| Primary Identifier | IPR011236 | Type | Family |
| Short Name | Ser/Thr_PPase_5 |
| description | These eukaryotic serine/threonine phosphoprotein phosphatases, first described from human (PP5) and Saccharomyces cerevisiae (PPT1), are distinguished from related protein phosphatases by an N-terminal region of about 200 residues that contains three tandem tetratricopeptide repeats (TPR) []. Structurally, TPR repeats form a helical scaffold of antiparallel α-helices with an amphipathic groove that mediates protein-protein interactions []. The TPR domains contribute to regulation of PP5 activity, which is normally low but stimulated by interaction with lipid [], and to interaction with other proteins [].PPT1 specifically binds to and dephosphorylates Hsp90 and this dephosphorylation positively regulates the Hsp90 chaperone machinery []. PPP5 is involved in a wide range of processes including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response hormones, calcium, fatty acids, TGF-beta and also oxidative and genotoxic stresses [, , ]. |
