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P97465

- DOK1_MOUSE

UniProt

P97465 - DOK1_MOUSE

Protein

Docking protein 1

Gene

Dok1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (17 Jan 2003)
      Previous versions | rss
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    Functioni

    DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3 By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. receptor signaling protein activity Source: MGI

    GO - Biological processi

    1. intracellular signal transduction Source: MGI
    2. MAPK cascade Source: MGI
    3. Ras protein signal transduction Source: MGI
    4. transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Docking protein 1
    Alternative name(s):
    Downstream of tyrosine kinase 1
    p62(dok)
    Gene namesi
    Name:Dok1
    Synonyms:Dok
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:893587. Dok1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Mice appear healthy and are fertile.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 482482Docking protein 1PRO_0000187269Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei269 – 2691Phosphoserine1 Publication
    Modified residuei290 – 2901PhosphoserineBy similarity
    Modified residuei295 – 2951Phosphotyrosine1 Publication
    Modified residuei336 – 3361Phosphotyrosine1 Publication
    Modified residuei340 – 3401Phosphotyrosine1 Publication
    Modified residuei361 – 3611Phosphotyrosine2 Publications
    Modified residuei376 – 3761Phosphotyrosine1 Publication
    Modified residuei397 – 3971Phosphotyrosine; by INSRBy similarity
    Modified residuei408 – 4081Phosphotyrosine1 Publication
    Modified residuei450 – 4501Phosphotyrosine2 Publications

    Post-translational modificationi

    Constitutively tyrosine-phosphorylated. Phosphorylated by TEC. Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway By similarity. Phosphorylated by LYN. Phosphorylated on tyrosine residues by SRMS By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP97465.
    PaxDbiP97465.
    PRIDEiP97465.

    PTM databases

    PhosphoSiteiP97465.

    Expressioni

    Tissue specificityi

    Expressed in lung, spleen, skeletal muscle and kidney.

    Gene expression databases

    BgeeiP97465.
    CleanExiMM_DOK1.
    GenevestigatoriP97465.

    Interactioni

    Subunit structurei

    Interacts with RasGAP, INPP5D/SHIP1 and ABL1. Interacts directly with phosphorylated ITGB3 By similarity. Interacts with SRMS (via the SH2 and SH3 domains) By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Abl1P005204EBI-914917,EBI-914519
    Nck1Q99M515EBI-914917,EBI-642202

    Protein-protein interaction databases

    BioGridi199267. 22 interactions.
    IntActiP97465. 13 interactions.
    MINTiMINT-148034.

    Structurei

    Secondary structure

    1
    482
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi153 – 1608
    Helixi163 – 1675
    Beta strandi172 – 1787
    Beta strandi180 – 1889
    Turni190 – 1923
    Beta strandi194 – 2029
    Helixi203 – 2053
    Beta strandi206 – 2116
    Beta strandi213 – 2208
    Beta strandi228 – 2347
    Helixi238 – 25316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P5TX-ray2.35A/B152-266[»]
    1UEFX-ray2.50A/B152-266[»]
    ProteinModelPortaliP97465.
    SMRiP97465. Positions 4-119, 152-287.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP97465.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 119116PHAdd
    BLAST
    Domaini151 – 259109IRS-type PTBPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi280 – 32243Pro-richAdd
    BLAST
    Compositional biasi359 – 43072Pro-richAdd
    BLAST

    Domaini

    PTB domain mediates receptor interaction.

    Sequence similaritiesi

    Belongs to the DOK family. Type A subfamily.Curated
    Contains 1 IRS-type PTB domain.PROSITE-ProRule annotation
    Contains 1 PH domain.Curated

    Phylogenomic databases

    eggNOGiNOG243145.
    GeneTreeiENSGT00730000110348.
    HOGENOMiHOG000112245.
    HOVERGENiHBG018962.
    InParanoidiP97465.
    KOiK14752.
    OMAiWPYTLLR.
    OrthoDBiEOG77WWC5.
    PhylomeDBiP97465.
    TreeFamiTF324994.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR002404. Insln_rcpt_S1.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF02174. IRS. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00310. PTBI. 1 hit.
    [Graphical view]
    PROSITEiPS51064. IRS_PTB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P97465-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS    50
    RGGRGGSRRL DCKMIRLAEC VSVVPVTVES PPEPGAVAFR LDTAQRSHLL 100
    AADAVSSTAW VQTLCRTAFP KGGWALAQTE NQPKFSALEM LENSLYSPTW 150
    EGSQFWVTSQ KTEASERCGL QGSYILRVEA EKLTLLTLGA QSQILEPLLF 200
    WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTSQGND IFQAVEAAIQ 250
    QQKAQGKVGQ AQDILRTDSH DGETEGKTVP PPVPQDPLGS PPALYAEPLD 300
    SLRIPPGPSQ DSVYSDPLGS TPAGAGEGVH SKKPLYWDLY GHVQQQLLKT 350
    KLTDSKEDPI YDEPEGLAPA PPRGLYDLPQ EPRDAWWCQA RLKEEGYELP 400
    YNPATDDYAV PPPRSPKPAP APKPQGLILP ESGTTRGSGS KGFSSDTALY 450
    SQVQKSGTSG AWDCGLSKVG NDRAGVKSEG ST 482
    Length:482
    Mass (Da):52,452
    Last modified:January 17, 2003 - v2
    Checksum:iC999C9FE0DA58EA3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21D → N in AAH13066. (PubMed:15489334)Curated
    Sequence conflicti87 – 871V → A in AAC95339. (PubMed:9927484)Curated
    Sequence conflicti87 – 871V → A in AAH13066. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78818 mRNA. Translation: AAB48827.2.
    AF084363 Genomic DNA. Translation: AAC95339.1.
    BC013066 mRNA. Translation: AAH13066.1.
    CCDSiCCDS20265.1.
    RefSeqiNP_001278728.1. NM_001291799.1.
    NP_034200.4. NM_010070.4.
    UniGeneiMm.156.

    Genome annotation databases

    EnsembliENSMUST00000089651; ENSMUSP00000087079; ENSMUSG00000068335.
    GeneIDi13448.
    KEGGimmu:13448.
    UCSCiuc009clr.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78818 mRNA. Translation: AAB48827.2 .
    AF084363 Genomic DNA. Translation: AAC95339.1 .
    BC013066 mRNA. Translation: AAH13066.1 .
    CCDSi CCDS20265.1.
    RefSeqi NP_001278728.1. NM_001291799.1.
    NP_034200.4. NM_010070.4.
    UniGenei Mm.156.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P5T X-ray 2.35 A/B 152-266 [» ]
    1UEF X-ray 2.50 A/B 152-266 [» ]
    ProteinModelPortali P97465.
    SMRi P97465. Positions 4-119, 152-287.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199267. 22 interactions.
    IntActi P97465. 13 interactions.
    MINTi MINT-148034.

    PTM databases

    PhosphoSitei P97465.

    Proteomic databases

    MaxQBi P97465.
    PaxDbi P97465.
    PRIDEi P97465.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000089651 ; ENSMUSP00000087079 ; ENSMUSG00000068335 .
    GeneIDi 13448.
    KEGGi mmu:13448.
    UCSCi uc009clr.2. mouse.

    Organism-specific databases

    CTDi 1796.
    MGIi MGI:893587. Dok1.

    Phylogenomic databases

    eggNOGi NOG243145.
    GeneTreei ENSGT00730000110348.
    HOGENOMi HOG000112245.
    HOVERGENi HBG018962.
    InParanoidi P97465.
    KOi K14752.
    OMAi WPYTLLR.
    OrthoDBi EOG77WWC5.
    PhylomeDBi P97465.
    TreeFami TF324994.

    Miscellaneous databases

    ChiTaRSi DOK1. mouse.
    EvolutionaryTracei P97465.
    NextBioi 283899.
    PROi P97465.
    SOURCEi Search...

    Gene expression databases

    Bgeei P97465.
    CleanExi MM_DOK1.
    Genevestigatori P97465.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR002404. Insln_rcpt_S1.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF02174. IRS. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00310. PTBI. 1 hit.
    [Graphical view ]
    PROSITEi PS51064. IRS_PTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok."
      Yamanashi Y., Baltimore D.
      Cell 88:205-211(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-46; 122-160; 257-276 AND 424-453.
      Strain: C57BL/6.
      Tissue: B-cell and Spleen.
    2. Yamanashi Y., Baltimore D.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 381 AND 384.
    3. "Comparative sequence of human and mouse BAC clones from the mnd2 region of chromosome 2p13."
      Jang W., Hua A., Spilson S.V., Miller W., Roe B.A., Meisler M.H.
      Genome Res. 9:53-61(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The role of Tec protein-tyrosine kinase in T cell signaling."
      Yang W.C., Ghiotto M., Barbarat B., Olive D.
      J. Biol. Chem. 274:607-617(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY TEC.
    6. "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells."
      Dunant N.M., Wisniewski D., Strife A., Clarkson B., Resh M.D.
      Cell. Signal. 12:317-326(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    7. "Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling."
      Yamanashi Y., Tamura T., Kanamori T., Yamane H., Nariuchi H., Yamamoto T., Baltimore D.
      Genes Dev. 14:11-16(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, PHOSPHORYLATION BY LYN.
    8. "SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates migration through two critical tyrosine residues and forms a novel signaling complex with DOK1 and CRKL."
      Sattler M., Verma S., Pride Y.B., Salgia R., Rohrschneider L.R., Griffin J.D.
      J. Biol. Chem. 276:2451-2458(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    9. "Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of mouse dok1 protein."
      Shi N., Liu Y., Ni M., Yang M., Wu J., Peng Y., Gao F., Sun F., Peng X., Qiang B., Rao Z., Yuan J.
      Acta Crystallogr. D 60:334-336(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-295; TYR-336; TYR-340 AND TYR-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361; TYR-408 AND TYR-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-376, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND TYR-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    14. "Structural basis for the specific recognition of RET by the Dok1 phosphotyrosine binding domain."
      Shi N., Ye S., Bartlam M., Yang M., Wu J., Liu Y., Sun F., Han X., Peng X., Qiang B., Yuan J., Rao Z.
      J. Biol. Chem. 279:4962-4969(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 152-266.

    Entry informationi

    Entry nameiDOK1_MOUSE
    AccessioniPrimary (citable) accession number: P97465
    Secondary accession number(s): Q9R213
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: January 17, 2003
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3