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Proteins/UNIPROT:Q15257
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). 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+) (By similarity). 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..
Function from UniProtKB (Q15257), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
2 rows
87 statements
87 statements · 3 reference databases · Subject: PTPA · Sources: gene ontology, Hetionet, WikiPathways
1 reaction
[protein]-peptidylproline (omega=180)[protein]-peptidylproline (omega=0)
Catalysed by PPIH or FKBP9 or PPIB or FKBP2 or PPIF or NKTR or PPIC or PPIA or FKBP1A or FKBP1B or FKBP3 or FKBP4 and 16 more alternatives
Reaction pageDirection not assertedBalance undeterminable
Rhea RHEA:16237CC BY 4.0Reference data
5 names
Resolves to: PTPA