DOK1

Last updated
DOK1
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases DOK1 , P62DOK, pp62, docking protein 1
External IDs OMIM: 602919 MGI: 893587 HomoloGene: 1057 GeneCards: DOK1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001291799
NM_010070

RefSeq (protein)

NP_001278728
NP_034200

Location (UCSC) Chr 2: 74.55 – 74.56 Mb Chr 6: 83.01 – 83.01 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Docking protein 1 is a protein that in humans is encoded by the DOK1 gene. [5] [6] [7]

Contents

Function

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. [8]

Interactions

DOK1 has been shown to interact with:

Related Research Articles

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A non-receptor tyrosine kinase (nRTK) is a cytosolic enzyme that is responsible for catalysing the transfer of a phosphate group from a nucleoside triphosphate donor, such as ATP, to tyrosine residues in proteins. Non-receptor tyrosine kinases are a subgroup of protein family tyrosine kinases, enzymes that can transfer the phosphate group from ATP to a tyrosine residue of a protein (phosphorylation). These enzymes regulate many cellular functions by switching on or switching off other enzymes in a cell.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000115325 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000068335 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Carpino N, Wisniewski D, Strife A, Marshak D, Kobayashi R, Stillman B, Clarkson B (February 1997). "p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells". Cell. 88 (2): 197–204. doi: 10.1016/S0092-8674(00)81840-1 . PMID   9008160. S2CID   16781519.
  6. Nelms K, Snow AJ, Noben-Trauth K (December 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.
  7. Ling Y, Maile LA, Badley-Clarke J, Clemmons DR (February 2005). "DOK1 mediates SHP-2 binding to the alphaVbeta3 integrin and thereby regulates insulin-like growth factor I signaling in cultured vascular smooth muscle cells". J. Biol. Chem. 280 (5): 3151–8. doi: 10.1074/jbc.M411035200 . PMID   15546884.
  8. "Entrez Gene: DOK1 docking protein 1, 62kDa (downstream of tyrosine kinase 1)".
  9. 1 2 3 4 van Dijk TB, van Den Akker E, Amelsvoort MP, Mano H, Löwenberg B, von Lindern M (November 2000). "Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells". Blood. 96 (10): 3406–13. doi:10.1182/blood.V96.10.3406. hdl: 1765/9530 . PMID   11071635.
  10. 1 2 Yamanashi Y, Baltimore D (January 1997). "Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok". Cell. 88 (2): 205–11. doi: 10.1016/s0092-8674(00)81841-3 . PMID   9008161. S2CID   14205526.
  11. 1 2 3 Liang X, Wisniewski D, Strife A, Clarkson B, Resh MD (April 2002). "Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling". J. Biol. Chem. 277 (16): 13732–8. doi: 10.1074/jbc.M200277200 . PMID   11825908.
  12. 1 2 3 Dunant NM, Wisniewski D, Strife A, Clarkson B, Resh MD (May 2000). "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells". Cell. Signal. 12 (5): 317–26. doi:10.1016/s0898-6568(00)00073-5. PMID   10822173.
  13. Némorin JG, Duplay P (May 2000). "Evidence that Llck-mediated phosphorylation of p56dok and p62dok may play a role in CD2 signaling". J. Biol. Chem. 275 (19): 14590–7. doi: 10.1074/jbc.275.19.14590 . PMID   10799545.
  14. Murakami H, Yamamura Y, Shimono Y, Kawai K, Kurokawa K, Takahashi M (September 2002). "Role of Dok1 in cell signaling mediated by RET tyrosine kinase". J. Biol. Chem. 277 (36): 32781–90. doi: 10.1074/jbc.M202336200 . PMID   12087092.
  15. Sylla BS, Murphy K, Cahir-McFarland E, Lane WS, Mosialos G, Kieff E (June 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. Bibcode:2000PNAS...97.7470S. doi: 10.1073/pnas.130193097 . PMC   16569 . PMID   10852966.

Further reading