PTPN9

Tyrosine-protein phosphatase non-receptor type 9 is an enzyme that in humans is encoded by the PTPN9 gene.[5][6]

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
Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q24.2 Start 75,463,251 bp[1] End 75,579,315 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 B Start 56,994,923 bp[2] End 57,062,807 bp[2]
RNA expression pattern 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 • GO:0001948 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: 56.99 – 57.06 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000169410 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032290 - 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. Gu M, Warshawsky I, Majerus PW (May 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. doi:10.1073/pnas.89.7.2980. PMC 48787. PMID 1557404.
6. "Entrez Gene: PTPN9 protein tyrosine phosphatase, non-receptor type 9".

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.
• 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. 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.
• 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. 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.

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)