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Gene Review

PTPN3  -  protein tyrosine phosphatase, non-receptor...

Homo sapiens

Synonyms: PTP-H1, PTPH1, Protein-tyrosine phosphatase H1, Tyrosine-protein phosphatase non-receptor type 3
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Disease relevance of PTPN3


High impact information on PTPN3

  • The open reading frame predicts a protein of 913 amino acids (approximately 104 kDa), termed PTPH1 [4].
  • PTPH1 is a predominant protein-tyrosine phosphatase capable of interacting with and dephosphorylating the T cell receptor zeta subunit [5].
  • Furthermore, phorbol ester-stimulated shedding of the TACE substrate tumor necrosis factor-alpha was decreased in cells expressing catalytically active PTPH1 compared with inactive PTPH1 [6].
  • Our results suggest that PTPH1 may exert its effects on cell growth through dephosphorylation of VCP, thus implicating tyrosine phosphorylation as an important regulator of VCP function [7].
  • To identify the direct target of PTPH1 in the cell, we generated a substrate-trapping mutant, in which an invariant aspartate residue was changed to alanine (D811A in PTPH1) [7].

Biological context of PTPN3


Anatomical context of PTPN3

  • RESULTS: PTPN3 and PTPN4 were expressed in all gastric cancer cell lines and clinical cancer tissue specimens examined [1].
  • PTPH1 mRNA was detected in all HCC cell lines (n = 6), and HCC and adjacent noncancerous tissues (n = 8) examined, indicating that PTPH1 was expressed in HCCs and hepatocytes [3].
  • In contrast, the expression of PTPH1 mRNA was significantly increased in cancer lesions compared with that in normal mucosa [9].

Chemical compound and disease context of PTPN3


Associations of PTPN3 with chemical compounds

  • Moreover, induction of wild type PTPH1 resulted in specific dephosphorylation of VCP without changing the overall phosphotyrosine profile of the cells [7].
  • These results raise the possibility that 14-3-3beta may function as an adaptor molecule in the regulation of PTPH1 and may provide a link between serine/threonine and tyrosine phosphorylation-dependent signaling pathways [11].
  • These results suggest that in addition to a potential role in controlling subcellular localization, the NH2-terminal band 4.1 homology domain of PTPH1 may exert a direct effect on catalytic function [12].

Regulatory relationships of PTPN3


Other interactions of PTPN3


Analytical, diagnostic and therapeutic context of PTPN3


  1. PTPN3 and PTPN4 tyrosine phosphatase expression in human gastric adenocarcinoma. Wu, C.W., Chen, J.H., Kao, H.L., Li, A.F., Lai, C.H., Chi, C.W., Lin, W.C. Anticancer Res. (2006) [Pubmed]
  2. Expression and chromosomal assignment of PTPH1 gene encoding a cytosolic protein tyrosine phosphatase homologous to cytoskeletal-associated proteins. Itoh, F., Ikuta, S., Hinoda, Y., Arimura, Y., Ohe, M., Adachi, M., Ariyama, T., Inazawa, J., Imai, K., Yachi, A. Int. J. Cancer (1993) [Pubmed]
  3. Expression of cytoskeletal-associated protein tyrosine phosphatase PTPH1 mRNA in human hepatocellular carcinoma. Ikuta, S., Itoh, F., Hinoda, Y., Toyota, M., Makiguchi, Y., Imai, K., Yachi, A. J. Gastroenterol. (1994) [Pubmed]
  4. Isolation of a cDNA clone encoding a human protein-tyrosine phosphatase with homology to the cytoskeletal-associated proteins band 4.1, ezrin, and talin. Yang, Q., Tonks, N.K. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  5. PTPH1 is a predominant protein-tyrosine phosphatase capable of interacting with and dephosphorylating the T cell receptor zeta subunit. Sozio, M.S., Mathis, M.A., Young, J.A., Wälchli, S., Pitcher, L.A., Wrage, P.C., Bartók, B., Campbell, A., Watts, J.D., Aebersold, R., Van Huijsduijnen, R.H., van Oers, N.S. J. Biol. Chem. (2004) [Pubmed]
  6. Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1. Zheng, Y., Schlondorff, J., Blobel, C.P. J. Biol. Chem. (2002) [Pubmed]
  7. Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1. Zhang, S.H., Liu, J., Kobayashi, R., Tonks, N.K. J. Biol. Chem. (1999) [Pubmed]
  8. Cytoskeletal protein tyrosine phosphatase PTPH1 reduces T cell antigen receptor signaling. Han, S., Williams, S., Mustelin, T. Eur. J. Immunol. (2000) [Pubmed]
  9. Expression of protein tyrosine phosphatases and its significance in esophageal cancer. Warabi, M., Nemoto, T., Ohashi, K., Kitagawa, M., Hirokawa, K. Exp. Mol. Pathol. (2000) [Pubmed]
  10. Degradation of tyrosine phosphatase PTPN3 (PTPH1) by association with oncogenic human papillomavirus E6 proteins. Jing, M., Bohl, J., Brimer, N., Kinter, M., Vande Pol, S.B. J. Virol. (2007) [Pubmed]
  11. Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta protein. Zhang, S.H., Kobayashi, R., Graves, P.R., Piwnica-Worms, H., Tonks, N.K. J. Biol. Chem. (1997) [Pubmed]
  12. Biochemical characterization of a human band 4.1-related protein-tyrosine phosphatase, PTPH1. Zhang, S.H., Eckberg, W.R., Yang, Q., Samatar, A.A., Tonks, N.K. J. Biol. Chem. (1995) [Pubmed]
  13. Gene for the human transmembrane-type protein tyrosine phosphatase H (PTPRH): genomic structure, fine-mapping and its exclusion as a candidate for Peutz-Jeghers syndrome. Marneros, A.G., Mehenni, H., Reichenberger, E., Antonarakis, S.E., Krieg, T., Olsen, B.R. Cytogenet. Cell Genet. (2001) [Pubmed]
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