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P05480 (SRC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuronal 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length541 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-132'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Ref.7 Ref.9 Ref.13 Ref.15

Catalytic activity

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

Enzyme regulation

Phosphorylation by CSK at Tyr-535 inhibits kinase activity. Inhibitory phosphorylation at Tyr-535 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-424 increases kinase activity. Ref.8

Subunit structure

Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2. Interacts with DDEF1/ASAP1 via its SH3 domain. Interacts with CCPG1. Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin. Interacts with RALGPS1 via its 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 FCAMR and PXN. Interacts with ARRB2. Interacts with ARRB1. Interacts with SRCIN1. Interacts with SRCIN1. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1, ESR1 (dimethylated on arginine) and FAK. 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 (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration. Interacts with ERBB2 and STAT1. Interacts with PDGFRA (tyrosine phosphorylated). Interacts with CSF1R. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with DDR2. Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Interacts with DDR1 and DAB2. Interacts with TRAP1. Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at 'Tyr-424'. Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21

Subcellular location

Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasmcytoskeleton. Note: Localizes to focal adhesion sites after integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain. Ref.13

Post-translational modification

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

Dephosphorylated at Tyr-535 by PTPRJ By similarity. Phosphorylated on Tyr-535 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-424. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-535, the SH3 domain engaged with the SH2-kinase linker, and Tyr-424 dephosphorylated. Dephosphorylation of Tyr-535 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-535, Tyr-424 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-535 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-74 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 similarity.

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-424 and may lead to lysosomal degradation By similarity.

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
Immunity
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Mitochondrion
Mitochondrion inner membrane
Nucleus
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone resorption

Inferred from mutant phenotype Ref.15. Source: UniProtKB

branching involved in mammary gland duct morphogenesis

Inferred from mutant phenotype PubMed 16007215. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from mutant phenotype PubMed 15292044. Source: MGI

forebrain development

Inferred from genetic interaction PubMed 16162939. Source: MGI

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from electronic annotation. Source: Ensembl

negative regulation of anoikis

Inferred from electronic annotation. Source: Ensembl

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

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of mitochondrial depolarization

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

oogenesis

Inferred from mutant phenotype PubMed 16007215. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 12526740. Source: MGI

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 17045821. Source: BHF-UCL

positive regulation of canonical Wnt signaling pathway

Inferred from genetic interaction PubMed 19920076. Source: MGI

positive regulation of podosome assembly

Inferred from direct assay PubMed 21525037. Source: MGI

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 11274221PubMed 15937334. Source: MGI

regulation of intracellular estrogen receptor signaling pathway

Inferred from mutant phenotype PubMed 16007215. Source: MGI

regulation of protein binding

Inferred from direct assay PubMed 22027834. Source: MGI

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

uterus development

Inferred from mutant phenotype PubMed 16007215. Source: MGI

   Cellular_componentcaveola

Inferred from electronic annotation. Source: Ensembl

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

late endosome

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 21525037. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ephrin receptor binding

Inferred from physical interaction Ref.14. Source: UniProtKB

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

kinase activity

Inferred from mutant phenotype PubMed 12808090. Source: MGI

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.15. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 8438166. Source: MGI

protein kinase activity

Inferred from direct assay PubMed 11274221PubMed 19920076. Source: MGI

protein tyrosine kinase activity

Inferred from mutant phenotype PubMed 14636584. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Bcar1Q637672EBI-298680,EBI-1176801From a different organism.
Csf1P071412EBI-298680,EBI-777188
Dlg4P310169EBI-298680,EBI-375655From a different organism.
enaQ8T4F72EBI-298680,EBI-466810From a different organism.
Ephb2P547633EBI-298680,EBI-537711
Grin2aQ009595EBI-298680,EBI-630970From a different organism.
ITGB3P051065EBI-298680,EBI-702847From a different organism.
PTK2Q053975EBI-298680,EBI-702142From a different organism.
PtpraP180522EBI-298680,EBI-6597520
PXNP490232EBI-298680,EBI-702209From a different organism.
ROR1Q019733EBI-298680,EBI-6082337From a different organism.
WasP703152EBI-298680,EBI-644195

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 541540Neuronal proto-oncogene tyrosine-protein kinase Src
PRO_0000088142

Regions

Domain83 – 15068SH3
Domain156 – 25398SH2
Domain275 – 528254Protein kinase
Nucleotide binding281 – 2899ATP By similarity

Sites

Active site3941Proton acceptor By similarity
Binding site3031ATP By similarity

Amino acid modifications

Modified residue171Phosphoserine By similarity
Modified residue341Phosphoserine By similarity
Modified residue681Phosphoserine By similarity
Modified residue731Phosphothreonine By similarity
Modified residue741Phosphoserine; by CDK5 By similarity
Modified residue1921Phosphotyrosine Ref.18
Modified residue4241Phosphotyrosine; by autocatalysis; alternate By similarity
Modified residue4241Phosphotyrosine; by FAK2; alternate By similarity
Modified residue4441Phosphotyrosine By similarity
Modified residue5161Phosphothreonine By similarity
Modified residue5271Phosphotyrosine By similarity
Modified residue5351Phosphotyrosine; by CSK By similarity
Lipidation21N-myristoyl glycine By similarity

Experimental info

Sequence conflict801P → A in AAA40135. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P05480 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 0534AF027783BCCF

FASTA54160,645
        10         20         30         40         50         60 
MGSNKSKPKD ASQRRRSLEP SENVHGAGGA FPASQTPSKP ASADGHRGPS AAFVPPAAEP 

        70         80         90        100        110        120 
KLFGGFNSSD TVTSPQRAGP LAGGVTTFVA LYDYESRTET DLSFKKGERL QIVNNTRKVD 

       130        140        150        160        170        180 
VREGDWWLAH SLSTGQTGYI PSNYVAPSDS IQAEEWYFGK ITRRESERLL LNAENPRGTF 

       190        200        210        220        230        240 
LVRESETTKG AYCLSVSDFD NAKGLNVKHY KIRKLDSGGF YITSRTQFNS LQQLVAYYSK 

       250        260        270        280        290        300 
HADGLCHRLT TVCPTSKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTRV 

       310        320        330        340        350        360 
AIKTLKPGTM SPEAFLQEAQ VMKKLRHEKL VQLYAVVSEE PIYIVTEYMN KGSLLDFLKG 

       370        380        390        400        410        420 
ETGKYLRLPQ LVDMSAQIAS GMAYVERMNY VHRDLRAANI LVGENLVCKV ADFGLARLIE 

       430        440        450        460        470        480 
DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILL TELTTKGRVP YPGMVNREVL 

       490        500        510        520        530        540 
DQVERGYRMP CPPECPESLH DLMCQCWRKE PEERPTFEYL QAFLEDYFTS TEPQYQPGEN 


L 

« Hide

References

« Hide 'large scale' references
[1]"Neuronal pp60c-src contains a six-amino acid insertion relative to its non-neuronal counterpart."
Martinez R., Mathey-Prevot B., Bernards A., Baltimore D.
Science 237:411-415(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"Characterization of quantitative trait loci influencing growth and adiposity using congenic mouse strains."
Farber C.R., Corva P.M., Medrano J.F.
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CAST/EiJ.
Tissue: Brain.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor."
Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D., Roussel M.F.
EMBO J. 12:943-950(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSF1R.
[6]"Direct and specific interaction of c-Src with Neu is involved in signaling by the epidermal growth factor receptor."
Muthuswamy S.K., Muller W.J.
Oncogene 11:271-279(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB2.
[7]"Activation of Src-family protein tyrosine kinases and phosphatidylinositol 3-kinase in 3T3-L1 mouse preadipocytes by interleukin-11."
Fuhrer D.K., Yang Y.C.
Exp. Hematol. 24:195-203(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN IL11-SIGNALING.
[8]"Bombesin, bradykinin, vasopressin, and phorbol esters rapidly and transiently activate Src family tyrosine kinases in Swiss 3T3 cells. Dissociation from tyrosine phosphorylation of p125 focal adhesion kinase."
Rodriguez-Fernandez J.L., Rozengurt E.
J. Biol. Chem. 271:27895-27901(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[9]"c-Src activates both STAT1 and STAT3 in PDGF-stimulated NIH3T3 cells."
Cirri P., Chiarugi P., Marra F., Raugei G., Camici G., Manao G., Ramponi G.
Biochem. Biophys. Res. Commun. 239:493-497(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STAT1.
[10]"ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src."
Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A., Randazzo P.A.
Mol. Cell. Biol. 18:7038-7051(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDEF1/ASAP1.
[11]"N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling."
Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.
Nat. Cell Biol. 3:650-657(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; FGFR4; SHC1; GAP43 AND CTTN.
[12]"The role of c-Src in platelet-derived growth factor alpha receptor internalization."
Avrov K., Kazlauskas A.
Exp. Cell Res. 291:426-434(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFRA.
[13]"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.
[14]"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.
[15]"Src kinase activity is essential for osteoclast function."
Miyazaki T., Sanjay A., Neff L., Tanaka S., Horne W.C., Baron R.
J. Biol. Chem. 279:17660-17666(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PTK2B/PYK2.
[16]"Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLT3.
[17]"Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCPG1.
[18]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[19]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Deficiency of a beta-arrestin-2 signal complex contributes to insulin resistance."
Luan B., Zhao J., Wu H., Duan B., Shu G., Wang X., Li D., Jia W., Kang J., Pei G.
Nature 457:1146-1149(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[21]"Collagen stimulates discoidin domain receptor 1-mediated migration of smooth muscle cells through Src."
Lu K.K., Trcka D., Bendeck M.P.
Cardiovasc. Pathol. 20:71-76(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDR1.
[22]"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.
[23]"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.
[24]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17031 mRNA. Translation: AAA40135.1.
AY902331 Genomic DNA. Translation: AAX90616.1.
AL672259 Genomic DNA. Translation: CAM16141.1.
CH466551 Genomic DNA. Translation: EDL06234.1.
CCDSCCDS38305.1.
PIRA43610.
RefSeqNP_001020566.1. NM_001025395.2.
NP_033297.2. NM_009271.3.
UniGeneMm.22845.

3D structure databases

ProteinModelPortalP05480.
SMRP05480. Positions 56-541.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203491. 37 interactions.
DIPDIP-31071N.
IntActP05480. 27 interactions.
MINTMINT-85032.
STRING10090.ENSMUSP00000105155.

Chemistry

BindingDBP05480.
ChEMBLCHEMBL3074.

PTM databases

PhosphoSiteP05480.

Proteomic databases

MaxQBP05480.
PaxDbP05480.
PRIDEP05480.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092576; ENSMUSP00000090237; ENSMUSG00000027646.
ENSMUST00000109529; ENSMUSP00000105155; ENSMUSG00000027646.
GeneID20779.
KEGGmmu:20779.
UCSCuc008npa.1. mouse.

Organism-specific databases

CTD6714.
MGIMGI:98397. Src.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00620000087702.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidQ2M4I4.
KOK05704.
OMACQCWRKD.
OrthoDBEOG7GTT2V.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.
ReactomeREACT_188257. Signal Transduction.
REACT_188576. Developmental Biology.
REACT_23985. Src is activated.

Gene expression databases

ArrayExpressP05480.
BgeeP05480.
CleanExMM_SRC.
GenevestigatorP05480.

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

NextBio299503.
PROP05480.
SOURCESearch...

Entry information

Entry nameSRC_MOUSE
AccessionPrimary (citable) accession number: P05480
Secondary accession number(s): Q2M4I4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 161 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot