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O60496

- DOK2_HUMAN

UniProt

O60496 - DOK2_HUMAN

Protein

Docking protein 2

Gene

DOK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (06 Mar 2007)
      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. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-stimulated MAP kinase activation By similarity.By similarity

    GO - Molecular functioni

    1. receptor signaling protein activity Source: Ensembl

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell surface receptor signaling pathway Source: ProtInc
    3. leukocyte migration Source: Reactome
    4. Ras protein signal transduction Source: Ensembl
    5. signal transduction Source: ProtInc
    6. transmembrane receptor protein tyrosine kinase signaling pathway Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_12621. Tie2 Signaling.
    SignaLinkiO60496.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Docking protein 2
    Alternative name(s):
    Downstream of tyrosine kinase 2
    p56(dok-2)
    Gene namesi
    Name:DOK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2991. DOK2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27457.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 412412Docking protein 2PRO_0000187270Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei271 – 2711PhosphotyrosineBy similarity
    Modified residuei299 – 2991Phosphotyrosine3 Publications
    Modified residuei345 – 3451PhosphotyrosineBy similarity

    Post-translational modificationi

    On immunoreceptor stimulation, phosphorylated on C-terminal tyrosine residues. Phosphorylation on Tyr-345 is required for binding to the SH2 domain of NCK. Phosphorylation on both Tyr-271 and Tyr-299 is required for interaction with RASGAP. Phosphorylated on tyrosine residues by TEK/TIE2 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO60496.
    PaxDbiO60496.
    PRIDEiO60496.

    2D gel databases

    OGPiO60496.

    PTM databases

    PhosphoSiteiO60496.

    Expressioni

    Tissue specificityi

    Highly expressed in peripheral blood leukocytes, lymph nodes and spleen. Lower expression in thymus, bone marrow and fetal liver.1 Publication

    Gene expression databases

    ArrayExpressiO60496.
    BgeeiO60496.
    CleanExiHS_DOK2.
    GenevestigatoriO60496.

    Organism-specific databases

    HPAiCAB004379.

    Interactioni

    Subunit structurei

    Interacts with phosphorylated RASGAP and EGFR. Interacts with RET and NCK. Interacts (via PH domain) with TEK/TIE2 (tyrosine phosphorylated) By similarity.By similarity

    Protein-protein interaction databases

    BioGridi114508. 20 interactions.
    IntActiO60496. 1 interaction.
    MINTiMINT-1452945.
    STRINGi9606.ENSP00000276420.

    Structurei

    Secondary structure

    1
    412
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139
    Beta strandi17 – 204
    Beta strandi25 – 317
    Beta strandi34 – 374
    Beta strandi40 – 445
    Beta strandi50 – 523
    Beta strandi57 – 604
    Helixi62 – 643
    Beta strandi65 – 706
    Beta strandi75 – 773
    Beta strandi82 – 909
    Beta strandi92 – 976
    Helixi99 – 11315
    Beta strandi151 – 1555
    Helixi159 – 1646
    Beta strandi168 – 1747
    Beta strandi176 – 1805
    Beta strandi184 – 1874
    Helixi196 – 1983
    Beta strandi202 – 2054
    Beta strandi208 – 2136
    Beta strandi221 – 2266
    Helixi231 – 24717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D9WNMR-A1-114[»]
    2DLWNMR-A148-247[»]
    ProteinModelPortaliO60496.
    SMRiO60496. Positions 5-116, 148-252, 301-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60496.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 114111PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini147 – 252106IRS-type PTBPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi250 – 29243Pro-richAdd
    BLAST
    Compositional biasi321 – 36343Pro-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.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG319058.
    HOGENOMiHOG000112245.
    HOVERGENiHBG018962.
    InParanoidiO60496.
    OMAiGKKWRRF.
    OrthoDBiEOG77WWC5.
    PhylomeDBiO60496.
    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.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O60496-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDGAVKQGF LYLQQQQTFG KKWRRFGASL YGGSDCALAR LELQEGPEKP    50
    RRCEAARKVI RLSDCLRVAE AGGEASSPRD TSAFFLETKE RLYLLAAPAA 100
    ERGDWVQAIC LLAFPGQRKE LSGPEGKQSR PCMEENELYS SAVTVGPHKE 150
    FAVTMRPTEA SERCHLRGSY TLRAGESALE LWGGPEPGTQ LYDWPYRFLR 200
    RFGRDKVTFS FEAGRRCVSG EGNFEFETRQ GNEIFLALEE AISAQKNAAP 250
    ATPQPQPATI PASLPRPDSP YSRPHDSLPP PSPTTPVPAP RPRGQEGEYA 300
    VPFDAVARSL GKNFRGILAV PPQLLADPLY DSIEETLPPR PDHIYDEPEG 350
    VAALSLYDSP QEPRGEAWRR QATADRDPAG LQHVQPAGQD FSASGWQPGT 400
    EYDNVVLKKG PK 412
    Length:412
    Mass (Da):45,379
    Last modified:March 6, 2007 - v2
    Checksum:iEFAEDBA68439757F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti166 – 1661L → R in AAC13265. (PubMed:9478921)Curated
    Sequence conflicti178 – 1781A → S in AAC13265. (PubMed:9478921)Curated
    Sequence conflicti347 – 3471E → K in AAC13265. (PubMed:9478921)Curated
    Sequence conflicti374 – 3741A → R in AAC13265. (PubMed:9478921)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti152 – 1521A → P.1 Publication
    Corresponds to variant rs1140295 [ dbSNP | Ensembl ].
    VAR_030951
    Natural varianti274 – 2741P → L.
    Corresponds to variant rs34215892 [ dbSNP | Ensembl ].
    VAR_053068
    Natural varianti394 – 3941S → A.
    Corresponds to variant rs2242241 [ dbSNP | Ensembl ].
    VAR_030952

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034970 mRNA. Translation: AAC13265.1.
    BC032623 mRNA. Translation: AAH32623.1.
    CCDSiCCDS6016.1.
    RefSeqiNP_003965.2. NM_003974.2.
    UniGeneiHs.71215.

    Genome annotation databases

    EnsembliENST00000276420; ENSP00000276420; ENSG00000147443.
    GeneIDi9046.
    KEGGihsa:9046.
    UCSCiuc003wzx.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034970 mRNA. Translation: AAC13265.1 .
    BC032623 mRNA. Translation: AAH32623.1 .
    CCDSi CCDS6016.1.
    RefSeqi NP_003965.2. NM_003974.2.
    UniGenei Hs.71215.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D9W NMR - A 1-114 [» ]
    2DLW NMR - A 148-247 [» ]
    ProteinModelPortali O60496.
    SMRi O60496. Positions 5-116, 148-252, 301-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114508. 20 interactions.
    IntActi O60496. 1 interaction.
    MINTi MINT-1452945.
    STRINGi 9606.ENSP00000276420.

    PTM databases

    PhosphoSitei O60496.

    2D gel databases

    OGPi O60496.

    Proteomic databases

    MaxQBi O60496.
    PaxDbi O60496.
    PRIDEi O60496.

    Protocols and materials databases

    DNASUi 9046.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000276420 ; ENSP00000276420 ; ENSG00000147443 .
    GeneIDi 9046.
    KEGGi hsa:9046.
    UCSCi uc003wzx.1. human.

    Organism-specific databases

    CTDi 9046.
    GeneCardsi GC08M021822.
    HGNCi HGNC:2991. DOK2.
    HPAi CAB004379.
    MIMi 604997. gene.
    neXtProti NX_O60496.
    PharmGKBi PA27457.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG319058.
    HOGENOMi HOG000112245.
    HOVERGENi HBG018962.
    InParanoidi O60496.
    OMAi GKKWRRF.
    OrthoDBi EOG77WWC5.
    PhylomeDBi O60496.
    TreeFami TF324994.

    Enzyme and pathway databases

    Reactomei REACT_12621. Tie2 Signaling.
    SignaLinki O60496.

    Miscellaneous databases

    EvolutionaryTracei O60496.
    GeneWikii DOK2.
    GenomeRNAii 9046.
    NextBioi 33885.
    PROi O60496.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60496.
    Bgeei O60496.
    CleanExi HS_DOK2.
    Genevestigatori O60496.

    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.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins."
      Di Cristofano A., Carpino N., Dunant N., Friedland G., Kobayashi R., Strife A., Wisniewski D., Clarkson B., Pandolfi P.P., Resh M.D.
      J. Biol. Chem. 273:4827-4830(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 8-21; 30-49; 59-89 AND 128-149, TISSUE SPECIFICITY, INTERACTION WITH RASGAP, VARIANT PRO-152.
    2. "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].
      Tissue: Brain.
    3. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    4. "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-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "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 TYR-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    6. "Solution structure of the PH and IRS domains of human docking protein 2, isoform A."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-247.

    Entry informationi

    Entry nameiDOK2_HUMAN
    AccessioniPrimary (citable) accession number: O60496
    Secondary accession number(s): Q8N5A4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3