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P97465

- DOK1_MOUSE

UniProt

P97465 - DOK1_MOUSE

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Protein

Docking protein 1

Gene
Dok1, Dok
Organism
Mus musculus (Mouse)
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. 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.

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
Complete GO annotation...

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
Complete GO annotation...

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-acetylmethionine By similarity
Modified residuei269 – 2691Phosphoserine1 Publication
Modified residuei290 – 2901Phosphoserine By 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 INSR By 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.2 Publications

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.2 Publications

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.

Miscellaneous databases

EvolutionaryTraceiP97465.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 119116PHAdd
BLAST
Domaini151 – 259109IRS-type PTBAdd
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.
Contains 1 PH domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21D → N in AAH13066. 1 Publication
Sequence conflicti87 – 871V → A in AAC95339. 1 Publication
Sequence conflicti87 – 871V → A in AAH13066. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 127 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

Similar proteinsi