PTPN2

Protein tyrosine phosphatase, non-receptor type 2
PDB rendering based on 1l8k.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1L8K​
Identifiers
Symbols	PTPN2 ; PTN2; PTPT; TC-PTP; TCELLPTP; TCPTP
External IDs	OMIM: 176887 MGI: 97806 HomoloGene: 7497 ChEMBL: 3807 GeneCards: PTPN2 Gene
EC number	3.1.3.48
Gene ontology Molecular function • protein tyrosine phosphatase activity • integrin binding • protein binding • protein kinase binding • syntaxin binding • receptor tyrosine kinase binding Cellular component • nucleus • nucleoplasm • endoplasmic reticulum • endoplasmic reticulum-Golgi intermediate compartment • plasma membrane Biological process • negative regulation of cell proliferation • insulin receptor signaling pathway • negative regulation of tumor necrosis factor-mediated signaling pathway • negative regulation of lipid storage • cytokine-mediated signaling pathway • B cell differentiation • T cell differentiation • erythrocyte differentiation • peptidyl-tyrosine dephosphorylation • negative regulation of epidermal growth factor receptor signaling pathway • negative regulation of tyrosine phosphorylation of Stat1 protein • negative regulation of tyrosine phosphorylation of Stat3 protein • negative regulation of tyrosine phosphorylation of Stat5 protein • negative regulation of tyrosine phosphorylation of Stat6 protein • glucose homeostasis • negative regulation of macrophage differentiation • positive regulation of gluconeogenesis • negative regulation of insulin receptor signaling pathway • negative regulation of inflammatory response • negative regulation of T cell receptor signaling pathway • negative regulation of chemotaxis • interferon-gamma-mediated signaling pathway • regulation of interferon-gamma-mediated signaling pathway • negative regulation of interferon-gamma-mediated signaling pathway • negative regulation of type I interferon-mediated signaling pathway • negative regulation of protein tyrosine kinase activity • negative regulation of interleukin-6-mediated signaling pathway • negative regulation of ERK1 and ERK2 cascade • regulation of hepatocyte growth factor receptor signaling pathway • negative regulation of interleukin-2-mediated signaling pathway • negative regulation of prolactin signaling pathway • negative regulation of interleukin-4-mediated signaling pathway • negative regulation of macrophage colony-stimulating factor signaling pathway • negative regulation of positive thymic T cell selection • positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway • positive regulation of PERK-mediated unfolded protein response • negative regulation of platelet-derived growth factor receptor-beta signaling pathway Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5771	19255
Ensembl	ENSG00000175354	ENSMUSG00000024539
UniProt	P17706	Q06180
RefSeq (mRNA)	NM_001207013	NM_001127177
RefSeq (protein)	NP_001193942	NP_001120649
Location (UCSC)	Chr 18: 12.79 – 12.93 Mb	Chr 18: 67.67 – 67.72 Mb
PubMed search

Tyrosine-protein phosphatase non-receptor type 2 is an enzyme that in humans is encoded by the PTPN2 gene.^[1][2]

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. Epidermal growth factor receptor and the adaptor protein Shc were reported to be substrates of this PTP, which suggested the roles in growth factor mediated cell signaling. Three alternatively spliced variants of this gene, which encode isoforms differing at their extreme C-termini, have been described. The different C-termini are thought to determine the substrate specificity, as well as the cellular localization of the isoforms. Two highly related but distinctly processed pseudogenes that localize to distinct chromosomes have been reported.^[2]

References

1. Brown-Shimer S, Johnson KA, Lawrence JB, Johnson C, Bruskin A, Green NR, Hill DE (Aug 1990). "Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B". Proc Natl Acad Sci U S A 87 (13): 5148–52. doi:10.1073/pnas.87.13.5148. PMC 54279. PMID 2164224.
2. "Entrez Gene: PTPN2 protein tyrosine phosphatase, non-receptor type 2".

Further reading

• Mosinger B, Tillmann U, Westphal H, Tremblay ML (1992). "Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase.". Proc. Natl. Acad. Sci. U.S.A. 89 (2): 499–503. doi:10.1073/pnas.89.2.499. PMC 48266. PMID 1731319.
• Swarup G, Kamatkar S, Radha V, Rema V (1991). "Molecular cloning and expression of a protein-tyrosine phosphatase showing homology with transcription factors Fos and Jun.". FEBS Lett. 280 (1): 65–9. doi:10.1016/0014-5793(91)80205-H. PMID 1849097.
• Cool DE, Tonks NK, Charbonneau H, et al. (1989). "cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family.". Proc. Natl. Acad. Sci. U.S.A. 86 (14): 5257–61. doi:10.1073/pnas.86.14.5257. PMC 297600. PMID 2546150.
• Lorenzen JA, Dadabay CY, Fischer EH (1995). "COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleus.". J. Cell Biol. 131 (3): 631–43. doi:10.1083/jcb.131.3.631. PMC 2120615. PMID 7593185.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Johnson CV, Cool DE, Glaccum MB, et al. (1993). "Isolation and mapping of human T-cell protein tyrosine phosphatase sequences: localization of genes and pseudogenes discriminated using fluorescence hybridization with genomic versus cDNA probes.". Genomics 16 (3): 619–29. doi:10.1006/geno.1993.1239. PMID 8325634.
• Tiganis T, Flint AJ, Adam SA, Tonks NK (1997). "Association of the T-cell protein tyrosine phosphatase with nuclear import factor p97.". J. Biol. Chem. 272 (34): 21548–57. doi:10.1074/jbc.272.34.21548. PMID 9261175.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Tiganis T, Bennett AM, Ravichandran KS, Tonks NK (1998). "Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase.". Mol. Cell. Biol. 18 (3): 1622–34. PMC 108877. PMID 9488479.
• Tiganis T, Kemp BE, Tonks NK (1999). "The protein-tyrosine phosphatase TCPTP regulates epidermal growth factor receptor-mediated and phosphatidylinositol 3-kinase-dependent signaling.". J. Biol. Chem. 274 (39): 27768–75. doi:10.1074/jbc.274.39.27768. PMID 10488121.
• Aoki N, Matsuda T (2002). "A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus.". Mol. Endocrinol. 16 (1): 58–69. doi:10.1210/me.16.1.58. PMID 11773439.
• Iversen LF, Moller KB, Pedersen AK, et al. (2002). "Structure determination of T cell protein-tyrosine phosphatase.". J. Biol. Chem. 277 (22): 19982–90. doi:10.1074/jbc.M200567200. PMID 11907034.
• Simoncic PD, Lee-Loy A, Barber DL, et al. (2002). "The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3.". Curr. Biol. 12 (6): 446–53. doi:10.1016/S0960-9822(02)00697-8. PMID 11909529.
• ten Hoeve J, de Jesus Ibarra-Sanchez M, Fu Y, et al. (2002). "Identification of a nuclear Stat1 protein tyrosine phosphatase.". Mol. Cell. Biol. 22 (16): 5662–8. doi:10.1128/MCB.22.16.5662-5668.2002. PMC 133976. PMID 12138178.
• Zhu W, Mustelin T, David M (2002). "Arginine methylation of STAT1 regulates its dephosphorylation by T cell protein tyrosine phosphatase.". J. Biol. Chem. 277 (39): 35787–90. doi:10.1074/jbc.C200346200. PMID 12171910.
• Yamamoto T, Sekine Y, Kashima K, et al. (2002). "The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation.". Biochem. Biophys. Res. Commun. 297 (4): 811–7. doi:10.1016/S0006-291X(02)02291-X. PMID 12359225.
• Gupta S, Radha V, Sudhakar Ch, Swarup G (2003). "A nuclear protein tyrosine phosphatase activates p53 and induces caspase-1-dependent apoptosis.". FEBS Lett. 532 (1-2): 61–6. doi:10.1016/S0014-5793(02)03628-1. PMID 12459463.
• 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.
• Galic S, Klingler-Hoffmann M, Fodero-Tavoletti MT, et al. (2003). "Regulation of insulin receptor signaling by the protein tyrosine phosphatase TCPTP.". Mol. Cell. Biol. 23 (6): 2096–108. doi:10.1128/MCB.23.6.2096-2108.2003. PMC 149470. PMID 12612081.