DOK1

DOK1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2V76
Identifiers
Aliases	DOK1, P62DOK, pp62, docking protein 1
External IDs	OMIM: 602919; MGI: 893587; HomoloGene: 1057; GeneCards: DOK1; OMA:DOK1 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p13.1 Start 74,549,026 bp[1] End 74,557,551 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6 C3|6 35.94 cM Start 83,007,915 bp[2] End 83,010,452 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tendon of biceps brachii pancreatic ductal cell monocyte granulocyte vena cava blood body of tongue internal globus pallidus spleen Skeletal muscle tissue of rectus abdominis Top expressed in stroma of bone marrow granulocyte mesenteric lymph nodes otic vesicle spleen fossa calvaria endothelial cell of lymphatic vessel thymus condyle More reference expression data BioGPS n/a
Gene ontology Molecular function protein binding Cellular component perinuclear region of cytoplasm nucleus cytoplasm cytosol Biological process cell surface receptor signaling pathway Ras protein signal transduction intracellular signal transduction signal transduction transmembrane receptor protein tyrosine kinase signaling pathway positive regulation of epidermal growth factor receptor signaling pathway axon guidance macrophage colony-stimulating factor signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1796 13448 Ensembl ENSG00000115325 ENSMUSG00000068335 UniProt Q99704 P97465 RefSeq (mRNA) NM_001197260 NM_001381 NM_001318866 NM_001318867 NM_001318868 NM_001318869 NM_001291799 NM_010070 RefSeq (protein) NP_001184189 NP_001305795 NP_001305796 NP_001305797 NP_001305798 NP_001372 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]

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:

• ABL1[9][10] and
• CD117,[11]
• INPP5D,[9][12]
• LYN,[9][11]
• RASA1,[10][12][13]
• RET,[14]
• SH2D1A,[15]
• SHC1,[12] and
• TEC.[9][11]

References

1. GRCh38: Ensembl release 89: ENSG00000115325 – Ensembl, May 2017
2. 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. 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. 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. 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. 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

• 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Wisniewski D, Strife A, Wojciechowicz D, Lambek C, Clarkson B (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, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• 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. doi:10.1016/S0092-8674(00)81841-3. PMID 9008161. S2CID 14205526.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. 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. doi:10.1084/jem.186.2.259. PMC 2198989. PMID 9221755.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Chen M, She H, Davis EM, Spicer CM, Kim L, Ren R, Le Beau MM, Li W (1998). "Identification of Nck family genes, chromosomal localization, expression, and signaling specificity". J. Biol. Chem. 273 (39): 25171–8. doi:10.1074/jbc.273.39.25171. PMID 9737977.
• Noguchi T, Matozaki T, Inagaki K, Tsuda M, Fukunaga K, Kitamura Y, Kitamura T, Shii K, Yamanashi Y, Kasuga M (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. PMC 1171261. PMID 10202139.
• Cong F, Yuan B, Goff SP (1999). "Characterization of a novel member of the DOK family that binds and modulates Abl signaling". Mol. Cell. Biol. 19 (12): 8314–25. doi:10.1128/MCB.19.12.8314. PMC 84915. PMID 10567556.
• Berg KL, Siminovitch KA, Stanley ER (1999). "SHP-1 regulation of p62(DOK) tyrosine phosphorylation in macrophages". J. Biol. Chem. 274 (50): 35855–65. doi:10.1074/jbc.274.50.35855. PMID 10585470.
• Becker E, Huynh-Do U, Holland S, Pawson T, Daniel TO, Skolnik EY (2000). "Nck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activation". Mol. Cell. Biol. 20 (5): 1537–45. doi:10.1128/MCB.20.5.1537-1545.2000. PMC 85333. 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. doi:10.1074/jbc.275.19.14590. PMID 10799545.
• Dunant NM, Wisniewski D, Strife A, Clarkson B, Resh MD (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.
• Yoshida K, Yamashita Y, Miyazato A, Ohya K, Kitanaka A, Ikeda U, Shimada K, Yamanaka T, Ozawa K, Mano H (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, Lane WS, Mosialos G, Kieff E (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.
• 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. doi:10.1046/j.1365-2370.2000.00203.x. PMID 10940083.
• Songyang Z, Yamanashi Y, Liu D, Baltimore D (2001). "Domain-dependent function of the rasGAP-binding protein p62Dok in cell signaling" (PDF). J. Biol. Chem. 276 (4): 2459–65. doi:10.1074/jbc.M005504200. PMID 11042170. S2CID 9752201.