is a catalytic subunit of protein phosphatase 1 (PP1), a ubiquitous cytosolic serine-threonine phosphatase. Composed a catalytic subunit (PPP1CA, PPP1CB or PPP1CC) which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting (or regulatory) subunits: PPP1R12A and PPP1R12B mediate binding to myosin; PPP1R3A, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen; and PPP1R15A and PPP1R15B mediate binding to EIF2S1. PP1 is essential for cell division, plays critical roles in many cellular processes including glycogen metabolism, muscle contractility and protein synthesis, and is involved in the regulation of ionic conductances and long-term synaptic plasticity. Inhibits the synthesis of proteins involved in synaptic plasticity. Binds to the transcription factor cyclic AMP-dependent response element binding (CREB) and dephosphorylates it. May regulate chromatin condensation through regulation of histone H3 phosphorylation. Differentially expressed in gastric cancer. May participate in the neurodegenerative progress in Alzheimer's disease. Down-regulated in lung squamous cell carcinoma. Note: This description may include information from UniProtKB.
Protein type: Nucleolus; Protein phosphatase, Ser/Thr (non-receptor); Motility/polarity/chemotaxis; EC 126.96.36.199
Molecular Function: phosphoprotein phosphatase activity; phosphoric monoester hydrolase activity; protein binding; protein kinase binding; protein N-terminus binding; protein serine/threonine phosphatase activity
Biological Process: circadian regulation of gene expression; entrainment of circadian clock by photoperiod; protein amino acid dephosphorylation; regulation of circadian rhythm; sister chromatid cohesion
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.