PP2A alpha + beta Recombinant Rabbit Monoclonal Antibody [SN70-08] (ET1611-54)

UNIPROT #

P62714

PROTEIN NAME

PP2A alpha + beta

SYNONYMS

PP2A A antibody;PP2A alpha antibody;PP2A B antibody;PP2A beta antibody;PP2A-alpha antibody;PP2AA_HUMAN antibody;PP2Ac antibody;PP2CB antibody;PPP2CA antibody;PPP2CB antibody;Protein phosphatase 2 catalytic subunit alpha isoform antibody;Protein phosphatase 2 catalytic subunit beta isoform antibody;Replication protein C antibody;RP C antibody;RP-C antibody;Serine/threonine protein phosphatase 2A catalytic subunit alpha isoform antibody;Serine/threonine protein phosphatase 2A catalytic subunit beta isoform antibody;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform antibody

SEQUENCE SIMILARITIES

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

POST-TRANSLATIONAL MODIFICATION

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.; May be monoubiquitinated by NOSIP.

SUBCELLULAR LOCATION

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus.

FUNCTION

The catalytic subunit of protein phosphatase 2A (PP2A) is inactivated by in vitro phosphorylation of Tyr-307 by receptor and nonreceptor protein tyrosine kinases. The catalytic subunit of PP2A is phosphorylated by tyrosine-specific protein kinases and associates with a variety of regulatory subunits. Phosphorylation is enhanced in the presence of the phosphatase inhibitor okadaic acid, consistent with an autodephosphorylation reaction. Phosphorylation is catalyzed by p60v-src, p56lck, epidermal growth factor receptors, and insulin receptors. Transient deactivation of PP2A might enhance transmission of cellular signals through kinase cascades within cells. In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases.