FEATURES

FAMILY

phosphatase 2A regulatory subunit A family

DESCRIPTION

Also known as 2AAA_MOUSE, Ppp2r1a. The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (PubMed:10100624). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (By similarity). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (By similarity). PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation sites (PubMed:22417654). Interacts with IPO9 (By similarity). Interacts with TP53 and SGO1 (By similarity). Interacts with PLA2G16; this interaction might decrease PP2A activity (By similarity). Interacts with CTTNBP2NL (By similarity). Interacts with GNA12; the interaction promotes protein phosphatase 2A activation causing dephosphorylation of MAPT (By similarity).Interacts with CIP2A; this interaction stabilizes CIP2A (By similarity). Interacts with PABIR1/FAM122A (By similarity). Interacts with ADCY8; antagonizes interaction between ADCY8 and calmodulin (PubMed:16258073). Interacts with CRTC3 (when phosphorylated at 'Ser-391') (PubMed:30611118). Interacts with SPRY2 (By similarity).

EXTERNAL LINKS

Ppp2r1a

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Mutations

Mutation(s) distribution

Mutations table

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