Docking protein 1 - Mus musculus (Mouse)

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P97465 (DOK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Docking protein 1

Alternative name(s):
Downstream of tyrosine kinase 1
p62(dok)

Gene names

Name:	Dok1
Synonyms:	Dok

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.6 Ref.8
Subcellular location	Cytoplasm 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. Ref.5 Ref.7 Phosphorylated on tyrosine residues by the insulin receptor kinase. Results in the negative regulation of the insulin signaling pathway By similarity. Phosphorylated by LYN. 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.

Ontologies

Keywords
Cellular component	Cytoplasm
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Traceable author statement PubMed 11470823. Source: MGI Ras protein signal transduction Inferred from physical interaction Ref.1. Source: MGI transmembrane receptor protein tyrosine kinase signaling pathway Inferred from physical interaction PubMed 10585470. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro receptor signaling protein activity Inferred from physical interaction PubMed 10585470. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Abl1	P00520	4	EBI-914917,EBI-914519
Nck1	Q99M51	5	EBI-914917,EBI-642202

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 482

482

Docking protein 1

PRO_0000187269

Regions

Domain

4 – 119

116

Domain

151 – 259

109

IRS-type PTB

Compositional bias

280 – 322

Pro-rich

Compositional bias

359 – 430

Pro-rich

Amino acid modifications

Modified residue

269

Phosphoserine Ref.14

Modified residue

290

Phosphoserine By similarity

Modified residue

295

Phosphotyrosine Ref.10

Modified residue

314

Phosphotyrosine Ref.10

Modified residue

336

Phosphotyrosine Ref.10

Modified residue

340

Phosphotyrosine Ref.10

Modified residue

361

Phosphotyrosine Ref.10 Ref.11 Ref.12

Modified residue

376

Phosphotyrosine Ref.10 Ref.13

Modified residue

397

Phosphotyrosine; by INSR By similarity

Modified residue

408

Phosphotyrosine Ref.11

Modified residue

450

Phosphotyrosine Ref.11 Ref.14

Experimental info

Sequence conflict

D → N in AAH13066. Ref.4

Sequence conflict

V → A in AAC95339. Ref.3

Sequence conflict

V → A in AAH13066. Ref.4

Secondary structure

482

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P97465 [UniParc].

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

482

52,452

        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' referencesShow '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-314; TYR-336; TYR-340; TYR-361 AND TYR-376, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. Tissue: Mast cell.
[12]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361, MASS SPECTROMETRY. Tissue: Brain.
[13]	"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, MASS SPECTROMETRY. Tissue: Macrophage.
[14]	"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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[15]	"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.

IPI

IPI00125534.

RefSeq

NP_034200.4. NM_010070.4.

UniGene

Mm.156.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P97465.

SMR

P97465. Positions 4-119, 152-287.

ModBase

Search...

Protein-protein interaction databases

IntAct

P97465. 12 interactions.

MINT

MINT-148034.

PTM databases

PhosphoSite

P97465.

Proteomic databases

PaxDb

P97465.

PRIDE

P97465.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000089651; ENSMUSP00000087079; ENSMUSG00000068335.

GeneID

13448.

KEGG

mmu:13448.

UCSC

uc009clr.2. mouse.

Organism-specific databases

CTD

1796.

MGI

MGI:893587. Dok1.

Phylogenomic databases

eggNOG

NOG243145.

GeneTree

ENSGT00700000104148.

HOGENOM

HOG000112245.

HOVERGEN

HBG018962.

InParanoid

P97465.

K14752.

OMA

WPYTLLR.

OrthoDB

EOG4GB76M.

Gene expression databases

Bgee

P97465.

CleanEx

MM_DOK1.

Genevestigator

P97465.

GermOnline

ENSMUSG00000068335. Mus musculus.

Family and domain databases

Gene3D

2.30.29.30. 2 hits.

InterPro

IPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]

Pfam

PF02174. IRS. 1 hit.
[Graphical view]

SMART

SM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view]

PROSITE

PS51064. IRS_PTB. 1 hit.
PS50003. PH_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DOK1. mouse.

EvolutionaryTrace

P97465.

NextBio

283899.

SOURCE

Search...

Entry information

Entry name

DOK1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents