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Gene Review

PTP1  -  Ptp1p

Saccharomyces cerevisiae S288c

Synonyms: PTPase 1, Protein-tyrosine phosphatase 1, Tyrosine-protein phosphatase 1, YDL230W
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Disease relevance of PTP1


High impact information on PTP1


Biological context of PTP1

  • In this report, we demonstrate that although ptp2 has no obvious phenotype by itself, it has a profound effect on cell growth when combined with mutations in a novel protein phosphatase gene [11].
  • The PCR fragment was used to identify the yeast PTP1 gene which has an open reading frame encoding a 335-amino acid residue protein [1].
  • Molecular analysis has shown that PTP1 and PTP2 are quite different structurally and are not especially well conserved at the amino acid sequence level [12].
  • Correspondingly, several proteins phosphorylated at tyrosine by endogenous protein kinases exhibited a marked increase in tyrosine phosphorylation in ptp1 mutant cells [13].
  • The biological functions of these proteins are unknown, but they have vigorous protein-tyrosine phosphatase activity in vitro and have a sequence motif, Cys-X5-Arg, that is present at the active sites of all known types of protein-tyrosine phosphatases [14].

Anatomical context of PTP1


Associations of PTP1 with chemical compounds


Regulatory relationships of PTP1


Other interactions of PTP1


Analytical, diagnostic and therapeutic context of PTP1


  1. Cloning and expression of a yeast protein tyrosine phosphatase. Guan, K.L., Deschenes, R.J., Qiu, H., Dixon, J.E. J. Biol. Chem. (1991) [Pubmed]
  2. Identification of residues in the N-terminal domain of the Yersinia tyrosine phosphatase that are critical for substrate recognition. Montagna, L.G., Ivanov, M.I., Bliska, J.B. J. Biol. Chem. (2001) [Pubmed]
  3. Multimerization of the protein-tyrosine phosphatase (PTP)-like insulin-dependent diabetes mellitus autoantigens IA-2 and IA-2beta with receptor PTPs (RPTPs). Inhibition of RPTPalpha enzymatic activity. Gross, S., Blanchetot, C., Schepens, J., Albet, S., Lammers, R., den Hertog, J., Hendriks, W. J. Biol. Chem. (2002) [Pubmed]
  4. Using yeast to screen for inhibitors of protein tyrosine phosphatase 1B. Montalibet, J., Kennedy, B.P. Biochem. Pharmacol. (2004) [Pubmed]
  5. Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni. Tolkatchev, D., Shaykhutdinov, R., Xu, P., Plamondon, J., Watson, D.C., Young, N.M., Ni, F. Protein Sci. (2006) [Pubmed]
  6. A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase. Zhan, X.L., Guan, K.L. Genes Dev. (1999) [Pubmed]
  7. Differential regulation of FUS3 MAP kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase MSG5 in Saccharomyces cerevisiae. Zhan, X.L., Deschenes, R.J., Guan, K.L. Genes Dev. (1997) [Pubmed]
  8. PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase. Spencer, S., Dowbenko, D., Cheng, J., Li, W., Brush, J., Utzig, S., Simanis, V., Lasky, L.A. J. Cell Biol. (1997) [Pubmed]
  9. Association of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells. Cloutier, J.F., Veillette, A. EMBO J. (1996) [Pubmed]
  10. MSG5, a novel protein phosphatase promotes adaptation to pheromone response in S. cerevisiae. Doi, K., Gartner, A., Ammerer, G., Errede, B., Shinkawa, H., Sugimoto, K., Matsumoto, K. EMBO J. (1994) [Pubmed]
  11. Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cerevisiae. Maeda, T., Tsai, A.Y., Saito, H. Mol. Cell. Biol. (1993) [Pubmed]
  12. Multiple protein tyrosine phosphatase-encoding genes in the yeast Saccharomyces cerevisiae. James, P., Hall, B.D., Whelen, S., Craig, E.A. Gene (1992) [Pubmed]
  13. The yeast immunophilin Fpr3 is a physiological substrate of the tyrosine-specific phosphoprotein phosphatase Ptp1. Wilson, L.K., Benton, B.M., Zhou, S., Thorner, J., Martin, G.S. J. Biol. Chem. (1995) [Pubmed]
  14. Low molecular weight protein-tyrosine phosphatases are highly conserved between fission yeast and man. Mondesert, O., Moreno, S., Russell, P. J. Biol. Chem. (1994) [Pubmed]
  15. Isolation and characterization of a second protein tyrosine phosphatase gene, PTP2, from Saccharomyces cerevisiae. Guan, K., Deschenes, R.J., Dixon, J.E. J. Biol. Chem. (1992) [Pubmed]
  16. Arrest at the G2/M transition of the cell cycle by protein-tyrosine phosphatase inhibition: studies on a neuronal and a glial cell line. Faure, R., Vincent, M., Dufour, M., Shaver, A., Posner, B.I. J. Cell. Biochem. (1995) [Pubmed]
  17. Inaugural article: myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate. Taylor, G.S., Maehama, T., Dixon, J.E. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  18. Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14p. Gu, M., Warshawsky, I., Majerus, P.W. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  19. The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif. Gross, C., Heumann, R., Erdmann, K.S. FEBS Lett. (2001) [Pubmed]
  20. The S. cerevisiae nitrogen starvation-induced Yvh1p and Ptp2p phosphatases play a role in control of sporulation. Park, H.D., Beeser, A.E., Clancy, M.J., Cooper, T.G. Yeast (1996) [Pubmed]
  21. Directed evolution of a yeast arsenate reductase into a protein-tyrosine phosphatase. Mukhopadhyay, R., Zhou, Y., Rosen, B.P. J. Biol. Chem. (2003) [Pubmed]
  22. Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases. Wurgler-Murphy, S.M., Maeda, T., Witten, E.A., Saito, H. Mol. Cell. Biol. (1997) [Pubmed]
  23. Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3. Wilson, L.K., Dhillon, N., Thorner, J., Martin, G.S. J. Biol. Chem. (1997) [Pubmed]
  24. Cloning and characterization of a Saccharomyces cerevisiae gene encoding the low molecular weight protein-tyrosine phosphatase. Ostanin, K., Pokalsky, C., Wang, S., Van Etten, R.L. J. Biol. Chem. (1995) [Pubmed]
  25. CDC14 of Saccharomyces cerevisiae. Cloning, sequence analysis, and transcription during the cell cycle. Wan, J., Xu, H., Grunstein, M. J. Biol. Chem. (1992) [Pubmed]
  26. A novel putative protein-tyrosine phosphatase contains a BRO1-like domain and suppresses Ha-ras-mediated transformation. Cao, L., Zhang, L., Ruiz-Lozano, P., Yang, Q., Chien, K.R., Graham, R.M., Zhou, M. J. Biol. Chem. (1998) [Pubmed]
  27. Molecular cloning and expression of a cDNA encoding a protein tyrosine phosphatase from mouse brain. Park, K.S., Kim, Y.W., Kim, C.W., Kang, D.O., Byun, S.M. Biochem. Mol. Biol. Int. (1996) [Pubmed]
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