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Protein

Docking protein 1

Gene

Dok1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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).By similarity

GO - Molecular functioni

  • receptor signaling protein activity Source: MGI

GO - Biological processi

  • intracellular signal transduction Source: MGI
  • MAPK cascade Source: MGI
  • Ras protein signal transduction Source: MGI
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_304877. IRS activation.
REACT_332866. PI3K Cascade.

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 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:893587. Dok1.

Subcellular locationi

GO - Cellular componenti

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-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.
GenevisibleiP97465. MM.

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. 29 interactions.
IntActiP97465. 13 interactions.
MINTiMINT-148034.
STRINGi10090.ENSMUSP00000087079.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
[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

        10         20         30         40         50
MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS
60 70 80 90 100
RGGRGGSRRL DCKMIRLAEC VSVVPVTVES PPEPGAVAFR LDTAQRSHLL
110 120 130 140 150
AADAVSSTAW VQTLCRTAFP KGGWALAQTE NQPKFSALEM LENSLYSPTW
160 170 180 190 200
EGSQFWVTSQ KTEASERCGL QGSYILRVEA EKLTLLTLGA QSQILEPLLF
210 220 230 240 250
WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTSQGND IFQAVEAAIQ
260 270 280 290 300
QQKAQGKVGQ AQDILRTDSH DGETEGKTVP PPVPQDPLGS PPALYAEPLD
310 320 330 340 350
SLRIPPGPSQ DSVYSDPLGS TPAGAGEGVH SKKPLYWDLY GHVQQQLLKT
360 370 380 390 400
KLTDSKEDPI YDEPEGLAPA PPRGLYDLPQ EPRDAWWCQA RLKEEGYELP
410 420 430 440 450
YNPATDDYAV PPPRSPKPAP APKPQGLILP ESGTTRGSGS KGFSSDTALY
460 470 480
SQVQKSGTSG AWDCGLSKVG NDRAGVKSEG ST
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi199267. 29 interactions.
IntActiP97465. 13 interactions.
MINTiMINT-148034.
STRINGi10090.ENSMUSP00000087079.

PTM databases

PhosphoSiteiP97465.

Proteomic databases

MaxQBiP97465.
PaxDbiP97465.
PRIDEiP97465.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1796.
MGIiMGI:893587. Dok1.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_304877. IRS activation.
REACT_332866. PI3K Cascade.

Miscellaneous databases

ChiTaRSiDok1. mouse.
EvolutionaryTraceiP97465.
NextBioi283899.
PROiP97465.
SOURCEiSearch...

Gene expression databases

BgeeiP97465.
CleanExiMM_DOK1.
GenevisibleiP97465. MM.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR002404. Insln_rcpt_S1.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
[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]
ProtoNetiSearch...

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: July 22, 2015
This is version 137 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.