Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12931 (SRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 186. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SRC
Synonyms:SRC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.14 Ref.15 Ref.16 Ref.22 Ref.28 Ref.31 Ref.35 Ref.40 Ref.46 Ref.51 Ref.52 Ref.54 Ref.59 Ref.60

Catalytic activity

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

Enzyme regulation

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. Ref.13 Ref.15 Ref.17 Ref.30 Ref.50

Subunit structure

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. Ref.15 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.31 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.43 Ref.45 Ref.46 Ref.51 Ref.53 Ref.54 Ref.59 Ref.61 Ref.65

Subcellular location

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. Ref.12 Ref.14 Ref.28

Tissue specificity

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

Domain

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

Post-translational modification

Myristoylated at Gly-2, and this is essential for targeting to membranes.

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. Ref.8 Ref.12 Ref.13 Ref.33 Ref.47 Ref.55

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. Ref.65

Involvement in disease

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

Sequence similarities

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

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processCell adhesion
Cell cycle
Host-virus interaction
Immunity
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Mitochondrion
Mitochondrion inner membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

Ras protein signal transduction

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

bone resorption

Inferred from sequence or structural similarity. Source: UniProtKB

branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to progesterone stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

forebrain development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

intracellular signal transduction

Inferred from direct assay PubMed 15248232. Source: BHF-UCL

leukocyte migration

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

negative regulation of anoikis

Inferred from mutant phenotype PubMed 22402981. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

negative regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

negative regulation of mitochondrial depolarization

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

negative regulation of protein homooligomerization

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

oogenesis

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 22732588. Source: MGI

platelet activation

Traceable author statement. Source: Reactome

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of integrin activation

Traceable author statement PubMed 19267251. Source: BHF-UCL

positive regulation of podosome assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

progesterone receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay PubMed 16441665. Source: UniProtKB

regulation of bone resorption

Traceable author statement PubMed 19267251. Source: BHF-UCL

regulation of intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

regulation of vascular permeability

Traceable author statement PubMed 19267251. Source: BHF-UCL

response to interleukin-1

Inferred from mutant phenotype PubMed 19281832. Source: BHF-UCL

signal complex assembly

Traceable author statement Ref.19. Source: ProtInc

signal transduction

Traceable author statement PubMed 10734107PubMed 9020193. Source: ProtInc

uterus development

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcaveola

Inferred from direct assay PubMed 17848177. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 16441665. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 19767770. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

late endosome

Inferred from direct assay PubMed 20605918. Source: UniProtKB

lysosome

Inferred from direct assay PubMed 20605918. Source: UniProtKB

mitochondrial inner membrane

Inferred from direct assay Ref.28. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 19767770. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 20605918. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

SH2 domain binding

Inferred from physical interaction PubMed 8070403. Source: UniProtKB

SH3/SH2 adaptor activity

Traceable author statement PubMed 9020193. Source: ProtInc

ephrin receptor binding

Inferred from physical interaction Ref.29. Source: UniProtKB

growth factor receptor binding

Inferred from physical interaction Ref.36. Source: UniProtKB

heme binding

Inferred from direct assay Ref.50. Source: UniProtKB

integrin binding

Traceable author statement PubMed 19267251. Source: BHF-UCL

ion channel binding

Inferred from physical interaction PubMed 12538589PubMed 8953041. Source: BHF-UCL

kinase activity

Traceable author statement. Source: Reactome

non-membrane spanning protein tyrosine kinase activity

Traceable author statement PubMed 19267251. Source: BHF-UCL

phosphoprotein binding

Inferred from physical interaction PubMed 16441665. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.36PubMed 19262695Ref.46Ref.51Ref.61PubMed 8070403PubMed 8681387PubMed 9763511. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 18616680. Source: UniProtKB

protein tyrosine kinase activity

Inferred from direct assay PubMed 16441665. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 19332538. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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
Htr4P972883EBI-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
PIK3R1P279865EBI-621482,EBI-79464
PTK2Q053976EBI-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

Alternative products

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

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

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

Sites

Active site3891Proton acceptor
Binding site2981ATP

Amino acid modifications

Modified residue171Phosphoserine Ref.42 Ref.48
Modified residue351Phosphoserine
Modified residue691Phosphoserine
Modified residue741Phosphothreonine
Modified residue751Phosphoserine; by CDK5 Ref.55
Modified residue1871Phosphotyrosine By similarity
Modified residue4191Phosphotyrosine; by autocatalysis; alternate Ref.8 Ref.33 Ref.47
Modified residue4191Phosphotyrosine; by FAK2; alternate By similarity
Modified residue4391Phosphotyrosine
Modified residue5111Phosphothreonine
Modified residue5221Phosphotyrosine
Modified residue5301Phosphotyrosine; by CSK Ref.12 Ref.48
Lipidation21N-myristoyl glycine Ref.12

Natural variations

Alternative sequence1171T → TRKVDVR in isoform 2.
VSP_012134
Natural variant1761L → F.
Corresponds to variant rs6018260 [ dbSNP | Ensembl ].
VAR_051699
Natural variant2371A → T. Ref.66
Corresponds to variant rs34881773 [ dbSNP | Ensembl ].
VAR_041830

Experimental info

Mutagenesis2981K → M: Kinase inactive. Abolishes ubiquitination promoted by CBLC. Ref.33

Secondary structure

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

Details...

Sequences

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

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

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

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

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

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

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

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

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

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

       490        500        510        520        530 
GYRMPCPPEC PESLHDLMCQ CWRKEPEERP TFEYLQAFLE DYFTSTEPQY QPGENL 

« Hide

Isoform 2 [UniParc].

Checksum: C12D30F8BCD5FF6B
Show »

FASTA54260,589

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"pp60c-src activation in human colon carcinoma."
Cartwright C.A., Kamps M.P., Meisler A.I., Pipas J.M., Eckhart W.
J. Clin. Invest. 83:2025-2033(1989) [PubMed] [Europe PMC] [Abstract]
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]"Butein, a specific protein tyrosine kinase inhibitor."
Yang E.B., Zhang K., Cheng L.Y., Mack P.
Biochem. Biophys. Res. Commun. 245:435-438(1998) [PubMed] [Europe PMC] [Abstract]
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]"Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes."
Luttrell L.M., Ferguson S.S.G., Daaka Y., Miller W.E., Maudsley S., Della Rocca G.J., Lin F.-T., Kawakatsu H., Owada K., Luttrell D.K., Caron M.G., Lefkowitz R.J.
Science 283:655-661(1999) [PubMed] [Europe PMC] [Abstract]
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[43]"Regulation of estrogen rapid signaling through arginine methylation by PRMT1."
Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S., Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.
Mol. Cell 31:212-221(2008) [PubMed] [Europe PMC] [Abstract]
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 BY PTPRJ AT TYR-419.
[48]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Regulation, substrates and functions of src."
Brown M.T., Cooper J.A.
Biochim. Biophys. Acta 1287:121-149(1996) [PubMed] [Europe PMC] [Abstract]
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]"Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis."
Yoshida S., Tsutsumi S., Muhlebach G., Sourbier C., Lee M.J., Lee S., Vartholomaiou E., Tatokoro M., Beebe K., Miyajima N., Mohney R.P., Chen Y., Hasumi H., Xu W., Fukushima H., Nakamura K., Koga F., Kihara K. expand/collapse author list , Trepel J., Picard D., Neckers L.
Proc. Natl. Acad. Sci. U.S.A. 110:E1604-E1612(2013) [PubMed] [Europe PMC] [Abstract]
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]"Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and structural study."
Charifson P.S., Shewchuk L.M., Rocque W., Hummel C.W., Jordan S.R., Mohr C., Pacofsky G.J., Peel M.R., Rodriguez M., Sternbach D.D., Consler T.G.
Biochemistry 36:6283-6293(1997) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-237.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , M16237, M16243, M16244, M16245, K03212, K03213, K03214, K03215, K03216, K03217 Genomic DNA. Translation: AAA60584.1.
X02647 expand/collapse EMBL AC list , X03995, X03996, X03997, X03998, X03999, X04000 Genomic DNA. Translation: CAA26485.1.
CCDSCCDS13294.1. [P12931-1]
PIRTVHUSC. A26891.
RefSeqNP_005408.1. NM_005417.4. [P12931-1]
NP_938033.1. NM_198291.2. [P12931-1]
UniGeneHs.195659.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP12931.
SMRP12931. Positions 86-536.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112592. 242 interactions.
DIPDIP-1059N.
IntActP12931. 170 interactions.
MINTMINT-93621.
STRING9606.ENSP00000350941.

Chemistry

BindingDBP12931.
ChEMBLCHEMBL2111336.
DrugBankDB01254. Dasatinib.
GuidetoPHARMACOLOGY2206.

PTM databases

PhosphoSiteP12931.

Polymorphism databases

DMDM125711.

2D gel databases

OGPP12931.

Proteomic databases

MaxQBP12931.
PaxDbP12931.
PRIDEP12931.

Protocols and materials databases

DNASU6714.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358208; ENSP00000350941; ENSG00000197122. [P12931-1]
ENST00000360723; ENSP00000353950; ENSG00000197122. [P12931-2]
ENST00000373558; ENSP00000362659; ENSG00000197122. [P12931-2]
ENST00000373567; ENSP00000362668; ENSG00000197122. [P12931-1]
ENST00000373578; ENSP00000362680; ENSG00000197122. [P12931-1]
ENST00000445403; ENSP00000408503; ENSG00000197122. [P12931-1]
GeneID6714.
KEGGhsa:6714.
UCSCuc002xgx.3. human. [P12931-1]

Organism-specific databases

CTD6714.
GeneCardsGC20P035973.
HGNCHGNC:11283. SRC.
HPACAB004023.
HPA030875.
MIM190090. gene.
neXtProtNX_P12931.
PharmGKBPA36111.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
KOK05704.
OMACQCWRKD.
OrthoDBEOG7GTT2V.
PhylomeDBP12931.
TreeFamTF351634.

Enzyme and pathway databases

BioCycMetaCyc:HS02256-MONOMER.
BRENDA2.7.10.2. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_11123. Membrane Trafficking.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP12931.

Gene expression databases

ArrayExpressP12931.
BgeeP12931.
CleanExHS_SRC.
GenevestigatorP12931.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRC. human.
EvolutionaryTraceP12931.
GeneWikiSrc_(gene).
GenomeRNAi6714.
NextBio26186.
PMAP-CutDBP12931.
PROP12931.
SOURCESearch...

Entry information

Entry nameSRC_HUMAN
AccessionPrimary (citable) accession number: P12931
Secondary accession number(s): E1P5V4 expand/collapse secondary AC list , Q76P87, Q86VB9, Q9H5A8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 186 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

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