SCUBA

PPP2CA — Protein phosphatase 2 catalytic subunit alpha

PPP2CA belongs to a gene co-expression module in 6 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

PPP2CA's module in each cell type

Cell typeModuleShares the module with
CD8⁺ T cellsVesicle Trafficking
Protein processing & ER
AP2M1, ARF1, CDC37, EWSR1, GHITM, GNB2, LMAN2, RAB11B +1 moreView in SCUBA
Gamma-delta T cellshnRNP Splicing Complex
RNA processing & translation
ASXL1, DDX21, HNRNPA1, HNRNPC, HNRNPH3, HSPA9, NOP58, PABPC1 +5 more
Innate lymphoid cellsIFN-driven ILC1 Activation
Inflammation
AFF3, AGPAT5, AKIRIN2, APMAP, ARF6, ARHGEF1, DNAJC1, DYNLT3 +21 moreView in SCUBA
MacrophagesActin Cytoskeleton Organization
Cytoskeletal
ACTR3, ARF1, ARHGDIA, ARPC4, CDC42, DERL1, EIF4G2, GARS1 +20 moreView in SCUBA
Mucosal-associated invariant T cellNF-κB RNA Regulation
RNA processing & translation
ARIH2, ATP1A1, BCLAF1, BNIP2, CALR, COG3, DDX6, EIF4G2 +14 more
Natural Killer cellsGlucocorticoid Response
Immune regulation
AREG, ARF6, BCLAF1, BEX2, BEX4, ELF1, ELL2, EPC1 +11 moreView in SCUBA

About the gene

SynonymsPP2AC, PP2Calpha
Chromosome5: 134194035-134226073
Predicted locationIntracellular
Essential geneYes
Protein classDisease related genes, Enzymes, Essential proteins, Human disease related genes, Potential drug targets, Predicted intracellular proteins
Molecular functionHydrolase, Protein phosphatase
Biological processMeiosis

Function

Catalytic subunit of protein phosphatase 2A (PP2A), a serine/threonine phosphatase involved in the regulation of a wide variety of enzymes, signal transduction pathways, and cellular events. PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate various proteins, such as SV40 large T antigen, AXIN1, p53/TP53, PIM3, WEE1. Activates RAF1 by dephosphorylating it at 'Ser-259'. Mediates dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint. Mediates dephosphorylation of MYC; promoting its ubiquitin-mediated proteolysis: interaction with AMBRA1 enhances interaction between PPP2CA and MYC. Mediates dephosphorylation of FOXO3; promoting its stabilization: interaction with AMBRA1 enhances interaction between PPP2CA and FOXO3. Catalyzes dephosphorylation of the pyrin domain of NLRP3, promoting assembly of the NLRP3 inflammasome (By similarity). Together with RACK1 adapter, mediates dephosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway (By similarity). Dephosphorylation of AKT1 is essential for regulatory T-cells (Treg) homeostasis and stability (By similarity). Catalyzes dephosphorylation of PIM3, promotinh PIM3 ubiquitination and proteasomal degradation. Part of the striatin- interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation. Key mediator of a quality checkpoint during transcription elongation as part of the Integrator-PP2A (INTAC) complex. The INTAC complex drives premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: within the INTAC complex, PPP2CA catalyzes dephosphorylation of the C-terminal domain (CTD) of Pol II subunit POLR2A/RPB1 and SUPT5H/SPT5, thereby preventing transcriptional elongation.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.