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O60496

- DOK2_HUMAN

UniProt

O60496 - DOK2_HUMAN

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Protein
Docking protein 2
Gene
DOK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

GO - Molecular functioni

  1. receptor signaling protein activity Source: Ensembl

GO - Biological processi

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

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
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27457.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiO60496.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 114111PH
Add
BLAST
Domaini147 – 252106IRS-type PTB
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi250 – 29243Pro-rich
Add
BLAST
Compositional biasi321 – 36343Pro-rich
Add
BLAST

Domaini

PTB domain mediates receptor interaction.

Sequence similaritiesi

Belongs to the DOK family. Type A subfamily.
Contains 1 PH domain.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661L → R in AAC13265. 1 Publication
Sequence conflicti178 – 1781A → S in AAC13265. 1 Publication
Sequence conflicti347 – 3471E → K in AAC13265. 1 Publication
Sequence conflicti374 – 3741A → R in AAC13265. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 119 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

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