PTPN9

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Protein tyrosine phosphatase, non-receptor type 9
File:PBB Protein PTPN9 image.jpg
PDB rendering based on 2pa5.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PTPN9 ; MEG2
External IDs Template:OMIM5 Template:MGI HomoloGene2121
RNA expression pattern
File:PBB GE PTPN9 202958 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Protein tyrosine phosphatase, non-receptor type 9, also known as PTPN9, is a human gene.[1]

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an N-terminal domain that shares a significant similarity with yeast SEC14, which is a protein that has phosphatidylinositol transfer activity and is required for protein secretion through the Golgi complex in yeast. This PTP was found to be activated by polyphosphoinositide, and is thought to be involved in signaling events regulating phagocytosis.[1]

References

  1. 1.0 1.1 "Entrez Gene: PTPN9 protein tyrosine phosphatase, non-receptor type 9".

Further reading

  • Gu M, Warshawsky I, Majerus PW (1992). "Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14p". Proc. Natl. Acad. Sci. U.S.A. 89 (7): 2980–4. PMID 1557404.
  • Kruger JM, Fukushima T, Cherepanov V; et al. (2002). "Protein-tyrosine phosphatase MEG2 is expressed by human neutrophils. Localization to the phagosome and activation by polyphosphoinositides". J. Biol. Chem. 277 (4): 2620–8. doi:10.1074/jbc.M104550200. PMID 11711529.
  • Qi Y, Zhao R, Cao H; et al. (2002). "Purification and characterization of protein tyrosine phosphatase PTP-MEG2". J. Cell. Biochem. 86 (1): 79–89. doi:10.1002/jcb.10195. PMID 12112018.
  • 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. doi:10.1073/pnas.242603899. PMID 12477932.
  • Pasquali C, Curchod ML, Wälchli S; et al. (2004). "Identification of protein tyrosine phosphatases with specificity for the ligand-activated growth hormone receptor". Mol. Endocrinol. 17 (11): 2228–39. doi:10.1210/me.2003-0011. PMID 12907755.
  • Xu MJ, Sui X, Zhao R; et al. (2004). "PTP-MEG2 is activated in polycythemia vera erythroid progenitor cells and is required for growth and expansion of erythroid cells". Blood. 102 (13): 4354–60. doi:10.1182/blood-2003-04-1308. PMID 12920026.
  • Huynh H, Wang X, Li W; et al. (2004). "Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells". J. Immunol. 171 (12): 6661–71. PMID 14662869.
  • Huynh H, Bottini N, Williams S; et al. (2004). "Control of vesicle fusion by a tyrosine phosphatase". Nat. Cell Biol. 6 (9): 831–9. doi:10.1038/ncb1164. PMID 15322554.
  • 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. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • Cho CY, Koo SH, Wang Y; et al. (2007). "Identification of the tyrosine phosphatase PTP-MEG2 as an antagonist of hepatic insulin signaling". Cell Metab. 3 (5): 367–78. doi:10.1016/j.cmet.2006.03.006. PMID 16679294.
  • Saito K, Williams S, Bulankina A; et al. (2007). "Association of protein-tyrosine phosphatase MEG2 via its Sec14p homology domain with vesicle-trafficking proteins". J. Biol. Chem. 282 (20): 15170–8. doi:10.1074/jbc.M608682200. PMID 17387180.

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