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P12931

- SRC_HUMAN

UniProt

P12931 - SRC_HUMAN

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
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    • History
      Entry version 188 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. ephrin receptor binding Source: UniProtKB
    3. growth factor receptor binding Source: UniProtKB
    4. heme binding Source: UniProtKB
    5. integrin binding Source: BHF-UCL
    6. ion channel binding Source: BHF-UCL
    7. kinase activity Source: Reactome
    8. non-membrane spanning protein tyrosine kinase activity Source: BHF-UCL
    9. phosphoprotein binding Source: UniProtKB
    10. protein 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. intracellular signal transduction Source: BHF-UCL
    14. leukocyte migration Source: Reactome
    15. membrane organization Source: Reactome
    16. negative regulation of anoikis Source: UniProtKB
    17. negative regulation of apoptotic process Source: UniProtKB
    18. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    19. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    20. negative regulation of focal adhesion assembly Source: BHF-UCL
    21. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    22. negative regulation of mitochondrial depolarization Source: UniProtKB
    23. negative regulation of protein homooligomerization Source: UniProtKB
    24. neurotrophin TRK receptor signaling pathway Source: Reactome
    25. oogenesis Source: Ensembl
    26. peptidyl-tyrosine phosphorylation Source: MGI
    27. platelet activation Source: Reactome
    28. positive regulation of canonical Wnt signaling pathway Source: Ensembl
    29. positive regulation of ERK1 and ERK2 cascade 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 intracellular estrogen receptor signaling pathway Source: Ensembl
    38. regulation of protein binding Source: Ensembl
    39. regulation of vascular permeability Source: BHF-UCL
    40. response to interleukin-1 Source: BHF-UCL
    41. signal complex assembly Source: ProtInc
    42. signal transduction Source: ProtInc
    43. T cell costimulation Source: Reactome
    44. uterus development Source: Ensembl
    45. viral process Source: UniProtKB-KW

    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_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-SubCell
    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-SubCell
    11. plasma membrane Source: UniProtKB

    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 – 171Phosphoserine3 Publications
    Modified residuei35 – 351Phosphoserine1 Publication
    Modified residuei69 – 691Phosphoserine1 Publication
    Modified residuei74 – 741Phosphothreonine1 Publication
    Modified residuei75 – 751Phosphoserine; by CDK52 Publications
    Modified residuei187 – 1871PhosphotyrosineBy similarity
    Modified residuei419 – 4191Phosphotyrosine; by autocatalysis; alternate4 Publications
    Modified residuei419 – 4191Phosphotyrosine; by FAK2; alternateBy similarity
    Modified residuei439 – 4391Phosphotyrosine1 Publication
    Modified residuei511 – 5111Phosphothreonine1 Publication
    Modified residuei522 – 5221Phosphotyrosine1 Publication
    Modified residuei530 – 5301Phosphotyrosine; by CSK3 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

    ArrayExpressiP12931.
    BgeeiP12931.
    CleanExiHS_SRC.
    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.
    EGFRP005336EBI-621482,EBI-297353
    ERBB2P0462611EBI-621482,EBI-641062
    ERBB3P218602EBI-621482,EBI-720706
    ESR1P033729EBI-621482,EBI-78473
    ESR1P03372-42EBI-621482,EBI-4309277
    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. 242 interactions.
    DIPiDIP-1059N.
    IntActiP12931. 171 interactions.
    MINTiMINT-93621.
    STRINGi9606.ENSP00000350941.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    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

    MGSNKSKPKD ASQRRRSLEP AENVHGAGGG AFPASQTPSK PASADGHRGP    50
    SAAFAPAAAE PKLFGGFNSS DTVTSPQRAG PLAGGVTTFV ALYDYESRTE 100
    TDLSFKKGER LQIVNNTEGD WWLAHSLSTG QTGYIPSNYV APSDSIQAEE 150
    WYFGKITRRE SERLLLNAEN PRGTFLVRES ETTKGAYCLS VSDFDNAKGL 200
    NVKHYKIRKL DSGGFYITSR TQFNSLQQLV AYYSKHADGL CHRLTTVCPT 250
    SKPQTQGLAK DAWEIPRESL RLEVKLGQGC FGEVWMGTWN GTTRVAIKTL 300
    KPGTMSPEAF LQEAQVMKKL RHEKLVQLYA VVSEEPIYIV TEYMSKGSLL 350
    DFLKGETGKY LRLPQLVDMA AQIASGMAYV ERMNYVHRDL RAANILVGEN 400
    LVCKVADFGL ARLIEDNEYT ARQGAKFPIK WTAPEAALYG RFTIKSDVWS 450
    FGILLTELTT KGRVPYPGMV NREVLDQVER GYRMPCPPEC PESLHDLMCQ 500
    CWRKEPEERP TFEYLQAFLE DYFTSTEPQY QPGENL 536
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 242 interactions.
    DIPi DIP-1059N.
    IntActi P12931. 171 interactions.
    MINTi MINT-93621.
    STRINGi 9606.ENSP00000350941.

    Chemistry

    BindingDBi P12931.
    ChEMBLi CHEMBL2111336.
    DrugBanki DB01254. Dasatinib.
    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.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    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_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

    ArrayExpressi P12931.
    Bgeei P12931.
    CleanExi HS_SRC.
    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

    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: October 1, 2014
    This is version 188 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