FUNCTION Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.CATALYTIC ACTIVITY O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphateCATALYTIC ACTIVITY O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphateCOFACTOR Binds 2 magnesium or manganese ions per subunit.SUBUNIT Monomer. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling. Interacts with the phosphorylated form of IKBKB/IKKB.INTERACTION Weakly associates at the membrane and N-myristoylation mediates the membrane localization.ALTERNATIVE PRODUCTS N-myristoylation is essential for the recognition of its substrates for dephosphorylation.SIMILARITY Belongs to the PP2C family.
recommendedName: Protein phosphatase 1A ecNumber evidence="3 9"3.1.3.16 alternativeName: Protein phosphatase 2C isoform alpha shortName: PP2C-alpha alternativeName: Protein phosphatase IA
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