DOK2

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Docking protein 2, 56kDa
PDB rendering based on 2d9w.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols DOK2 ; p56DOK; p56dok-2
External IDs Template:OMIM5 Template:MGI HomoloGene2957
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Docking protein 2, 56kDa, also known as DOK2, is a human gene.[1]

The protein encoded by this gene is constitutively tyrosine phosphorylated in hematopoietic progenitors isolated from chronic myelogenous leukemia (CML) patients in the chronic phase. It may be a critical substrate for p210(bcr/abl), a chimeric protein whose presence is associated with CML. This encoded protein binds p120 (RasGAP) from CML cells.[1]

References

  1. 1.0 1.1 "Entrez Gene: DOK2 docking protein 2, 56kDa".

Further reading

  • Jiang H, Harris MB, Rothman P (2000). "IL-4/IL-13 signaling beyond JAK/STAT". J. Allergy Clin. Immunol. 105 (6 Pt 1): 1063–70. PMID 10856136.
  • Di Cristofano A, Carpino N, Dunant N; et al. (1998). "Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins". J. Biol. Chem. 273 (9): 4827–30. PMID 9478921.
  • Jones N, Dumont DJ (1998). "The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R". Oncogene. 17 (9): 1097–108. doi:10.1038/sj.onc.1202115. PMID 9764820.
  • Jones N, Dumont DJ (2000). "Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation". Curr. Biol. 9 (18): 1057–60. PMID 10508618.
  • Némorin JG, Duplay P (2000). "Evidence that Llck-mediated phosphorylation of p56dok and p62dok may play a role in CD2 signaling". J. Biol. Chem. 275 (19): 14590–7. PMID 10799545.
  • Dunant NM, Wisniewski D, Strife A; et al. (2000). "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells". Cell. Signal. 12 (5): 317–26. PMID 10822173.
  • Némorin JG, Laporte P, Bérubé G, Duplay P (2001). "p62dok negatively regulates CD2 signaling in Jurkat cells". J. Immunol. 166 (7): 4408–15. PMID 11254695.
  • Grimm J, Sachs M, Britsch S; et al. (2001). "Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation". J. Cell Biol. 154 (2): 345–54. PMID 11470823.
  • Master Z, Jones N, Tran J; et al. (2001). "Dok-R plays a pivotal role in angiopoietin-1-dependent cell migration through recruitment and activation of Pak". EMBO J. 20 (21): 5919–28. doi:10.1093/emboj/20.21.5919. PMID 11689432.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Salomon AR, Ficarro SB, Brill LM; et al. (2003). "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry". Proc. Natl. Acad. Sci. U.S.A. 100 (2): 443–8. doi:10.1073/pnas.2436191100. PMID 12522270.
  • Jones N, Chen SH, Sturk C; et al. (2003). "A unique autophosphorylation site on Tie2/Tek mediates Dok-R phosphotyrosine binding domain binding and function". Mol. Cell. Biol. 23 (8): 2658–68. PMID 12665569.
  • Master Z, Tran J, Bishnoi A; et al. (2003). "Dok-R binds c-Abl and regulates Abl kinase activity and mediates cytoskeletal reorganization". J. Biol. Chem. 278 (32): 30170–9. doi:10.1074/jbc.M301339200. PMID 12777393.
  • García A, Prabhakar S, Hughan S; et al. (2004). "Differential proteome analysis of TRAP-activated platelets: involvement of DOK-2 and phosphorylation of RGS proteins". Blood. 103 (6): 2088–95. doi:10.1182/blood-2003-07-2392. PMID 14645010.
  • Gérard A, Favre C, Garçon F; et al. (2004). "Functional interaction of RasGAP-binding proteins Dok-1 and Dok-2 with the Tec protein tyrosine kinase". Oncogene. 23 (8): 1594–8. doi:10.1038/sj.onc.1207283. PMID 14647425.
  • Brill LM, Salomon AR, Ficarro SB; et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Rush J, Moritz A, Lee KA; et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
  • Van Slyke P, Coll ML, Master Z; et al. (2005). "Dok-R mediates attenuation of epidermal growth factor-dependent mitogen-activated protein kinase and Akt activation through processive recruitment of c-Src and Csk". Mol. Cell. Biol. 25 (9): 3831–41. doi:10.1128/MCB.25.9.3831-3841.2005. PMID 15831486.

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