Difference between revisions of "Phosphatase Subfamily PPP1C"
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=== Evolution === | === Evolution === | ||
PPP1C subfamily is found throughout eukaryotes even in some prokaryotes. It has many lineage-specific gene duplications. In particular, 10 PPP1Cs are found in fruit fly, 3 in human, 3 in ''C. elegans'', and 4 in yeast. | PPP1C subfamily is found throughout eukaryotes even in some prokaryotes. It has many lineage-specific gene duplications. In particular, 10 PPP1Cs are found in fruit fly, 3 in human, 3 in ''C. elegans'', and 4 in yeast. | ||
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| + | === Domain === | ||
| + | PPP1C has a single domain - phosphatase domain. | ||
=== Functions === | === Functions === | ||
Revision as of 17:38, 5 January 2015
Phosphatase Classification: Fold MTDP: Superfamily MTDP: Family PPP: Subfamily PPP1C
PPP1C is a ubiquitous serine/threonine phosphatase found throughout eukaryotes and even in some prokaryotes. By forming complexes with different regulatory subunits, it is involved in many various processes.
Contents
Evolution
PPP1C subfamily is found throughout eukaryotes even in some prokaryotes. It has many lineage-specific gene duplications. In particular, 10 PPP1Cs are found in fruit fly, 3 in human, 3 in C. elegans, and 4 in yeast.
Domain
PPP1C has a single domain - phosphatase domain.
Functions
PPP1C also called PP1 is the catalytic subunit binding to regulatory subunits to achieve diverse functions [1]. Over 50 different regulatory subunits are known in human and at least 20 in yeast. These different complexes play key roles in various cellular processes from cell cycle progression [2] to glycogen metabolism.
References
- Heroes E, Lesage B, Görnemann J, Beullens M, Van Meervelt L, and Bollen M. The PP1 binding code: a molecular-lego strategy that governs specificity. FEBS J. 2013 Jan;280(2):584-95. DOI:10.1111/j.1742-4658.2012.08547.x |
- Grallert A, Boke E, Hagting A, Hodgson B, Connolly Y, Griffiths JR, Smith DL, Pines J, and Hagan IM. A PP1-PP2A phosphatase relay controls mitotic progression. Nature. 2015 Jan 1;517(7532):94-98. DOI:10.1038/nature14019 |
