Protein phosphatase that associates with over 200 regulatoryproteins to form highly specific holoenzymes which dephosphorylatehundreds of biological targets. Protein phosphatase 1 (PP1) isessential for cell division, and participates in the regulation ofglycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synapticplasticity. May play an important role in dephosphorylating substratessuch as the postsynaptic density-associated Ca (2+) /calmodulin dependentprotein kinase II. Component of the PTW/PP1 phosphatase complex, whichplays a role in the control of chromatin structure and cell cycleprogression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosomenumber and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Inbalance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivatingFOXP3 and rendering Treg cells functionally defective. Dephosphorylates CENPA. Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociationof ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy. [1-5]

MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK