Recombinant human PPP2R1A + PP2A-alpha protein (Active) (6x His tag N-Terminus, GST tag N-Terminus)

Specifications

Form

Liquid

Additional notes

Affinity purified.

General info

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 (PubMed : 10801873, PubMed : 12473674, PubMed : 17245430, PubMed : 22613722, PubMed : 33243860, PubMed : 34004147, PubMed : 9920888). PP2A is the major phosphatase for microtubule-associated proteins (MAPs) (PubMed : 22613722). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase (PubMed : 22613722). 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 (PubMed : 10801873, PubMed : 12473674, PubMed : 17245430, PubMed : 9920888). Activates RAF1 by dephosphorylating it at 'Ser-259' (PubMed : 10801873). Mediates dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint (PubMed : 33108758). Mediates dephosphorylation of MYC; promoting its ubiquitin-mediated proteolysis : interaction with AMBRA1 enhances interaction between PPP2CA and MYC (PubMed : 25438055). Mediates dephosphorylation of FOXO3; promoting its stabilization : interaction with AMBRA1 enhances interaction between PPP2CA and FOXO3 (PubMed : 30513302). 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, promoting PIM3 ubiquitination and proteasomal degradation (PubMed : 12473674). Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed : 33633399). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling (PubMed : 33633399). Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed : 33633399). Key mediator of a quality checkpoint during transcription elongation as part of the Integrator-PP2A (INTAC) complex (PubMed : 33243860, PubMed : 34004147, PubMed : 37080207). 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 (PubMed : 33243860, PubMed : 34004147, PubMed : 37080207).

Sequence similarities

Belongs to the PPP phosphatase family. PP-1 subfamily.

Post-translational modifications

Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1 (PPME1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.. Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation.. Polyubiquitinated, leading to its degradation by the proteasome.

Subcellular localisation

Nucleus