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Q9WUD9

- SRC_RAT

UniProt

Q9WUD9 - SRC_RAT

Protein

Proto-oncogene tyrosine-protein kinase Src

Gene

Src

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 4 (13 Nov 2013)
      Previous versions | rss
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    Functioni

    Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of ADRBK1, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-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.By similarity1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    Phosphorylation by CSK at Tyr-530 inhibits kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced by heme. Further phosphorylation by CDK1 partially reactivates CSK-inactivated SRC and facilitates complete reactivation by protein tyrosine phosphatase PTPRC. Integrin engagement stimulates kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and pseudosubstrate-based peptide inhibitors like CIYKYYF act as inhibitors By similarity. Phosphorylation at Tyr-419 increases kinase activity.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei298 – 2981ATPPROSITE-ProRule annotation
    Active sitei389 – 3891Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi276 – 2849ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cell adhesion molecule binding Source: RGD
    3. enzyme binding Source: RGD
    4. estrogen receptor binding Source: RGD
    5. heme binding Source: UniProtKB
    6. insulin receptor binding Source: RGD
    7. kinase activity Source: RGD
    8. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    9. protein binding Source: UniProtKB
    10. protein complex binding Source: RGD
    11. protein C-terminus binding Source: RGD
    12. protein kinase binding Source: RGD
    13. protein kinase C binding Source: RGD
    14. protein tyrosine kinase activity Source: RGD
    15. receptor binding Source: RGD

    GO - Biological processi

    1. activation of protein kinase B activity Source: UniProtKB
    2. adherens junction organization Source: RGD
    3. bone resorption Source: UniProtKB
    4. cell cycle Source: UniProtKB-KW
    5. cell proliferation Source: RGD
    6. cellular response to fatty acid Source: RGD
    7. cellular response to hypoxia Source: RGD
    8. cellular response to insulin stimulus Source: RGD
    9. cellular response to lipopolysaccharide Source: RGD
    10. cellular response to progesterone stimulus Source: BHF-UCL
    11. epidermal growth factor receptor signaling pathway Source: RGD
    12. immune system process Source: UniProtKB-KW
    13. negative regulation of focal adhesion assembly Source: BHF-UCL
    14. negative regulation of transcription, DNA-templated Source: UniProtKB
    15. neurotrophin TRK receptor signaling pathway Source: RGD
    16. peptidyl-serine phosphorylation Source: UniProtKB
    17. peptidyl-tyrosine phosphorylation Source: GOC
    18. positive regulation of apoptotic process Source: RGD
    19. positive regulation of cell adhesion Source: RGD
    20. positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    21. positive regulation of cytokine secretion Source: RGD
    22. positive regulation of DNA biosynthetic process Source: UniProtKB
    23. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    24. positive regulation of gene expression Source: RGD
    25. positive regulation of glucose metabolic process Source: RGD
    26. positive regulation of insulin receptor signaling pathway Source: RGD
    27. positive regulation of intracellular signal transduction Source: RGD
    28. positive regulation of MAP kinase activity Source: UniProtKB
    29. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    30. positive regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    31. positive regulation of protein autophosphorylation Source: UniProtKB
    32. positive regulation of protein transport Source: RGD
    33. positive regulation of smooth muscle cell migration Source: RGD
    34. positive regulation of transcription, DNA-templated Source: UniProtKB
    35. progesterone receptor signaling pathway Source: BHF-UCL
    36. protein autophosphorylation Source: UniProtKB
    37. response to acidic pH Source: RGD
    38. response to drug Source: RGD
    39. response to electrical stimulus Source: RGD
    40. response to fatty acid Source: RGD
    41. response to hydrogen peroxide Source: RGD
    42. response to mechanical stimulus Source: RGD
    43. response to mineralocorticoid Source: RGD
    44. response to nutrient levels Source: RGD
    45. response to virus Source: RGD
    46. single organismal cell-cell adhesion Source: RGD
    47. transcytosis Source: RGD

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion, Cell cycle, Immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_195025. Signaling by SCF-KIT.
    REACT_197451. Regulation of KIT signaling.
    REACT_198646. FCGR activation.
    REACT_199007. Spry regulation of FGF signaling.
    REACT_203466. Signaling by ERBB2.
    REACT_206819. Downstream signal transduction.
    REACT_207015. Signaling by EGFR.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene tyrosine-protein kinase Src (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene c-Src
    pp60c-src
    Short name:
    p60-Src
    Gene namesi
    Name:Src
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi620795. Src.

    Subcellular locationi

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

    GO - Cellular componenti

    1. caveola Source: RGD
    2. cytosol Source: UniProtKB
    3. mitochondrial inner membrane Source: UniProtKB
    4. neuron projection Source: RGD
    5. nucleus Source: UniProtKB-SubCell
    6. plasma membrane Source: RGD
    7. postsynaptic density Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 536535Proto-oncogene tyrosine-protein kinase SrcPRO_0000088143Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei17 – 171PhosphoserineBy similarity
    Modified residuei34 – 341PhosphoserineBy similarity
    Modified residuei69 – 691PhosphoserineBy similarity
    Modified residuei74 – 741PhosphothreonineBy similarity
    Modified residuei75 – 751Phosphoserine; by CDK5By similarity
    Modified residuei187 – 1871PhosphotyrosineBy similarity
    Modified residuei419 – 4191Phosphotyrosine; by FAK21 Publication
    Modified residuei420 – 4201Phosphothreonine; by autocatalysisBy similarity
    Modified residuei439 – 4391PhosphotyrosineBy similarity
    Modified residuei511 – 5111PhosphothreonineBy similarity
    Modified residuei522 – 5221PhosphotyrosineBy similarity
    Modified residuei530 – 5301Phosphotyrosine; by CSKBy similarity

    Post-translational modificationi

    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.By similarity2 Publications
    S-nitrosylation is important for activation of its kinase activity.By similarity
    Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation By similarity.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9WUD9.
    PRIDEiQ9WUD9.

    PTM databases

    PhosphoSiteiQ9WUD9.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Inductioni

    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.1 Publication

    Gene expression databases

    GenevestigatoriQ9WUD9.

    Interactioni

    Subunit structurei

    Interacts with DDEF1/ASAP1; via the SH3 domain. Interacts with CCPG1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ERBB2, STAT1 and PNN. Interacts with 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-419.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cacna1cP220024EBI-7784541,EBI-1185084
    Cd63P286482EBI-7784541,EBI-7784314
    PtprrO086172EBI-7784541,EBI-8584374

    Protein-protein interaction databases

    DIPiDIP-42731N.
    IntActiQ9WUD9. 8 interactions.
    MINTiMINT-1488989.
    STRINGi10116.ENSRNOP00000059291.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini84 – 14562SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini151 – 24898SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini270 – 523254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00620000087702.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiQ9WUD9.
    KOiK05704.
    OMAiCQCWRKD.
    TreeFamiTF351634.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9WUD9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGSNKSKPKD ASQRRRSLEP AENVHGAGGA FPASQTPSKP ASADGHRGPN    50
    AAFVPPAAAE PKLFGGFNSS DTVTSPQRAG PLAGGVTTFV ALYDYESRTE 100
    TDLSFKKGER LQIVNNTEGD WWLAHSLSTG QTGYIPSNYV APSDSIQAEE 150
    WYFGKITRRE SERLLLNAEN PRGTFLVRES ETTKGAYCLS VSDFDNAKGL 200
    NVKHYKIRKL DSGGFYITSR TQFNSLQQLV AYYSKHADGL CHRLTTVCPT 250
    SKPQTQGLAK DAWEIPRESL RLEVKLGQGC FGEVWMGTWN GTTRVAIKTL 300
    KPGTMSPEAF LQEAQVMKKL RHEKLVQLYA VVSEEPIYIV TEYMNKGSLL 350
    DFLKGETGKY LRLPQLVDMS AQIASGMAYV ERMNYVHRDL RAANILVGEN 400
    LVCKVADFGL ARLIEDNEYT ARQGAKFPIK WTAPEAALYG RFTIKSDVWS 450
    FGILLTELTT KGRVPYPGMV NREVLDQVER GYRMPCPPEC PESLHDLMCQ 500
    CWRKEPEERP TFEYLQAFLE DYFTSTEPQY QPGENL 536
    Length:536
    Mass (Da):59,973
    Last modified:November 13, 2013 - v4
    Checksum:i453D1E904EC660A3
    GO
    Isoform 2 (identifier: Q9WUD9-2) [UniParc]FASTAAdd to Basket

    Also known as: Neuronal Src

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

    Show »
    Length:542
    Mass (Da):60,727
    Checksum:i6AC21D6DD66B0B39
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431S → F in AAD24180. 1 PublicationCurated
    Sequence conflicti143 – 1431S → F in AAZ23849. 1 PublicationCurated
    Sequence conflicti143 – 1431S → F in AAZ23848. 1 PublicationCurated
    Sequence conflicti381 – 3811E → D in AAD24180. 1 PublicationCurated
    Sequence conflicti381 – 3811E → D in AAZ23849. 1 PublicationCurated
    Sequence conflicti381 – 3811E → D in AAZ23848. 1 PublicationCurated
    Sequence conflicti528 – 5281P → R in AAD24180. 1 PublicationCurated
    Sequence conflicti528 – 5281P → R in AAZ23849. 1 PublicationCurated
    Sequence conflicti528 – 5281P → R in AAZ23848. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei117 – 1171T → TRKVDVR in isoform 2. 1 PublicationVSP_053395

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_114183.1. NM_031977.1. [Q9WUD9-2]
    XP_006235449.1. XM_006235387.1. [Q9WUD9-2]
    XP_006235450.1. XM_006235388.1. [Q9WUD9-1]
    UniGeneiRn.112600.

    Genome annotation databases

    EnsembliENSRNOT00000012739; ENSRNOP00000012739; ENSRNOG00000009495. [Q9WUD9-1]
    GeneIDi83805.
    KEGGirno:83805.
    UCSCiRGD:620795. rat. [Q9WUD9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_114183.1. NM_031977.1. [Q9WUD9-2 ]
    XP_006235449.1. XM_006235387.1. [Q9WUD9-2 ]
    XP_006235450.1. XM_006235388.1. [Q9WUD9-1 ]
    UniGenei Rn.112600.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-42731N.
    IntActi Q9WUD9. 8 interactions.
    MINTi MINT-1488989.
    STRINGi 10116.ENSRNOP00000059291.

    Chemistry

    BindingDBi Q9WUD9.
    ChEMBLi CHEMBL3014.

    PTM databases

    PhosphoSitei Q9WUD9.

    Proteomic databases

    PaxDbi Q9WUD9.
    PRIDEi Q9WUD9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000012739 ; ENSRNOP00000012739 ; ENSRNOG00000009495 . [Q9WUD9-1 ]
    GeneIDi 83805.
    KEGGi rno:83805.
    UCSCi RGD:620795. rat. [Q9WUD9-1 ]

    Organism-specific databases

    CTDi 6714.
    RGDi 620795. Src.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00620000087702.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi Q9WUD9.
    KOi K05704.
    OMAi CQCWRKD.
    TreeFami TF351634.

    Enzyme and pathway databases

    Reactomei REACT_195025. Signaling by SCF-KIT.
    REACT_197451. Regulation of KIT signaling.
    REACT_198646. FCGR activation.
    REACT_199007. Spry regulation of FGF signaling.
    REACT_203466. Signaling by ERBB2.
    REACT_206819. Downstream signal transduction.
    REACT_207015. Signaling by EGFR.

    Miscellaneous databases

    NextBioi 35583878.

    Gene expression databases

    Genevestigatori Q9WUD9.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
      , 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 AT TYR-530 BY PTPRJ.

    Entry informationi

    Entry nameiSRC_RAT
    AccessioniPrimary (citable) accession number: Q9WUD9
    Secondary accession number(s): G3V776, Q45QJ2, Q9JJ10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 13, 2013
    Last modified: October 1, 2014
    This is version 135 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

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