PPP1CA

PPP1CA is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function.

protein phosphatase 1 catalytic subunit alpha

Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number 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. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208).
Dephosphorylates CENPA (PubMed:25556658).
Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (PubMed:26083323).
(Microbial infection) Necessary for alphaviruses replication.

Beta-catenin destruction complex disassemblyISS:ParkinsonsUK-UCL
Branching morphogenesis of an epithelial tubeIEA:Ensembl
Cell cycleIEA:UniProtKB-KW
Cell divisionIEA:UniProtKB-KW
Circadian regulation of gene expressionISS:UniProtKB
DephosphorylationManual Assertion Based On ExperimentIDA:CACAO
Entrainment of circadian clock by photoperiodISS:UniProtKB
Glycogen metabolic processIEA:UniProtKB-KW
Lung developmentIEA:Ensembl
Negative regulation of protein bindingISS:ParkinsonsUK-UCL
Peptidyl-serine dephosphorylationManual Assertion Based On ExperimentTAS:ARUK-UCL
Peptidyl-threonine dephosphorylationManual Assertion Based On ExperimentTAS:ARUK-UCL
Positive regulation of extrinsic apoptotic signaling pathway in absence of ligandIEA:Ensembl
Protein dephosphorylationManual Assertion Based On ExperimentIMP:CACAO
Regulation of canonical Wnt signaling pathway1 PublicationIC:ParkinsonsUK-UCL
Regulation of circadian rhythmManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of glycogen biosynthetic processIEA:Ensembl
Regulation of glycogen catabolic processIEA:Ensembl
Regulation of translational initiation by eIF2 alpha dephosphorylationISS:ParkinsonsUK-UCL
Response to lead ionISS:ARUK-UCL

Cytoplasm
Nucleus
Nucleus, nucleoplasm
Nucleus, nucleolus
Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. Shuttles toward the cytosol during infection with VEEV (PubMed:29769351).

Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation.