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P97465 (DOK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Docking protein 1
Alternative name(s):
Downstream of tyrosine kinase 1
p62(dok)
Gene names
Name:Dok1
Synonyms:Dok
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.6 Ref.8

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Expressed in lung, spleen, skeletal muscle and kidney.

Domain

PTB domain mediates receptor interaction.

Post-translational modification

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. Ref.5 Ref.7

Disruption phenotype

No visible phenotype. Mice appear healthy and are fertile. Ref.7

Sequence similarities

Belongs to the DOK family. Type A subfamily.

Contains 1 IRS-type PTB domain.

Contains 1 PH domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Docking protein 1
PRO_0000187269

Regions

Domain4 – 119116PH
Domain151 – 259109IRS-type PTB
Compositional bias280 – 32243Pro-rich
Compositional bias359 – 43072Pro-rich

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2691Phosphoserine Ref.13
Modified residue2901Phosphoserine By similarity
Modified residue2951Phosphotyrosine Ref.10
Modified residue3361Phosphotyrosine Ref.10
Modified residue3401Phosphotyrosine Ref.10
Modified residue3611Phosphotyrosine Ref.10 Ref.11
Modified residue3761Phosphotyrosine Ref.12
Modified residue3971Phosphotyrosine; by INSR By similarity
Modified residue4081Phosphotyrosine Ref.11
Modified residue4501Phosphotyrosine Ref.11 Ref.13

Experimental info

Sequence conflict21D → N in AAH13066. Ref.4
Sequence conflict871V → A in AAC95339. Ref.3
Sequence conflict871V → A in AAH13066. Ref.4

Secondary structure

..................... 482
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P97465 [UniParc].

Last modified January 17, 2003. Version 2.
Checksum: C999C9FE0DA58EA3

FASTA48252,452
        10         20         30         40         50         60 
MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS RGGRGGSRRL 

        70         80         90        100        110        120 
DCKMIRLAEC VSVVPVTVES PPEPGAVAFR LDTAQRSHLL AADAVSSTAW VQTLCRTAFP 

       130        140        150        160        170        180 
KGGWALAQTE NQPKFSALEM LENSLYSPTW EGSQFWVTSQ KTEASERCGL QGSYILRVEA 

       190        200        210        220        230        240 
EKLTLLTLGA QSQILEPLLF WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTSQGND 

       250        260        270        280        290        300 
IFQAVEAAIQ QQKAQGKVGQ AQDILRTDSH DGETEGKTVP PPVPQDPLGS PPALYAEPLD 

       310        320        330        340        350        360 
SLRIPPGPSQ DSVYSDPLGS TPAGAGEGVH SKKPLYWDLY GHVQQQLLKT KLTDSKEDPI 

       370        380        390        400        410        420 
YDEPEGLAPA PPRGLYDLPQ EPRDAWWCQA RLKEEGYELP YNPATDDYAV PPPRSPKPAP 

       430        440        450        460        470        480 
APKPQGLILP ESGTTRGSGS KGFSSDTALY SQVQKSGTSG AWDCGLSKVG NDRAGVKSEG 


ST 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U78818 mRNA. Translation: AAB48827.2.
AF084363 Genomic DNA. Translation: AAC95339.1.
BC013066 mRNA. Translation: AAH13066.1.
CCDSCCDS20265.1.
RefSeqNP_001278728.1. NM_001291799.1.
NP_034200.4. NM_010070.4.
UniGeneMm.156.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P5TX-ray2.35A/B152-266[»]
1UEFX-ray2.50A/B152-266[»]
ProteinModelPortalP97465.
SMRP97465. Positions 4-119, 152-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199267. 22 interactions.
IntActP97465. 13 interactions.
MINTMINT-148034.

PTM databases

PhosphoSiteP97465.

Proteomic databases

MaxQBP97465.
PaxDbP97465.
PRIDEP97465.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089651; ENSMUSP00000087079; ENSMUSG00000068335.
GeneID13448.
KEGGmmu:13448.
UCSCuc009clr.2. mouse.

Organism-specific databases

CTD1796.
MGIMGI:893587. Dok1.

Phylogenomic databases

eggNOGNOG243145.
GeneTreeENSGT00730000110348.
HOGENOMHOG000112245.
HOVERGENHBG018962.
InParanoidP97465.
KOK14752.
OMAWPYTLLR.
OrthoDBEOG77WWC5.
PhylomeDBP97465.
TreeFamTF324994.

Gene expression databases

BgeeP97465.
CleanExMM_DOK1.
GenevestigatorP97465.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF02174. IRS. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view]
PROSITEPS51064. IRS_PTB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDOK1. mouse.
EvolutionaryTraceP97465.
NextBio283899.
PROP97465.
SOURCESearch...

Entry information

Entry nameDOK1_MOUSE
AccessionPrimary (citable) accession number: P97465
Secondary accession number(s): Q9R213
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: January 17, 2003
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot