Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q99704

- DOK1_HUMAN

UniProt

Q99704 - DOK1_HUMAN

Protein

Docking protein 1

Gene

DOK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 ITGB3.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. receptor signaling protein activity Source: Ensembl

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. insulin receptor signaling pathway Source: Reactome
    3. Ras protein signal transduction Source: Ensembl
    4. signal transduction Source: ProtInc
    5. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_508. Signal attenuation.
    REACT_570. IRS activation.
    REACT_976. PI3K Cascade.
    SignaLinkiQ99704.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Docking protein 1
    Alternative name(s):
    Downstream of tyrosine kinase 1
    p62(dok)
    pp62
    Gene namesi
    Name:DOK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2990. DOK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB
    4. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi362 – 3621Y → F: No association with NCK. No association with GAP; when associated with F-398. 1 Publication
    Mutagenesisi398 – 3981Y → F: No association with GAP; when associated with F-362. 1 Publication

    Organism-specific databases

    PharmGKBiPA27456.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 481481Docking protein 1PRO_0000187268Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei269 – 2691Phosphoserine2 Publications
    Modified residuei291 – 2911Phosphoserine1 Publication
    Modified residuei296 – 2961PhosphotyrosineBy similarity
    Modified residuei337 – 3371PhosphotyrosineBy similarity
    Modified residuei341 – 3411Phosphotyrosine1 Publication
    Modified residuei362 – 3621Phosphotyrosine; by INSR3 Publications
    Modified residuei377 – 3771Phosphotyrosine1 Publication
    Modified residuei398 – 3981Phosphotyrosine; by INSR2 Publications
    Modified residuei409 – 4091Phosphotyrosine1 Publication
    Modified residuei449 – 4491PhosphotyrosineBy similarity

    Post-translational modificationi

    Constitutively tyrosine-phosphorylated. Phosphorylated by TEC By similarity. Phosphorylated by LYN By similarity. Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway. Phosphorylated on tyrosine residues by SRMS.By similarity7 Publications
    Isoform 3 contains a N-acetylmethionine at position 1.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99704.
    PaxDbiQ99704.
    PRIDEiQ99704.

    PTM databases

    PhosphoSiteiQ99704.

    Expressioni

    Tissue specificityi

    Expressed in pancreas, heart, leukocyte and spleen. Expressed in both resting and activated peripheral blood T-cells. Expressed in breast cancer.1 Publication

    Gene expression databases

    ArrayExpressiQ99704.
    BgeeiQ99704.
    CleanExiHS_DOK1.
    GenevestigatoriQ99704.

    Organism-specific databases

    HPAiCAB004224.
    HPA048561.

    Interactioni

    Subunit structurei

    Interacts with ABL1 By similarity. Interacts with RasGAP and INPP5D/SHIP1. Interacts directly with phosphorylated ITGB3. Interacts with SRMS (via the SH2 and SH3 domains).By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cbll1Q9JIY22EBI-1384360,EBI-7644904From a different organism.
    ERBB2P046262EBI-1384360,EBI-641062
    ORFQ9Q2G42EBI-1384360,EBI-6248094From a different organism.
    SRMSQ9H3Y67EBI-1384360,EBI-8541270

    Protein-protein interaction databases

    BioGridi108131. 35 interactions.
    IntActiQ99704. 10 interactions.
    MINTiMINT-1494101.
    STRINGi9606.ENSP00000233668.

    Structurei

    Secondary structure

    1
    481
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi153 – 1597
    Helixi163 – 1675
    Beta strandi172 – 1787
    Beta strandi180 – 1889
    Beta strandi195 – 2028
    Helixi203 – 2053
    Beta strandi206 – 2116
    Beta strandi213 – 2208
    Beta strandi228 – 2347
    Helixi238 – 25114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V76X-ray1.60A/B/C/D152-256[»]
    ProteinModelPortaliQ99704.
    SMRiQ99704. Positions 4-119, 153-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99704.

    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 – 31839Pro-richAdd
    BLAST
    Compositional biasi356 – 43378Pro-richAdd
    BLAST

    Domaini

    The 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.
    HOGENOMiHOG000112245.
    HOVERGENiHBG018962.
    InParanoidiQ99704.
    KOiK14752.
    OMAiWPYTLLR.
    OrthoDBiEOG77WWC5.
    PhylomeDBiQ99704.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform 1 (identifier: Q99704-1) [UniParc]FASTAAdd to Basket

    Also known as: p62Dok1

    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

    MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS    50
    GGGRGSSRRL DCKVIRLAEC VSVAPVTVET PPEPGATAFR LDTAQRSHLL 100
    AADAPSSAAW VQTLCRNAFP KGSWTLAPTD NPPKLSALEM LENSLYSPTW 150
    EGSQFWVTVQ RTEAAERCGL HGSYVLRVEA ERLTLLTVGA QSQILEPLLS 200
    WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTAQGND IFQAVETAIH 250
    RQKAQGKAGQ GHDVLRADSH EGEVAEGKLP SPPGPQELLD SPPALYAEPL 300
    DSLRIAPCPS QDSLYSDPLD STSAQAGEGV QRKKPLYWDL YEHAQQQLLK 350
    AKLTDPKEDP IYDEPEGLAP VPPQGLYDLP REPKDAWWCQ ARVKEEGYEL 400
    PYNPATDDYA VPPPRSTKPL LAPKPQGPAF PEPGTATGSG IKSHNSALYS 450
    QVQKSGASGS WDCGLSRVGT DKTGVKSEGS T 481
    Length:481
    Mass (Da):52,392
    Last modified:May 1, 1997 - v1
    Checksum:iE9D947831244BA6C
    GO
    Isoform 2 (identifier: Q99704-2) [UniParc]FASTAAdd to Basket

    Also known as: p22Dokdel

    The sequence of this isoform differs from the canonical sequence as follows:
         153-177: SQFWVTVQRTEAAERCGLHGSYVLR → HVLFRGRPPLPLRPWNLHLPDGTGK
         178-481: Missing.

    Show »
    Length:177
    Mass (Da):19,370
    Checksum:i91A504A89EB6ED15
    GO
    Isoform 3 (identifier: Q99704-3) [UniParc]FASTAAdd to Basket

    Also known as: p44Dok

    The sequence of this isoform differs from the canonical sequence as follows:
         1-139: Missing.

    Note: Produced by alternative initiation at Met-140 of isoform 1. Contains a N-acetylmethionine at position 1.

    Show »
    Length:342
    Mass (Da):37,405
    Checksum:iDEF8E9DF694C38C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 2020MDGAV…RFGTK → RLPAQASATREREPRWSPFQ in AAB88182. 1 PublicationCuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 139139Missing in isoform 3. CuratedVSP_038224Add
    BLAST
    Alternative sequencei153 – 17725SQFWV…SYVLR → HVLFRGRPPLPLRPWNLHLP DGTGK in isoform 2. 1 PublicationVSP_003852Add
    BLAST
    Alternative sequencei178 – 481304Missing in isoform 2. 1 PublicationVSP_003853Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70987 mRNA. Translation: AAC51127.1.
    AF180527 mRNA. Translation: AAF19167.1.
    AF035299 mRNA. Translation: AAB88182.1.
    AC005033 Genomic DNA. Translation: AAX93224.1.
    BC114440 mRNA. Translation: AAI14441.1.
    CCDSiCCDS1954.1. [Q99704-1]
    CCDS56125.1. [Q99704-3]
    RefSeqiNP_001184189.1. NM_001197260.1. [Q99704-3]
    NP_001372.1. NM_001381.3. [Q99704-1]
    XP_005264237.1. XM_005264180.1. [Q99704-2]
    XP_006712022.1. XM_006711959.1. [Q99704-3]
    UniGeneiHs.103854.

    Genome annotation databases

    EnsembliENST00000233668; ENSP00000233668; ENSG00000115325. [Q99704-1]
    ENST00000340004; ENSP00000344330; ENSG00000115325. [Q99704-2]
    ENST00000409429; ENSP00000387016; ENSG00000115325. [Q99704-3]
    GeneIDi1796.
    KEGGihsa:1796.
    UCSCiuc002smr.3. human. [Q99704-1]

    Polymorphism databases

    DMDMi17366642.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70987 mRNA. Translation: AAC51127.1 .
    AF180527 mRNA. Translation: AAF19167.1 .
    AF035299 mRNA. Translation: AAB88182.1 .
    AC005033 Genomic DNA. Translation: AAX93224.1 .
    BC114440 mRNA. Translation: AAI14441.1 .
    CCDSi CCDS1954.1. [Q99704-1 ]
    CCDS56125.1. [Q99704-3 ]
    RefSeqi NP_001184189.1. NM_001197260.1. [Q99704-3 ]
    NP_001372.1. NM_001381.3. [Q99704-1 ]
    XP_005264237.1. XM_005264180.1. [Q99704-2 ]
    XP_006712022.1. XM_006711959.1. [Q99704-3 ]
    UniGenei Hs.103854.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V76 X-ray 1.60 A/B/C/D 152-256 [» ]
    ProteinModelPortali Q99704.
    SMRi Q99704. Positions 4-119, 153-283.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108131. 35 interactions.
    IntActi Q99704. 10 interactions.
    MINTi MINT-1494101.
    STRINGi 9606.ENSP00000233668.

    PTM databases

    PhosphoSitei Q99704.

    Polymorphism databases

    DMDMi 17366642.

    Proteomic databases

    MaxQBi Q99704.
    PaxDbi Q99704.
    PRIDEi Q99704.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233668 ; ENSP00000233668 ; ENSG00000115325 . [Q99704-1 ]
    ENST00000340004 ; ENSP00000344330 ; ENSG00000115325 . [Q99704-2 ]
    ENST00000409429 ; ENSP00000387016 ; ENSG00000115325 . [Q99704-3 ]
    GeneIDi 1796.
    KEGGi hsa:1796.
    UCSCi uc002smr.3. human. [Q99704-1 ]

    Organism-specific databases

    CTDi 1796.
    GeneCardsi GC02P074776.
    HGNCi HGNC:2990. DOK1.
    HPAi CAB004224.
    HPA048561.
    MIMi 602919. gene.
    neXtProti NX_Q99704.
    PharmGKBi PA27456.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG243145.
    HOGENOMi HOG000112245.
    HOVERGENi HBG018962.
    InParanoidi Q99704.
    KOi K14752.
    OMAi WPYTLLR.
    OrthoDBi EOG77WWC5.
    PhylomeDBi Q99704.
    TreeFami TF324994.

    Enzyme and pathway databases

    Reactomei REACT_508. Signal attenuation.
    REACT_570. IRS activation.
    REACT_976. PI3K Cascade.
    SignaLinki Q99704.

    Miscellaneous databases

    EvolutionaryTracei Q99704.
    GeneWikii DOK1.
    GenomeRNAii 1796.
    NextBioi 7317.
    PROi Q99704.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99704.
    Bgeei Q99704.
    CleanExi HS_DOK1.
    Genevestigatori Q99704.

    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. "p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells."
      Carpino N., Wisniewski D., Strife A., Marshak D., Kobayashi R., Stillman B., Clarkson B.
      Cell 88:197-204(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT TYROSINE RESIDUES.
    2. "Molecular cloning of a truncated p62Dok1 isoform, p22Dokdel."
      Hubert P., Ferreira V., Debre P., Bismuth G.
      Eur. J. Immunogenet. 27:145-148(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. Yu W., Sarginson J., Gibbs R.A.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
    6. "Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GTPase-activating protein and Nck and is essential for inhibiting insulin-stimulated activation of Ras and Akt."
      Wick M.J., Dong L.Q., Hu D., Langlais P., Liu F.
      J. Biol. Chem. 276:42843-42850(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-362 AND TYR-398, MUTAGENESIS OF TYR-362 AND TYR-398.
    7. "DOK4 and DOK5: new Dok-related genes expressed in human T cells."
      Favre C., Gerard A., Clauzier E., Pontarotti P., Olive D., Nunes J.A.
      Genes Immun. 4:40-45(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "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-362; TYR-377; TYR-398 AND TYR-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Targeted mass spectrometric analysis of N-terminally truncated isoforms generated via alternative translation initiation."
      Kobayashi R., Patenia R., Ashizawa S., Vykoukal J.
      FEBS Lett. 583:2441-2445(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 3), ACETYLATION AT MET-1 (ISOFORM 3).
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; TYR-341 AND TYR-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The unique N-terminal region of SRMS regulates enzymatic activity and phosphorylation of its novel substrate Dok1."
      Goel R.K., Miah S., Black K., Kalra N., Dai C., Lukong K.E.
      FEBS J. 280:4539-4559(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH SRMS.
    15. "An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin binding."
      Oxley C.L., Anthis N.J., Lowe E.D., Vakonakis I., Campbell I.D., Wegener K.L.
      J. Biol. Chem. 283:5420-5426(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 152-256, FUNCTION, INTERACTION WITH ITGB3.

    Entry informationi

    Entry nameiDOK1_HUMAN
    AccessioniPrimary (citable) accession number: Q99704
    Secondary accession number(s): O43204, Q53TY2, Q9UHG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3