P05480 (SRC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Protein existence	Evidence 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' By similarity. Phosphorylates BCAR1 at 'Tyr-132' By similarity. 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 By similarity. 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 By similarity. 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 By similarity. 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. Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 Ref.22
Subcellular location	Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasm › cytoskeleton. 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.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Cell adhesion Cell cycle Immunity
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane Mitochondrion Mitochondrion inner membrane Nucleus
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bone 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 intracellular protein kinase cascade Inferred from electronic annotation. Source: Compara negative regulation of anoikis Inferred from electronic annotation. Source: Compara negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of extrinsic apoptotic signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of intrinsic apoptotic signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of protein homooligomerization Inferred from electronic annotation. Source: Compara 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 receptor 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 cascade Inferred from electronic annotation. Source: Compara 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: Compara uterus development Inferred from mutant phenotype PubMed 16007215. Source: MGI
Cellular_component	caveola Inferred from electronic annotation. Source: Compara cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome late endosome Inferred from electronic annotation. Source: Compara lysosome Inferred from electronic annotation. Source: Compara 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_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from sequence or structural similarity. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from mutant phenotype PubMed 14636584. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Bcar1	Q63767	2	EBI-298680,EBI-1176801	From a different organism.
Csf1	P07141	2	EBI-298680,EBI-777188
ena	Q8T4F7	2	EBI-298680,EBI-466810	From a different organism.
Ephb2	P54763	3	EBI-298680,EBI-537711
ITGB3	P05106	5	EBI-298680,EBI-702847	From a different organism.
PXN	P49023	2	EBI-298680,EBI-702209	From a different organism.
ROR1	Q01973	3	EBI-298680,EBI-6082337	From a different organism.
Was	P70315	2	EBI-298680,EBI-644195

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 541	541	Neuronal proto-oncogene tyrosine-protein kinase Src		PRO_0000088142
Regions
	Domain	83 – 150	68	SH3
	Domain	156 – 253	98	SH2
	Domain	275 – 528	254	Protein kinase
	Nucleotide binding	281 – 289	9	ATP By similarity
Sites
	Active site	394	1	Proton acceptor By similarity
	Binding site	303	1	ATP By similarity
Amino acid modifications
	Modified residue	17	1	Phosphoserine Ref.20
	Modified residue	34	1	Phosphoserine By similarity
	Modified residue	68	1	Phosphoserine By similarity
	Modified residue	73	1	Phosphothreonine By similarity
	Modified residue	74	1	Phosphoserine; by CDK5 By similarity
	Modified residue	192	1	Phosphotyrosine Ref.18
	Modified residue	424	1	Phosphotyrosine; by autocatalysis; alternate By similarity
	Modified residue	424	1	Phosphotyrosine; by FAK2; alternate By similarity
	Modified residue	444	1	Phosphotyrosine By similarity
	Modified residue	506	1	S-nitrosocysteine By similarity
	Modified residue	516	1	Phosphothreonine By similarity
	Modified residue	527	1	Phosphotyrosine By similarity
	Modified residue	535	1	Phosphotyrosine; by CSK By similarity
	Lipidation	2	1	N-myristoyl glycine By similarity
Experimental info
	Sequence conflict	80	1	P → A in AAA40135. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P05480 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: 0534AF027783BCCF	FASTA	541	60,645
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Tissue: Brain.
[19]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, MASS SPECTROMETRY. Tissue: Brain cortex.
[20]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, MASS SPECTROMETRY. Tissue: Melanoma.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
IPI	IPI00222801.
PIR	A43610.
RefSeq	NP_001020566.1. NM_001025395.2. NP_033297.2. NM_009271.3.
UniGene	Mm.22845.
3D structure databases
ProteinModelPortal	P05480.
SMR	P05480. Positions 56-541.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31071N.
IntAct	P05480. 14 interactions.
MINT	MINT-85032.
STRING	10090.ENSMUSP00000105155.
PTM databases
PhosphoSite	P05480.
Proteomic databases
PaxDb	P05480.
PRIDE	P05480.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000092576; ENSMUSP00000090237; ENSMUSG00000027646. ENSMUST00000109529; ENSMUSP00000105155; ENSMUSG00000027646.
GeneID	20779.
KEGG	mmu:20779.
Organism-specific databases
CTD	6714.
MGI	MGI:98397. Src.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00620000087702.
HOGENOM	HOG000233858.
HOVERGEN	HBG008761.
InParanoid	Q2M4I4.
KO	K05704.
OMA	CQCWRKD.
OrthoDB	EOG4KKZ2S.
Enzyme and pathway databases
BRENDA	2.7.10.2. 3474.
Reactome	REACT_115202. Signal Transduction. REACT_127416. Developmental Biology. REACT_23985. Src is activated.
Gene expression databases
ArrayExpress	P05480.
Bgee	P05480.
CleanEx	MM_SRC.
Genevestigator	P05480.
GermOnline	ENSMUSG00000027646. Mus musculus.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_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]
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50001. SH2. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P05480.
ChEMBL	CHEMBL3074.
NextBio	299503.
SOURCE	Search...

Entry information

Entry name

SRC_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 147 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program