[1]	NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 8-21; 30-49; 59-89 AND 128-149, TISSUE SPECIFICITY, INTERACTION WITH RASGAP, AND VARIANT PRO-152. DOI=10.1074/jbc.273.9.4827; PubMed=9478921 [NCBI, ExPASy, EBI, Israel, Japan] Di Cristofano A., Carpino N., Dunant N., Friedland G., Kobayashi R., Strife A., Wisniewski D., Clarkson B., Pandolfi P.P., Resh M.D.; "Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins."; J. Biol. Chem. 273:4827-4830(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-299, AND MASS SPECTROMETRY. DOI=10.1073/pnas.2436191100; PubMed=12522270 [NCBI, ExPASy, EBI, Israel, Japan] Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-299, AND MASS SPECTROMETRY. DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; Nat. Biotechnol. 23:94-101(2005).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-299, AND MASS SPECTROMETRY. TISSUE=T-cell; DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan] Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.; "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."; Nat. Methods 2:591-598(2005).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-299, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[7]	STRUCTURE BY NMR OF 1-247. RIKEN structural genomics initiative (RSGI); "Solution structure of the PH and IRS domains of human docking protein 2, isoform A."; Submitted (OCT-2006) to the PDB data bank.

Comments

FUNCTION: Docking proteins interact with receptor tyrosine kinases and mediate particular biological responses. 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).
SUBUNIT: Interacts with phosphorylated RASGAP and EGFR. Interacts with RET and NCK (By similarity).
INTERACTION:
Self; NbExp=1; IntAct=EBI-1046024, EBI-1046024;
Q9NVP2:ASF1B; NbExp=1; IntAct=EBI-1046024, EBI-1055650;
O15519:CFLAR; NbExp=1; IntAct=EBI-1046024, EBI-514941;
Q9UBS4:DNAJB11; NbExp=1; IntAct=EBI-1046024, EBI-713113;
P01588:EPO; NbExp=1; IntAct=EBI-1046024, EBI-1027362;
O95757:HSPA4L; NbExp=1; IntAct=EBI-1046024, EBI-358652;
O75832:PSMD10; NbExp=1; IntAct=EBI-1046024, EBI-752185;
P61026:RAB10; NbExp=1; IntAct=EBI-1046024, EBI-726075;
O43791:SPOP; NbExp=1; IntAct=EBI-1046024, EBI-743549;
O60232:SSSCA1; NbExp=1; IntAct=EBI-1046024, EBI-741415;
TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes, lymph nodes and spleen. Lower expression in thymus, bone marrow and fetal liver.
DOMAIN: PTB domain mediates receptor interaction.
PTM: 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 (By similarity).
SIMILARITY: Belongs to the DOK family. Type A subfamily.
SIMILARITY: Contains 1 IRS-type PTB domain.
SIMILARITY: Contains 1 PH domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF034970; AAC13265.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032623; AAH32623.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_003965.2; -.

UniGene

Hs.71215

3D structure databases

PDB

2D9W; NMR; -; A=1-116.	[ExPASy / RCSB / EBI]
2DLW; NMR; -; A=153-247.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2D9W; -.
2DLW; -.

ModBase

O60496.

Protein-protein interaction databases

IntAct

O60496; 14.

PTM databases

PhosphoSite

O60496; -.

2D gel databases

OGP

O60496; -.

Organism-specific databases

GC08M021822; -.

HGNC:2991; DOK2.

CAB004379; -.

604997; gene. [NCBI / EBI]

PharmGKB

PA27457; -.

GeneCards

O60496.

Gene expression databases

ArrayExpress

O60496; -.

CleanEx

HS_DOK2; -.

GermOnline

ENSG00000147443; Homo sapiens.

Ontologies

GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0005158;	Molecular function: insulin receptor binding (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002404; Insln_rcpt_S1.
IPR001849; PH.
IPR011993; PH_type.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.29.30; PH_type; 1.

Pfam

PF02174; IRS; 1.
PF00169; PH; 1.
Pfam graphical view of domain structure.

SMART

SM00233; PH; 1.
SM00310; PTBI; 1.
SMART graphical view of domain structure.

PROSITE

PS51064; IRS_PTB; 1.
PS50003; PH_DOMAIN; 1.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

O60496; -.

Genome annotation databases

Ensembl

ENSG00000147443; Homo sapiens. [Contig view]

GeneID

9046; -.

KEGG

hsa:9046; -.

Phylogenomic databases

HOGENOM

O60496; -.

HOVERGEN

O60496; -.

Other

33885; -.

DOK2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 412`	`412`	`Docking protein 2.`	`PRO_0000187270`
`DOMAIN`	`4 114`	`111`	`PH.`
`DOMAIN`	`147 252`	`106`	`IRS-type PTB.`
`COMPBIAS`	`250 292`	`43`	`Pro-rich.`
`COMPBIAS`	`321 363`	`43`	`Pro-rich.`
`MOD_RES`	`271 271`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`299 299`		`Phosphotyrosine.`
`MOD_RES`	`345 345`		`Phosphotyrosine (By similarity).`
`VARIANT`	`152 152`	`1`	`A -> P (in dbSNP:rs1140295 [NCBI]).`	`VAR_030951`
`VARIANT`	`274 274`	`1`	`P -> L (in dbSNP:rs34215892 [NCBI]).`	`VAR_053068`
`VARIANT`	`394 394`	`1`	`S -> A (in dbSNP:rs2242241 [NCBI]).`	`VAR_030952`
`CONFLICT`	`166 166`		`L -> R (in Ref. 1; AAC13265).`
`CONFLICT`	`178 178`		`A -> S (in Ref. 1; AAC13265).`
`CONFLICT`	`347 347`		`E -> K (in Ref. 1; AAC13265).`
`CONFLICT`	`374 374`		`A -> R (in Ref. 1; AAC13265).`
`STRAND`	`5 13`	`9`
`STRAND`	`17 20`	`4`
`STRAND`	`25 31`	`7`
`STRAND`	`34 37`	`4`
`STRAND`	`40 44`	`5`
`STRAND`	`50 52`	`3`
`STRAND`	`57 60`	`4`
`HELIX`	`62 64`	`3`
`STRAND`	`65 70`	`6`
`STRAND`	`75 77`	`3`
`STRAND`	`82 90`	`9`
`STRAND`	`92 97`	`6`
`HELIX`	`99 113`	`15`
`STRAND`	`151 155`	`5`
`HELIX`	`159 164`	`6`
`STRAND`	`168 174`	`7`
`STRAND`	`176 180`	`5`
`STRAND`	`184 187`	`4`
`HELIX`	`196 198`	`3`
`STRAND`	`202 205`	`4`
`STRAND`	`208 213`	`6`
`STRAND`	`221 226`	`6`

Sequence information

Length: 412 AA [This is the length of the unprocessed precursor]

Molecular weight: 45379 Da [This is the MW of the unprocessed precursor]

CRC64: EFAEDBA68439757F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGDGAVKQGF LYLQQQQTFG KKWRRFGASL YGGSDCALAR LELQEGPEKP RRCEAARKVI 

        70         80         90        100        110        120 
RLSDCLRVAE AGGEASSPRD TSAFFLETKE RLYLLAAPAA ERGDWVQAIC LLAFPGQRKE 

       130        140        150        160        170        180 
LSGPEGKQSR PCMEENELYS SAVTVGPHKE FAVTMRPTEA SERCHLRGSY TLRAGESALE 

       190        200        210        220        230        240 
LWGGPEPGTQ LYDWPYRFLR RFGRDKVTFS FEAGRRCVSG EGNFEFETRQ GNEIFLALEE 

       250        260        270        280        290        300 
AISAQKNAAP ATPQPQPATI PASLPRPDSP YSRPHDSLPP PSPTTPVPAP RPRGQEGEYA 

       310        320        330        340        350        360 
VPFDAVARSL GKNFRGILAV PPQLLADPLY DSIEETLPPR PDHIYDEPEG VAALSLYDSP 

       370        380        390        400        410 
QEPRGEAWRR QATADRDPAG LQHVQPAGQD FSASGWQPGT EYDNVVLKKG PK

O60496 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools