[1]
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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).
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[2]
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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).
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[3]
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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).
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[4]
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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).
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[5]
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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).
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[6]
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STRUCTURE BY NMR OF 153-247.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the IRS domain of human docking protein 2, isoform A.";
Submitted (OCT-2006) to the PDB data bank.
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- 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.
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