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Gene Review

PTPRR  -  protein tyrosine phosphatase, receptor...

Homo sapiens

Synonyms: Ch-1PTPase, EC-PTP, ECPTP, NC-PTPCOM1, PCPTP1, ...
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Disease relevance of PTPRR


High impact information on PTPRR

  • TEL/PTPRR did not exhibit any tyrosine phosphatase activity [2].
  • Importantly, overexpression of TEL/PTPRR in granulocyte macrophage colony-stimulating factor-dependent UT7/GM cells resulted in their factor-independent proliferation, whereas overexpression of tTEL did not [2].
  • The chimeric gene fused exon 4 of the TEL gene with exon 7 of the PTPRR gene, and produced 10 isoforms through alternative splicing [2].
  • Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway [3].
  • PTP-SL is a substrate of ERK5 and independent of phosphorylation binding to the kinase enhances its catalytic phosphatase activity [3].

Biological context of PTPRR

  • This locus, however, does not appear to correspond to the PTPRR or CPM, although a contribution of mutations in regulatory regions cannot be excluded at this time [4].
  • Here, we examined the array of post-translational modifications imposed on the PTPRR protein isoforms PTPBR7, PTP-SL, PTPPBSgamma42 and PTPPBSgamma37, which have distinct N-terminal segments and localize to different parts of the cell [5].
  • Therefore, it is likely that the decrease in the level of PCPTP1 mRNA might be associated or correlated with cell differentiation in PC12h cells [6].
  • In contrast to the PTP-SL structure, however, HePTP crystallized with a well-ordered phosphate ion bound at the active site [7].
  • A transcriptional up-regulation during sporogony is supported by a strong increase in the relative amount of Ecptp mRNAs within host cells sampled at late post-infection times [8].

Anatomical context of PTPRR

  • The 3.9-kb PCPTP1 mRNA was detected in the brain and adrenal gland, but not in other non-neuronal tissues in adult rats [6].
  • RESULTS: We found a single KIM-containing PTP to be endogenously expressed in rat PC12 cells: the transmembrane PTPRR isoform termed PCPTP1 [9].

Associations of PTPRR with chemical compounds

  • These two proteins correspond to the products translated from the second and fifth methionine of PCPTP1, respectively [6].

Physical interactions of PTPRR

  • Under control conditions, PTP-SL bound preferentially to ERK1/2, whereas STEP and HePTP bound preferentially to p38alpha [10].

Regulatory relationships of PTPRR

  • In intact cells, PTP-SL and STEP distinctively regulated the kinase activity and the nuclear translocation of ERK1/2 and p38alpha [10].

Other interactions of PTPRR

  • Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agents [10].
  • The protein tyrosine phosphatases (PTPs) PTP-SL, STEP and HePTP are mitogen-activated protein kinase (MAPK) substrates and regulators that bind to MAPKs through a kinase-interaction motif (KIM) located in their non-catalytic regulatory domains [10].
  • The HePTP catalytic phosphatase domain displays the classical PTP1B fold and superimposes well with PTP-SL, the first KIM-containing phosphatase solved to high resolution [7].

Analytical, diagnostic and therapeutic context of PTPRR

  • After cytokine depletion, phosphorylated signal transducers and activators of transcription 3 (STAT3) significantly declined in mock cells, but remained in both tTEL- and TEL/PTPRR-overexpressing cells [2].
  • Northern blot analysis showed only one 3.9-kb transcript in PC12h cells, indicating that PCPTP1 corresponds to this 3.9-kb transcript [6].
  • Western blot analysis using a polyclonal Ab (antibody) raised against the cytoplasmic region of PCPTP1 detected two products, a major 65-kDa and minor 42-kDa protein, designated PCPTP1-MFI and PCPTP1-MVQ, respectively, in PC12h cells [6].


  1. Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases. Eswaran, J., von Kries, J.P., Marsden, B., Longman, E., Debreczeni, J.E., Ugochukwu, E., Turnbull, A., Lee, W.H., Knapp, S., Barr, A.J. Biochem. J. (2006) [Pubmed]
  2. Cloning and characterization of the novel chimeric gene TEL/PTPRR in acute myelogenous leukemia with inv(12)(p13q13). Nakamura, F., Nakamura, Y., Maki, K., Sato, Y., Mitani, K. Cancer Res. (2005) [Pubmed]
  3. Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway. Buschbeck, M., Eickhoff, J., Sommer, M.N., Ullrich, A. J. Biol. Chem. (2002) [Pubmed]
  4. Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes. Bektas, A., Hughes, J.N., Warram, J.H., Krolewski, A.S., Doria, A. Diabetes (2001) [Pubmed]
  5. Proteolytic processing of the receptor-type protein tyrosine phosphatase PTPBR7. Dilaver, G., van de Vorstenbosch, R., Tárrega, C., Ríos, P., Pulido, R., van Aerde, K., Fransen, J., Hendriks, W. FEBS J. (2007) [Pubmed]
  6. Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase. Shiozuka, K., Watanabe, Y., Ikeda, T., Hashimoto, S., Kawashima, H. Gene (1995) [Pubmed]
  7. Structure of the hematopoietic tyrosine phosphatase (HePTP) catalytic domain: structure of a KIM phosphatase with phosphate bound at the active site. Mustelin, T., Tautz, L., Page, R. J. Mol. Biol. (2005) [Pubmed]
  8. The microsporidian polar tube: evidence for a third polar tube protein (PTP3) in Encephalitozoon cuniculi. Peuvel, I., Peyret, P., Méténier, G., Vivarès, C.P., Delbac, F. Mol. Biochem. Parasitol. (2002) [Pubmed]
  9. Tyrosine-specific MAPK phosphatases and the control of ERK signaling in PC12 cells. Noordman, Y.E., Jansen, P.A., Hendriks, W.J. Journal of molecular signaling (2006) [Pubmed]
  10. Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agents. Muñoz, J.J., Tárrega, C., Blanco-Aparicio, C., Pulido, R. Biochem. J. (2003) [Pubmed]
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