DOK1

From Wikipedia, the free encyclopedia

Docking protein 1, 62kDa (downstream of tyrosine kinase 1)

Identifiers

DOK1; MGC117395; MGC138860; P62DOK

External IDs

OMIM: 602919 MGI: 893587 HomoloGene: 1057

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

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_001381 (mRNA)
NP_001372 (protein)

NM_010070 (mRNA)
NP_034200 (protein)

Location

n/a

Chr 6: 83 - 83 Mb

Pubmed search

[1]

[2]

Docking protein 1, 62kDa (downstream of tyrosine kinase 1), also known as DOK1, is a human gene.

Docking protein 1 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. Docking protein 1 contains a putative pleckstrin homology domain at the amino terminus and ten PXXP SH3 recognition motifs. Docking protein 2 binds p120 (RasGAP) from CML cells. It has been postulated to play a role in mitogenic signaling.^[1]

[edit] References

^ Entrez Gene: DOK1 docking protein 1, 62kDa (downstream of tyrosine kinase 1).

[edit] Further reading

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Wisniewski D, Strife A, Wojciechowicz D, et al. (1994). "A 62-kilodalton tyrosine phosphoprotein constitutively present in primary chronic phase chronic myelogenous leukemia enriched lineage negative blast populations.". Leukemia 8 (4): 688–93. PMID 8152267.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Carpino N, Wisniewski D, Strife A, et al. (1997). "p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells.". Cell 88 (2): 197–204. PMID 9008160.
Yamanashi Y, Baltimore D (1997). "Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok.". Cell 88 (2): 205–11. PMID 9008161.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
Vuica M, Desiderio S, Schneck JP (1997). "Differential effects of B cell receptor and B cell receptor-FcgammaRIIB1 engagement on docking of Csk to GTPase-activating protein (GAP)-associated p62.". J. Exp. Med. 186 (2): 259–67. PMID 9221755.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Chen M, She H, Davis EM, et al. (1998). "Identification of Nck family genes, chromosomal localization, expression, and signaling specificity.". J. Biol. Chem. 273 (39): 25171–8. PMID 9737977.
Nelms K, Snow AJ, Noben-Trauth K (1998). "Dok1 encoding p62(dok) maps to mouse chromosome 6 and human chromosome 2 in a region of translocation in chronic lymphocytic leukemia.". Genomics 53 (2): 243–5. doi:10.1006/geno.1998.5514. PMID 9790776.
Noguchi T, Matozaki T, Inagaki K, et al. (1999). "Tyrosine phosphorylation of p62(Dok) induced by cell adhesion and insulin: possible role in cell migration.". EMBO J. 18 (7): 1748–60. doi:10.1093/emboj/18.7.1748. PMID 10202139.
Cong F, Yuan B, Goff SP (2000). "Characterization of a novel member of the DOK family that binds and modulates Abl signaling.". Mol. Cell. Biol. 19 (12): 8314–25. PMID 10567556.
Berg KL, Siminovitch KA, Stanley ER (2000). "SHP-1 regulation of p62(DOK) tyrosine phosphorylation in macrophages.". J. Biol. Chem. 274 (50): 35855–65. PMID 10585470.
Becker E, Huynh-Do U, Holland S, et al. (2000). "Nck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activation.". Mol. Cell. Biol. 20 (5): 1537–45. PMID 10669731.
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.
Yoshida K, Yamashita Y, Miyazato A, et al. (2000). "Mediation by the protein-tyrosine kinase Tec of signaling between the B cell antigen receptor and Dok-1.". J. Biol. Chem. 275 (32): 24945–52. doi:10.1074/jbc.M909012199. PMID 10823839.
Sylla BS, Murphy K, Cahir-McFarland E, et al. (2000). "The X-linked lymphoproliferative syndrome gene product SH2D1A associates with p62dok (Dok1) and activates NF-kappa B.". Proc. Natl. Acad. Sci. U.S.A. 97 (13): 7470–5. doi:10.1073/pnas.130193097. PMID 10852966.
Hubert P, Ferreira V, Debre P, Bismuth G (2000). "Molecular cloning of a truncated p62Dok1 isoform, p22Dok(del).". Eur. J. Immunogenet. 27 (3): 145–8. PMID 10940083.
Songyang Z, Yamanashi Y, Liu D, Baltimore D (2001). "Domain-dependent function of the rasGAP-binding protein p62Dok in cell signaling.". J. Biol. Chem. 276 (4): 2459–65. doi:10.1074/jbc.M005504200. PMID 11042170.