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Q9WUD9 (SRC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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-738'. Enhances DDX58/RIG-I-elicited antiviral signaling By similarity. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-226'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Ref.10

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 By similarity. Phosphorylation at Tyr-419 increases kinase activity. Ref.6

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 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 (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 with PDGFRA (tyrosine phosphorylated). Interacts with CSF1R. Interacts with DDR1. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with AMOTL2; this interaction promotes the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Interacts with DDR2 and DAB2. Interacts with TRAP1. Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at Tyr-419. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

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

Tissue specificity

Isoform 2 is expressed in the brain with highest expression in the pyramidal layers of the hippocampus and the granular layer of the dentate gyrus and moderate expression in cortical regions, with higher levels in the superficial layers than in the deep layers. Isoform 2 may be neuron-specific. Isoform 1 is expressed at very low levels in the forebrain. Ref.2

Induction

Isoform 2 is up-regulated by MK-801, an uncompetitive N-methyl-d-aspartate (NMDA) receptor antagonist, mostly in the superficial layers of the parietal, temporal, occipital and frontal cortices. Ref.2 Ref.6

Post-translational modification

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

Dephosphorylated at Tyr-530 by PTPRJ. Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src By similarity. 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 SRX 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 By similarity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity. Ref.6 Ref.11

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 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
   Coding sequence diversityAlternative splicing
   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_processactivation of protein kinase B activity

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

adherens junction organization

Inferred from direct assay PubMed 15389520. Source: RGD

bone resorption

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from direct assay PubMed 15856020. Source: RGD

cellular response to fatty acid

Inferred from expression pattern PubMed 20149623. Source: RGD

cellular response to hypoxia

Inferred from expression pattern PubMed 20380727. Source: RGD

cellular response to insulin stimulus

Inferred from expression pattern PubMed 19952103. Source: RGD

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 20149623. Source: RGD

cellular response to progesterone stimulus

Inferred from mutant phenotype PubMed 21440892. Source: BHF-UCL

epidermal growth factor receptor signaling pathway

Inferred from expression pattern PubMed 15856020. Source: RGD

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of focal adhesion assembly

Inferred from mutant phenotype PubMed 21440892. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Inferred from direct assay PubMed 15546918. Source: RGD

peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 12488346. Source: GOC

positive regulation of DNA biosynthetic process

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 15322113. Source: RGD

positive regulation of cell adhesion

Inferred from direct assay Ref.11. Source: RGD

positive regulation of cyclin-dependent protein kinase activity

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

positive regulation of cytokine secretion

Inferred from mutant phenotype PubMed 19736311. Source: RGD

positive regulation of gene expression

Inferred from mutant phenotype PubMed 19763735PubMed 20333648. Source: RGD

positive regulation of glucose metabolic process

Inferred from mutant phenotype PubMed 19230846. Source: RGD

positive regulation of insulin receptor signaling pathway

Inferred from direct assay PubMed 14985360. Source: RGD

positive regulation of intracellular signal transduction

Inferred from mutant phenotype PubMed 19713443. Source: RGD

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

positive regulation of platelet-derived growth factor receptor signaling pathway

Inferred from expression pattern PubMed 16530387. Source: UniProtKB

positive regulation of protein autophosphorylation

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

positive regulation of protein transport

Inferred from mutant phenotype PubMed 15007081. Source: RGD

positive regulation of smooth muscle cell migration

Inferred from mutant phenotype PubMed 19736311. Source: RGD

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 16530387. Source: UniProtKB

progesterone receptor signaling pathway

Inferred from mutant phenotype PubMed 21440892. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay PubMed 16530387. Source: UniProtKB

response to acidity

Inferred from expression pattern PubMed 12081562. Source: RGD

response to drug

Inferred from expression pattern PubMed 20149623. Source: RGD

response to electrical stimulus

Inferred from expression pattern PubMed 20356829. Source: RGD

response to fatty acid

Inferred from expression pattern PubMed 19736311. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern PubMed 12226102. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 15731459. Source: RGD

response to mineralocorticoid

Inferred from expression pattern PubMed 16157790. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 20357031. Source: RGD

response to virus

Inferred from expression pattern PubMed 20333648. Source: RGD

single organismal cell-cell adhesion

Inferred from expression pattern PubMed 15591141. Source: RGD

transcytosis

Inferred from direct assay PubMed 15007081. Source: RGD

   Cellular_componentcaveola

Inferred from direct assay PubMed 20167931. Source: RGD

cytosol

Non-traceable author statement PubMed 16530387. Source: UniProtKB

mitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from direct assay PubMed 19737347. Source: RGD

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 6253989. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 20356829. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion molecule binding

Inferred from physical interaction PubMed 19948503. Source: RGD

enzyme binding

Inferred from physical interaction PubMed 15069201. Source: RGD

estrogen receptor binding

Inferred from physical interaction PubMed 14751567. Source: RGD

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

insulin receptor binding

Inferred from physical interaction PubMed 19952103. Source: RGD

kinase activity

Traceable author statement PubMed 12007793. Source: RGD

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein C-terminus binding

Inferred from physical interaction PubMed 14699011PubMed 19737347. Source: RGD

protein binding

Inferred from physical interaction PubMed 16530387. Source: UniProtKB

protein complex binding

Inferred from physical interaction PubMed 12618293PubMed 20197063. Source: RGD

protein kinase C binding

Inferred from physical interaction PubMed 14751567PubMed 15337529PubMed 19952103. Source: RGD

protein kinase binding

Inferred from physical interaction PubMed 12700184. Source: RGD

protein tyrosine kinase activity

Inferred from direct assay PubMed 12488346. Source: RGD

receptor binding

Inferred from physical interaction PubMed 11478920. Source: RGD

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WUD9-1)

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: Q9WUD9-2)

Also known as: Neuronal Src;

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 By similarity
Chain2 – 536535Proto-oncogene tyrosine-protein kinase Src
PRO_0000088143

Regions

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

Sites

Active site3891Proton acceptor By similarity
Binding site2981ATP By similarity

Amino acid modifications

Modified residue171Phosphoserine By similarity
Modified residue341Phosphoserine By similarity
Modified residue691Phosphoserine By similarity
Modified residue741Phosphothreonine By similarity
Modified residue751Phosphoserine; by CDK5 By similarity
Modified residue1871Phosphotyrosine By similarity
Modified residue4191Phosphotyrosine; by FAK2 Ref.6
Modified residue4201Phosphothreonine; by autocatalysis By similarity
Modified residue4391Phosphotyrosine By similarity
Modified residue5111Phosphothreonine By similarity
Modified residue5221Phosphotyrosine By similarity
Modified residue5301Phosphotyrosine; by CSK By similarity
Lipidation21N-myristoyl glycine By similarity

Natural variations

Alternative sequence1171T → TRKVDVR in isoform 2.
VSP_053395

Experimental info

Sequence conflict1431S → F in AAD24180. Ref.1
Sequence conflict1431S → F in AAZ23849. Ref.5
Sequence conflict1431S → F in AAZ23848. Ref.5
Sequence conflict3811E → D in AAD24180. Ref.1
Sequence conflict3811E → D in AAZ23849. Ref.5
Sequence conflict3811E → D in AAZ23848. Ref.5
Sequence conflict5281P → R in AAD24180. Ref.1
Sequence conflict5281P → R in AAZ23849. Ref.5
Sequence conflict5281P → R in AAZ23848. Ref.5

Sequences

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

Last modified November 13, 2013. Version 4.
Checksum: 453D1E904EC660A3

FASTA53659,973
        10         20         30         40         50         60 
MGSNKSKPKD ASQRRRSLEP AENVHGAGGA FPASQTPSKP ASADGHRGPN AAFVPPAAAE 

        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 TEYMNKGSLL DFLKGETGKY 

       370        380        390        400        410        420 
LRLPQLVDMS 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 (Neuronal Src) [UniParc].

Checksum: 6AC21D6DD66B0B39
Show »

FASTA54260,727

References

« Hide 'large scale' references
[1]"Rattus norvegicus proto-oncogene encoding tyrosine-protein kinase pp60-c-src."
Stockand J.D., Al-Khalili O., Spier B.J., Eaton D.C.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Sprague-Dawley.
Tissue: Testis.
[2]"Increased expression of neuronal Src and tyrosine phosphorylation of NMDA receptors in rat brain after systemic treatment with MK-801."
Linden A., Storvik M., Lakso M., Haapasalo A., Lee D., Witkin J.M., Sei Y., Castren E., Wong G.
Neuropharmacology 40:469-481(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION.
Strain: Wistar.
Tissue: Temporal cortex.
[3]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Genetic similarity between spontaneously hypertensive rats and Wistar-Kyoto rats in the coding regions of signal transduction proteins."
Jackson E.K., Zhu C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-529 (ISOFORM 1).
Strain: SHR and Wistar Kyoto.
[6]"A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation."
Dikic I., Tokiwa G., Lev S., Courtneidge S.A., Schlessinger J.
Nature 383:547-550(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2B/PYK2, ENZYME REGULATION, PHOSPHORYLATION AT TYR-419.
[7]"The proliferative and antiapoptotic effects of substance P are facilitated by formation of a beta -arrestin-dependent scaffolding complex."
DeFea K.A., Vaughn Z.D., O'Bryan E.M., Nishijima D., Dery O., Bunnett N.W.
Proc. Natl. Acad. Sci. U.S.A. 97:11086-11091(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB1.
[8]"Discoidin domain receptor 2 interacts with Src and Shc following its activation by type I collagen."
Ikeda K., Wang L.H., Torres R., Zhao H., Olaso E., Eng F.J., Labrador P., Klein R., Lovett D., Yancopoulos G.D., Friedman S.L., Lin H.C.
J. Biol. Chem. 277:19206-19212(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDR2.
[9]"Characterization of a novel negative regulator (DOC-2/DAB2) of c-Src in normal prostatic epithelium and cancer."
Zhou J., Scholes J., Hsieh J.T.
J. Biol. Chem. 278:6936-6941(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[10]"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, INTERACTION WITH DDR2.
[11]"The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue."
Pera I.L., Iuliano R., Florio T., Susini C., Trapasso F., Santoro M., Chiariotti L., Schettini G., Viglietto G., Fusco A.
Oncogene 24:3187-3195(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-530, DEPHOSPHORYLATION BY PTPRJ AT TYR-530.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF130457 mRNA. Translation: AAD24180.1.
AF157016 mRNA. Translation: AAF80335.1.
AABR06027223 Genomic DNA. No translation available.
CH474005 Genomic DNA. Translation: EDL96675.1.
CH474005 Genomic DNA. Translation: EDL96676.1.
CH474005 Genomic DNA. Translation: EDL96677.1.
CH474005 Genomic DNA. Translation: EDL96678.1.
CH474005 Genomic DNA. Translation: EDL96679.1.
DQ120509 mRNA. Translation: AAZ23848.1.
DQ120510 mRNA. Translation: AAZ23849.1.
RefSeqNP_114183.1. NM_031977.1. [Q9WUD9-2]
XP_006235449.1. XM_006235387.1. [Q9WUD9-2]
XP_006235450.1. XM_006235388.1. [Q9WUD9-1]
UniGeneRn.112600.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-42731N.
IntActQ9WUD9. 8 interactions.
MINTMINT-1488989.
STRING10116.ENSRNOP00000059291.

Chemistry

BindingDBQ9WUD9.
ChEMBLCHEMBL3014.

PTM databases

PhosphoSiteQ9WUD9.

Proteomic databases

PaxDbQ9WUD9.
PRIDEQ9WUD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012739; ENSRNOP00000012739; ENSRNOG00000009495. [Q9WUD9-1]
GeneID83805.
KEGGrno:83805.
UCSCRGD:620795. rat. [Q9WUD9-1]

Organism-specific databases

CTD6714.
RGD620795. Src.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00620000087702.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidQ9WUD9.
KOK05704.
OMACQCWRKD.
TreeFamTF351634.

Enzyme and pathway databases

ReactomeREACT_197471. Cell-Cell communication.

Gene expression databases

GenevestigatorQ9WUD9.

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

NextBio35583878.

Entry information

Entry nameSRC_RAT
AccessionPrimary (citable) accession number: Q9WUD9
Secondary accession number(s): G3V776, Q45QJ2, Q9JJ10
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 13, 2013
Last modified: July 9, 2014
This is version 133 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