Biology:PTPN9
 Generic protein structure example |
Tyrosine-protein phosphatase non-receptor type 9 is an enzyme that in humans is encoded by the PTPN9 gene.[1][2]
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.[2]
References
- ↑ "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. May 1992. doi:10.1073/pnas.89.7.2980. PMID 1557404. Bibcode: 1992PNAS...89.2980G.
- ↑ 2.0 2.1 "Entrez Gene: PTPN9 protein tyrosine phosphatase, non-receptor type 9". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5780.
Further reading
- "Protein-tyrosine phosphatase MEG2 is expressed by human neutrophils. Localization to the phagosome and activation by polyphosphoinositides". J. Biol. Chem. 277 (4): 2620–8. 2002. doi:10.1074/jbc.M104550200. PMID 11711529.
- "Purification and characterization of protein tyrosine phosphatase PTP-MEG2". J. Cell. Biochem. 86 (1): 79–89. 2002. doi:10.1002/jcb.10195. PMID 12112018.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Identification of protein tyrosine phosphatases with specificity for the ligand-activated growth hormone receptor". Mol. Endocrinol. 17 (11): 2228–39. 2004. doi:10.1210/me.2003-0011. PMID 12907755.
- "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. 2004. doi:10.1182/blood-2003-04-1308. PMID 12920026.
- "Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells". J. Immunol. 171 (12): 6661–71. 2004. doi:10.4049/jimmunol.171.12.6661. PMID 14662869.
- "Control of vesicle fusion by a tyrosine phosphatase". Nat. Cell Biol. 6 (9): 831–9. 2004. doi:10.1038/ncb1164. PMID 15322554.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Identification of the tyrosine phosphatase PTP-MEG2 as an antagonist of hepatic insulin signaling". Cell Metab. 3 (5): 367–78. 2007. doi:10.1016/j.cmet.2006.03.006. PMID 16679294.
- "Association of protein-tyrosine phosphatase MEG2 via its Sec14p homology domain with vesicle-trafficking proteins". J. Biol. Chem. 282 (20): 15170–8. 2007. 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)
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