PTPN2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1L8K

Identifiers

Aliases

PTPN2, PTN2, PTPT, TC-PTP, TCELLPTP, TCPTP, protein tyrosine phosphatase, non-receptor type 2

External IDs

MGI: 97806 HomoloGene: 7497 GeneCards: PTPN2

Gene location (Human)

Chr.	Chromosome 18 (human)^[1]

Band	No data available	Start	12,785,478 bp^[1]
Band	No data available	End	12,929,643 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 18 (mouse)^[2]

Band	No data available	Start	67,665,511 bp^[2]
Band	No data available	End	67,724,595 bp^[2]

Gene ontology
Molecular function	• protein binding • protein kinase binding • phosphatase activity • integrin binding • phosphoprotein phosphatase activity • syntaxin binding • non-membrane spanning protein tyrosine phosphatase activity • receptor tyrosine kinase binding • hydrolase activity • protein tyrosine phosphatase activity • STAT family protein binding
Cellular component	• cytoplasm • membrane • plasma membrane • endoplasmic reticulum • nucleus • endoplasmic reticulum-Golgi intermediate compartment • nucleoplasm • cytosol
Biological process	• negative regulation of type I interferon-mediated signaling pathway • negative regulation of epidermal growth factor receptor signaling pathway • positive regulation of PERK-mediated unfolded protein response • dephosphorylation • negative regulation of interleukin-4-mediated signaling pathway • positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway • negative regulation of interleukin-6-mediated signaling pathway • negative regulation of cell proliferation • protein dephosphorylation • negative regulation of interleukin-2-mediated signaling pathway • regulation of interferon-gamma-mediated signaling pathway • negative regulation of protein tyrosine kinase activity • regulation of hepatocyte growth factor receptor signaling pathway • negative regulation of platelet-derived growth factor receptor-beta signaling pathway • insulin receptor signaling pathway • negative regulation of interferon-gamma-mediated signaling pathway • glucose homeostasis • negative regulation of chemotaxis • negative regulation of tumor necrosis factor-mediated signaling pathway • negative regulation of macrophage differentiation • negative regulation of T cell receptor signaling pathway • negative regulation of positive thymic T cell selection • negative regulation of insulin receptor signaling pathway • T cell differentiation • negative regulation of ERK1 and ERK2 cascade • erythrocyte differentiation • negative regulation of lipid storage • B cell differentiation • peptidyl-tyrosine dephosphorylation • positive regulation of gluconeogenesis • negative regulation of macrophage colony-stimulating factor signaling pathway • negative regulation of inflammatory response • negative regulation of transcription from RNA polymerase II promoter • negative regulation of tyrosine phosphorylation of STAT protein
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


5771


19255

Ensembl


ENSG00000175354


ENSMUSG00000024539

UniProt


P17706


Q06180

RefSeq (mRNA)


NM_001207013 NM_001308287 NM_002828 NM_080422 NM_080423


NM_001127177 NM_008977

RefSeq (protein)


NP_001193942 NP_001295216 NP_002819 NP_536347 NP_536348


NP_001120649 NP_033003

Location (UCSC)

Chr 18: 12.79 – 12.93 Mb

Chr 18: 67.67 – 67.72 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Tyrosine-protein phosphatase non-receptor type 2 is an enzyme that in humans is encoded by the PTPN2 gene.^[5]^[6]

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.^[6]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000175354 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024539 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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. PMC 54279 . PMID 2164224. doi:10.1073/pnas.87.13.5148.
1 2 "Entrez Gene: PTPN2 protein tyrosine phosphatase, non-receptor type 2".

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. PMC 48266 . PMID 1731319. doi:10.1073/pnas.89.2.499.
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. PMID 1849097. doi:10.1016/0014-5793(91)80205-H.
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. PMC 297600 . PMID 2546150. doi:10.1073/pnas.86.14.5257.
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. PMC 2120615 . PMID 7593185. doi:10.1083/jcb.131.3.631.
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. PMID 8125298. doi:10.1016/0378-1119(94)90802-8.
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. PMID 8325634. doi:10.1006/geno.1993.1239.
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. PMID 9261175. doi:10.1074/jbc.272.34.21548.
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. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3.
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. PMID 10488121. doi:10.1074/jbc.274.39.27768.
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. PMID 11773439. doi:10.1210/me.16.1.58.
Iversen LF, Moller KB, Pedersen AK, et al. (2002). "Structure determination of T cell protein-tyrosine phosphatase.". J. Biol. Chem. 277 (22): 19982–90. PMID 11907034. doi:10.1074/jbc.M200567200.
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. PMID 11909529. doi:10.1016/S0960-9822(02)00697-8.
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. PMC 133976 . PMID 12138178. doi:10.1128/MCB.22.16.5662-5668.2002.
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. PMID 12171910. doi:10.1074/jbc.C200346200.
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. PMID 12359225. doi:10.1016/S0006-291X(02)02291-X.
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. PMID 12459463. doi:10.1016/S0014-5793(02)03628-1.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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. PMC 149470 . PMID 12612081. doi:10.1128/MCB.23.6.2096-2108.2003.

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs

Receptor type PTPs	PTPRA PTPRB PTPRC PTPRD PTPRE PTPRF PTPRG PTPRH PTPRJ PTPRK PTPRM PTPRN PTPRN2 PTPRO PTPRQ PTPRR PTPRS PTPRT PTPRU PTPRZ1 PTPRZ2
Non receptor type PTPs	PTPN1 PTPN2 PTPN3 PTPN4 PTPN5 PTPN6 PTPN7 PTPN9 PTPN11 PTPN12 PTPN13 PTPN14 PTPN18 PTPN20 PTPN21 PTPN22 PTPN23

VH1-like or
dual specific
phosphatases
(DSPs)

MAPK phosphatases (MKPs)	DUSP1 DUSP2 DUSP4 DUSP5 DUSP6 DUSP7 DUSP8 DUSP9 DUSP10 DUSP16 MK-STYX
Slingshots	SSH1 SSH2 SSH3
PRLs	PTP4A1 PTP4A2 PTP4A3
CDC14s	CDC14A CDC14B CDKN3 PTP9Q22
Atypical DSPs	DUSP3 DUSP11 DUSP12 DUSP13A DUSP13B DUSP14 DUSP15 DUSP18 DUSP19 DUSP21 DUSP22 DUSP23 DUSP24 DUSP25 DUSP26 DUSP27 EMP2A RNGTT STYX
Phosphatase and tensin homologs (PTENs)	PTEN TPIP TPTE TNS TENC1
Myotubularins	MTM1 MTMR2 MTMR3 MTMR4 MTMR5 MTMR6 MTMR7 MTMR8 MTMR9 MTMR10 MTMR11 MTMR12 MTMR13 MTMR14 MTMR15

Class II

ACP1

Class III

Cdc25
- CDC25A
- CDC25B
- CDC25C

Class IV

EYA1
EYA2
EYA3
EYA4

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PTPN2

References

Further reading