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Gene Review

Ppm1l  -  protein phosphatase 1 (formerly 2C)-like

Mus musculus

Synonyms: 3222401G13, 5930404J21Rik, AI481720, AW045850, Kiaa4175, ...
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Disease relevance of Ppm1l

  • Our findings highlight a role of PP2C and AMPK in the derangements of cardiac lipid metabolism in obesity and provide new insights as to the mechanisms of the liporegulatory disorder leading to lipotoxic cardiomyopathy [1].
  • In contrast, PP2C activity showed no remarkable alteration in the autoimmune disease model mice as compared with that in the control mice [2].
  • In poorly differentiated hepatomas, however, only PP1 alpha mRNA was specifically increased, in contrast to PP2A and PP2C, which were at the control levels or below [3].

High impact information on Ppm1l


Biological context of Ppm1l


Anatomical context of Ppm1l

  • The differential assay conditions for protein phosphatases PP1, PP2A, and PP2C were extensively studied by using crude extracts from mouse lymphoid tissues as enzyme sources [2].

Associations of Ppm1l with chemical compounds

  • It is a type 2C enzyme in view of its Mg2+ requirement, resistance to okadaic acid and calyculin A, inability to use phosphorylase alpha as substrate, and a segment of amino acid sequence typical of all PP2C type phosphatases known to date [7].
  • However, it differs from the other PP2C enzymes, particularly the mammalian PP2C alpha and -beta isoforms, in that its molecular weight, 76,000, is considerably larger and that it is inhibited by Ca2+, NaF, and polycations, but not by orthovanadate [7].
  • Role of PP2C in cardiac lipid accumulation in obese rodents and its prevention by troglitazone [1].


  1. Role of PP2C in cardiac lipid accumulation in obese rodents and its prevention by troglitazone. Wang, M.Y., Unger, R.H. Am. J. Physiol. Endocrinol. Metab. (2005) [Pubmed]
  2. Increase in potential activities of protein phosphatases PP1 and PP2A in lymphoid tissues of autoimmune MRL/MpJ-lpr/lpr mice. Matsuzawa, S., Tamura, T., Mizuno, Y., Kobayashi, S., Okuyama, H., Tsukitani, Y., Uemura, D., Kikuchi, K. J. Biochem. (1992) [Pubmed]
  3. Gene expressions and activities of protein phosphatases 1 alpha, 2A and 2C in hepatocarcinogenesis and regeneration after partial hepatectomy. Kikuchi, K., Kitamura, K., Kakinoki, Y., Nakamura, K., Matsuzawa, S., Saadat, M., Mizuno, Y. Cancer Detect. Prev. (1997) [Pubmed]
  4. Regulation of the multifunctional Ca2+/calmodulin-dependent protein kinase II by the PP2C phosphatase PPM1F in fibroblasts. Harvey, B.P., Banga, S.S., Ozer, H.L. J. Biol. Chem. (2004) [Pubmed]
  5. Ca(2+)-dependent conformational changes in guanylyl cyclase-activating protein 2 (GCAP-2) revealed by site-specific phosphorylation and partial proteolysis. Peshenko, I.V., Olshevskaya, E.V., Dizhoor, A.M. J. Biol. Chem. (2004) [Pubmed]
  6. Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon). Li, M.G., Katsura, K., Nomiyama, H., Komaki, K., Ninomiya-Tsuji, J., Matsumoto, K., Kobayashi, T., Tamura, S. J. Biol. Chem. (2003) [Pubmed]
  7. A Mg(2+)-dependent, Ca(2+)-inhibitable serine/threonine protein phosphatase from bovine brain. Wang, Y., Santini, F., Qin, K., Huang, C.Y. J. Biol. Chem. (1995) [Pubmed]
  8. Uniquely conserved non-translated regions are involved in generation of the two major transcripts of protein phosphatase 2Cbeta. Seroussi, E., Shani, N., Ben-Meir, D., Chajut, A., Divinski, I., Faier, S., Gery, S., Karby, S., Kariv-Inbal, Z., Sella, O., Smorodinsky, N.I., Lavi, S. J. Mol. Biol. (2001) [Pubmed]
  9. Localization of the mouse protein serine/threonine phosphatase 2C beta gene to chromosome 17E 4-5. Ohnishi, M., Nakagawara, K., Mori, M., Kobayashi, T., Kato, S., Sasahara, Y., Kusuda, K., Chida, N., Kobayashi, T., Yanagawa, Y., Hiraga, A., Takeuchi, T., Tamura, S. Genomics (1996) [Pubmed]
  10. Molecular cloning and characterization of a novel human protein phosphatase 2C cDNA (PP2C epsilon*). Jin, F., Ji, C., Liu, L., Dai, J., Gu, S., Sun, X., Xie, Y., Mao, Y. Mol. Biol. Rep. (2004) [Pubmed]
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