Annu. Rev. Cell Dev. Biol. 13:513-609(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  58. "Novel regulation and function of Src tyrosine kinase."
    Ma Y.C., Huang X.Y.
    Cell. Mol. Life Sci. 59:456-462(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  59. "A direct interaction between the large GTPase dynamin-2 and FAK regulates focal adhesion dynamics in response to active Src."
    Wang Y., Cao H., Chen J., McNiven M.A.
    Mol. Biol. Cell 22:1529-1538(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FOCAL ADHESION DYNAMICS, INTERACTION WITH PTK2/FAK1 AND DNM2.
  60. "Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14."
    Zhang P., Guo A., Possemato A., Wang C., Beard L., Carlin C., Markowitz S.D., Polakiewicz R.D., Wang Z.
    Oncogene 32:2087-2095(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BCAR1.
  61. Cited for: INTERACTION WITH TRAP1.
  62. "Three-dimensional structure of the tyrosine kinase c-Src."
    Xu W., Harrison S.C., Eck M.J.
    Nature 385:595-602(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 86-536.
  63. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 145-249.
  64. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 204-249.
  65. "Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c."
    Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M., Yamanashi Y., Yamamoto T., Nakagawa A.
    J. Biochem. 152:487-495(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 412-424 IN COMPLEX WITH CBLC, UBIQUITINATION, INTERACTION WITH CBLC.
  66. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-237.

Entry informationi

Entry nameiSRC_HUMAN
AccessioniPrimary (citable) accession number: P12931
Secondary accession number(s): E1P5V4
, Q76P87, Q86VB9, Q9H5A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 190 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3