PTPN9

PTPN9
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2PA5, 4GE2, 4GE5, 4GE6, 4ICZ
Identifiers
Aliases	PTPN9, MEG2, PTPMEG2, protein tyrosine phosphatase, non-receptor type 9, protein tyrosine phosphatase non-receptor type 9
External IDs	OMIM: 600768; MGI: 1928376; HomoloGene: 2121; GeneCards: PTPN9; OMA:PTPN9 - orthologs
Gene location (Human) Chr. Chromosome 15 (human) Band 15q24.2 Start 75,463,251 bp End 75,579,315 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 B Start 56,902,207 bp End 56,970,091 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence stromal cell of endometrium right lobe of thyroid gland left lobe of thyroid gland tibial nerve monocyte hair follicle islet of Langerhans rectum Top expressed in entorhinal cortex perirhinal cortex lactiferous gland choroid plexus of fourth ventricle Ileal epithelium CA3 field corneal stroma maxillary prominence Gonadal ridge mandibular prominence More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein tyrosine phosphatase activity phosphoprotein phosphatase activity hydrolase activity non-membrane spanning protein tyrosine phosphatase activity phosphatase activity protein binding Cellular component cytoplasm nucleoplasm neuron projection terminus Biological process protein dephosphorylation dephosphorylation cellular response to cytokine stimulus negative regulation of neuron projection development peptidyl-tyrosine dephosphorylation positive regulation of protein localization to plasma membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5780 56294 Ensembl ENSG00000169410 ENSMUSG00000032290 UniProt P43378 O35239 RefSeq (mRNA) NM_002833 NM_019651 RefSeq (protein) NP_002824 NP_062625 Location (UCSC) Chr 15: 75.46 – 75.58 Mb Chr 9: 56.9 – 56.97 Mb PubMed search
Wikidata
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Tyrosine-protein phosphatase non-receptor type 9 is an enzyme that in humans is encoded by the PTPN9 gene.

Function

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 poly-phosphoinositide, and is thought to be involved in signaling events regulating phagocytosis.

Further reading

• 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. S2CID 42894613.
• 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.
• 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. doi:10.4049/jimmunol.171.12.6661. 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. S2CID 25311826.
• 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.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Tyrosine-protein phosphatase non-receptor type 9 (PTPN9)