DOK2

From Wikipedia, the free encyclopedia

Docking protein 2, 56kDa

PDB rendering based on 2d9w.

Available structures: 2d9w, 2dlw

Identifiers

Symbol(s)

DOK2; p56DOK; p56dok-2

External IDs

OMIM: 604997 MGI: 1332623 HomoloGene: 2957

Gene ontology
Molecular Function:	• transmembrane receptor protein tyrosine kinase docking protein activity • insulin receptor binding • protein binding
Biological Process:	• cell surface receptor linked signal transduction • transmembrane receptor protein tyrosine kinase signaling pathway • Ras protein signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003974 (mRNA)
NP_003965 (protein)

NM_010071 (mRNA)
NP_034201 (protein)

Location

Chr 8: 21.82 - 21.83 Mb

Chr 14: 69.51 - 69.51 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: DOK2 docking protein 2, 56kDa.

[edit] 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.