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(Top) 1 Function 2 Interactions 3 References 4 Further reading

DOK2

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DOK2

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2D9W, 2DLW

Identifiers

Aliases

DOK2, p56DOK, p56dok-2, docking protein 2

External IDs

OMIM: 604997; MGI: 1332623; HomoloGene: 2957; GeneCards: DOK2; OMA:DOK2 - orthologs

Gene location (Human)

Chr.	Chromosome 8 (human)^[1]

Band	8p21.3	Start	21,908,873 bp^[1]
Band	8p21.3	End	21,913,690 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 14 (mouse)^[2]

Band	14 D2\|14 36.71 cM	Start	70,766,036 bp^[2]
Band	14 D2\|14 36.71 cM	End	70,778,495 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

granulocyte

monocyte

blood

spleen

lymph node

appendix

upper lobe of left lung

testicle

lower lobe of lung

right lung

Top expressed in

granulocyte

thymus

tibiofemoral joint

blood

spleen

morula

embryo

lymph node

fetal liver hematopoietic progenitor cell

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding transmembrane receptor protein tyrosine kinase adaptor activity
Cellular component	cytosol
Biological process	cell surface receptor signaling pathway Ras protein signal transduction leukocyte migration signal transduction transmembrane receptor protein tyrosine kinase signaling pathway axon guidance
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


9046


13449

Ensembl


ENSG00000147443


ENSMUSG00000022102

UniProt


O60496


O70469

RefSeq (mRNA)


NM_003974 NM_201349 NM_001317800 NM_001401272


NM_010071

RefSeq (protein)


NP_001304729 NP_003965 NP_958728


NP_034201 NP_001388209 NP_001388210

Location (UCSC)

Chr 8: 21.91 – 21.91 Mb

Chr 14: 70.77 – 70.78 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Docking protein 2 is a protein that in humans is encoded by the DOK2 gene.^[5]^[6]^[7]

Function[edit]

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.^[7]

Interactions[edit]

DOK2 has been shown to interact with INPP5D^[8] and TEK tyrosine kinase.^[9]^[10]

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000147443 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000022102 – Ensembl, May 2017

^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ Di Cristofano A, Carpino N, Dunant N, Friedland G, Kobayashi R, Strife A, Wisniewski D, Clarkson B, Pandolfi PP, Resh MD (March 1998). "Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins". J Biol Chem. 273 (9): 4827–30. doi:10.1074/jbc.273.9.4827. PMID 9478921.

^ Garcia A, Prabhakar S, Hughan S, Anderson TW, Brock CJ, Pearce AC, Dwek RA, Watson SP, Hebestreit HF, Zitzmann N (March 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.

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

^ 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.

^ 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. S2CID 20187169.

^ Master Z, Jones N, Tran J, Jones J, Kerbel RS, Dumont DJ (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. PMC 125712. PMID 11689432.

Further reading[edit]

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. doi:10.1067/mai.2000.107604. PMID 10856136.

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. S2CID 20187169.

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. doi:10.1016/S0960-9822(99)80458-8. PMID 10508618. S2CID 18831513.

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, 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. doi:10.1016/S0898-6568(00)00073-5. 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. doi:10.4049/jimmunol.166.7.4408. 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" (PDF). J. Cell Biol. 154 (2): 345–54. doi:10.1083/jcb.200102032. PMC 2150770. 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. PMC 125712. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. Bibcode:2003PNAS..100..443S. doi:10.1073/pnas.2436191100. PMC 141014. 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. doi:10.1128/MCB.23.8.2658-2668.2003. PMC 152553. 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.

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. S2CID 11822165.

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. PMC 528928. 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. S2CID 7200157.

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. PMC 1084282. PMID 15831486.

v t e PDB gallery
2d9w: Solution structure of the PH domain of Docking protein 2 from human 2dlw: Solution structure of the IRS domain of human docking protein 2, isoform a

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