Tyrosine-protein phosphatase non-receptor type 3 is an enzyme that in humans is encoded by the PTPN3 gene.[1][2]
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 protein contains a C-terminal PTP domain and an N-terminal domain homologous to the band 4.1 superfamily of cytoskeletal-associated proteins. P97, a cell cycle regulator involved in a variety of membrane related functions, has been shown to be a substrate of this PTP. This PTP was also found to interact with, and be regulated by adaptor protein 14-3-3 beta.[2]
Interactions [link]
PTPN3 has been shown to interact with YWHAB.[3]
References [link]
- ^ Yang Q, Tonks NK (Aug 1991). "Isolation of a cDNA clone encoding a human protein-tyrosine phosphatase with homology to the cytoskeletal-associated proteins band 4.1, ezrin, and talin". Proc Natl Acad Sci USA 88 (14): 5949–53. DOI:10.1073/pnas.88.14.5949. PMC 51999. PMID 1648725. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=51999.
- ^ a b "Entrez Gene: PTPN3 protein tyrosine phosphatase, non-receptor type 3". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5774.
- ^ Zhang, S H; Kobayashi R, Graves P R, Piwnica-Worms H, Tonks N K (Oct. 1997). "Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta protein". J. Biol. Chem. (UNITED STATES) 272 (43): 27281–7. DOI:10.1074/jbc.272.43.27281. ISSN 0021-9258. PMID 9341175.
Further reading [link]
- Arimura Y, Hinoda Y, Itoh F, et al. (1992). "cDNA cloning of new protein tyrosine phosphatases in the human colon.". Tumour Biol. 13 (3): 180–6. DOI:10.1159/000217763. PMID 1626183.
- Ikuta S, Itoh F, Hinoda Y, et al. (1995). "Expression of cytoskeletal-associated protein tyrosine phosphatase PTPH1 mRNA in human hepatocellular carcinoma.". J. Gastroenterol. 29 (6): 727–32. DOI:10.1007/BF02349278. PMID 7874267.
- Itoh F, Ikuta S, Hinoda Y, et al. (1994). "Expression and chromosomal assignment of PTPH1 gene encoding a cytosolic protein tyrosine phosphatase homologous to cytoskeletal-associated proteins.". Int. J. Cancer 55 (6): 947–51. DOI:10.1002/ijc.2910550612. PMID 8253532.
- Zhang SH, Kobayashi R, Graves PR, et al. (1997). "Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta protein.". J. Biol. Chem. 272 (43): 27281–7. DOI:10.1074/jbc.272.43.27281. PMID 9341175.
- Zhang SH, Liu J, Kobayashi R, Tonks NK (1999). "Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1.". J. Biol. Chem. 274 (25): 17806–12. DOI:10.1074/jbc.274.25.17806. PMID 10364224.
- Gjörloff-Wingren A, Saxena M, Han S, et al. (2000). "Subcellular localization of intracellular protein tyrosine phosphatases in T cells.". Eur. J. Immunol. 30 (8): 2412–21. DOI:10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J. PMID 10940933.
- Zheng Y, Schlondorff J, Blobel CP (2003). "Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1.". J. Biol. Chem. 277 (45): 42463–70. DOI:10.1074/jbc.M207459200. PMID 12207026.
- 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Sozio MS, Mathis MA, Young JA, et al. (2004). "PTPH1 is a predominant protein-tyrosine phosphatase capable of interacting with and dephosphorylating the T cell receptor zeta subunit.". J. Biol. Chem. 279 (9): 7760–9. DOI:10.1074/jbc.M309994200. PMID 14672952.
- Blanchetot C, Chagnon M, Dubé N, et al. (2005). "Substrate-trapping techniques in the identification of cellular PTP targets.". Methods 35 (1): 44–53. DOI:10.1016/j.ymeth.2004.07.007. PMID 15588985.
- Benzinger A, Muster N, Koch HB, et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer.". Mol. Cell Proteomics 4 (6): 785–95. DOI:10.1074/mcp.M500021-MCP200. PMID 15778465.
- Jespersen T, Gavillet B, van Bemmelen MX, et al. (2006). "Cardiac sodium channel Na(v)1.5 interacts with and is regulated by the protein tyrosine phosphatase PTPH1.". Biochem. Biophys. Res. Commun. 348 (4): 1455–62. DOI:10.1016/j.bbrc.2006.08.014. PMID 16930557.
- Jing M, Bohl J, Brimer N, et al. (2007). "Degradation of tyrosine phosphatase PTPN3 (PTPH1) by association with oncogenic human papillomavirus E6 proteins.". J. Virol. 81 (5): 2231–9. DOI:10.1128/JVI.01979-06. PMC 1865939. PMID 17166906. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1865939.
- Töpffer S, Müller-Schiffmann A, Matentzoglu K, et al. (2007). "Protein tyrosine phosphatase H1 is a target of the E6 oncoprotein of high-risk genital human papillomaviruses.". J. Gen. Virol. 88 (Pt 11): 2956–65. DOI:10.1099/vir.0.83123-0. PMID 17947517.
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