| Function | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis.the function appears to be independent from PP2A. |
| Protein Name | Serine/Threonine-Protein Phosphatase 2a ActivatorPp2a - Subunit B' - Pr53 IsoformPhosphotyrosyl Phosphatase ActivatorPtpaSerine/Threonine-Protein Phosphatase 2a Regulatory Subunit 4Serine/Threonine-Protein Phosphatase 2a Regulatory Subunit B' |
| Cellular Localisation | CytoplasmNucleus |
| Alternative Protein Names | Serine/Threonine-Protein Phosphatase 2a Activator proteinPp2a - Subunit B' - Pr53 Isoform proteinPhosphotyrosyl Phosphatase Activator proteinPtpa proteinSerine/Threonine-Protein Phosphatase 2a Regulatory Subunit 4 proteinSerine/Threonine-Protein Phosphatase 2a Regulatory Subunit B' proteinPTPA proteinPPP2R4 protein |
Information sourced from Uniprot.org
