| Primary Identifier | IPR037981 | Type | Family |
| Short Name | PPP1CC |
| description | Serine/threonine-protein phosphatase PP1 () is a complex of a catalytic subunit, either PPP1CA, PPP1CB or PPP1CC, with one or more regulatory or targeting subunits. Example targeting subunits are PPP1R12A and PPP1R12C, which mediate binding of PP1 to myosin [, , ]; PPP1R3A, which mediates binding to glycogen in the skeletal muscle []; PPP1R7, []; PPP1R15A, which mediates binding to EIF2S1 []. The phosphatase associates with any one of many other regulatory proteins to form a complex that dephosphorylates a specific target protein. For example, centrosome splitting is regulated by the association of NEK2 with PP1 via the PPP1CA subunit [], binding to ATG16L1 antagonizes casein kinase 2-mediated phosphorylation of ATG16L1 affecting the fate of cadiomyocytes []and association with TNF-a induces phosphorylation of FOXP3 which controls regulatory T cell function []. PP1 is required for the cell cycle [], cell division, glycogen metabolism [], muscle contraction []and protein synthesis. PPP1CA and PPP1CB are components of the PTW/PP1 phosphatase complex [].This entry includes the catalytic subunit gamma (PPP1CC) from mammals, Dis2 from fission yeasts and Glc7 from budding yeasts. Glc7 is also a component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB []. |
