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Gene Review

DOK2  -  docking protein 2, 56kDa

Homo sapiens

Synonyms: Docking protein 2, Dok-2, Downstream of tyrosine kinase 2, p56(dok-2), p56DOK, ...
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High impact information on DOK2


Biological context of DOK2

  • p62(DOK1) (DOK1) and p56(DOK2) (DOK2) are sequence homologs that act as docking proteins downstream of receptor or nonreceptor tyrosine kinases [4].
  • The data provide evidence that DOK1 and DOK2 proteins have a similar role in regulating cell proliferation and differentiation and are positive regulators of the MAPK signaling pathway in this context [4].

Anatomical context of DOK2

  • The data in this report show that both the DOK1 and the DOK2 adaptor proteins are constitutively expressed in the myelomonoblastic leukemia cell line, HL-60, and that expression of both proteins is induced by the chemotherapeutic differentiation causing agents, all-trans retinoic acid (atRA) and 1,25-dihydroxyvitamin D3 (VD3) [4].
  • Moreover, in CD2-stimulated Jurkat cells, Dok-1 coimmunoprecipitates with tyrosine-phosphorylated Dok-2 [3].

Associations of DOK2 with chemical compounds

  • Dok-R, also known as Dok-2/FRIP, belongs to the DOK family of signaling molecules that become tyrosine-phosphorylated by several different receptor and cytoplasmic tyrosine kinases [5].
  • Further, they raise the interesting possibility that Dok2 plays an important role in integrin outside-in signaling through a physical and functional interaction with integrin alpha(IIb)beta(3) [6].
  • Background: We previously demonstrated that Dok2 is rapidly phosphorylated on tyrosine residues in platelets in response to thrombin, the immunoreceptor tyrosine-based activation motif-coupled collagen receptor glycoprotein (GP) VI, and by integrin alpha(IIb)beta(3) [6].

Other interactions of DOK2


Analytical, diagnostic and therapeutic context of DOK2


  1. T cell receptor for antigen induces linker for activation of T cell-dependent activation of a negative signaling complex involving Dok-2, SHIP-1, and Grb-2. Dong, S., Corre, B., Foulon, E., Dufour, E., Veillette, A., Acuto, O., Michel, F. J. Exp. Med. (2006) [Pubmed]
  2. Differential proteome analysis of TRAP-activated platelets: involvement of DOK-2 and phosphorylation of RGS proteins. García, A., Prabhakar, S., Hughan, S., Anderson, T.W., Brock, C.J., Pearce, A.C., Dwek, R.A., Watson, S.P., Hebestreit, H.F., Zitzmann, N. Blood (2004) [Pubmed]
  3. Phosphotyrosine binding-mediated oligomerization of downstream of tyrosine kinase (Dok)-1 and Dok-2 is involved in CD2-induced Dok phosphorylation. Boulay, I., Némorin, J.G., Duplay, P. J. Immunol. (2005) [Pubmed]
  4. All-trans retinoic acid induces p62DOK1 and p56DOK2 expression which enhances induced differentiation and G0 arrest of HL-60 leukemia cells. Lamkin, T.J., Chin, V., Yen, A. Am. J. Hematol. (2006) [Pubmed]
  5. Dok-R binds c-Abl and regulates Abl kinase activity and mediates cytoskeletal reorganization. Master, Z., Tran, J., Bishnoi, A., Chen, S.H., Ebos, J.M., Van Slyke, P., Kerbel, R.S., Dumont, D.J. J. Biol. Chem. (2003) [Pubmed]
  6. Differential regulation of adapter proteins Dok2 and Dok1 in platelets, leading to an association of Dok2 with integrin alphabeta. Hughan, S.C., Watson, S.P. J. Thromb. Haemost. (2007) [Pubmed]
  7. Dok-3 sequesters Grb2 and inhibits the Ras-Erk pathway downstream of protein-tyrosine kinases. Honma, M., Higuchi, O., Shirakata, M., Yasuda, T., Shibuya, H., Iemura, S., Natsume, T., Yamanashi, Y. Genes Cells (2006) [Pubmed]
  8. Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins. Di Cristofano, A., Carpino, N., Dunant, N., Friedland, G., Kobayashi, R., Strife, A., Wisniewski, D., Clarkson, B., Pandolfi, P.P., Resh, M.D. J. Biol. Chem. (1998) [Pubmed]
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