| Post Translational Modifications | Acetylation impairs ability to promote interaction between Akt/AKT1 and PHLPP1. Deacetylation by SIRT7 promotes interaction between Akt/AKT1 and PHLPP1, leading to suppress Akt/AKT1 activation. Ubiquitinated, leading to degradation in a proteasome-dependent manner. Deubiquitinated by USP49, leading to stabilization. |
| Function | Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappa-B activation, and IFN production. |
| Protein Name | Peptidyl-Prolyl Cis-Trans Isomerase Fkbp5Ppiase Fkbp551 Kda Fk506-Binding Protein51 Kda FkbpFkbp-5154 Kda Progesterone Receptor-Associated ImmunophilinAndrogen-Regulated Protein 6Ff1 AntigenFk506-Binding Protein 5Fkbp-5Fkbp54P54Hsp90-Binding ImmunophilinRotamase |
| Database Links | Reactome: R-HSA-3371497Reactome: R-HSA-8939211Reactome: R-HSA-9022699Reactome: R-HSA-9909505 |
| Cellular Localisation | CytoplasmNucleus |
| Alternative Antibody Names | Anti-Peptidyl-Prolyl Cis-Trans Isomerase Fkbp5 antibodyAnti-Ppiase Fkbp5 antibodyAnti-51 Kda Fk506-Binding Protein antibodyAnti-51 Kda Fkbp antibodyAnti-Fkbp-51 antibodyAnti-54 Kda Progesterone Receptor-Associated Immunophilin antibodyAnti-Androgen-Regulated Protein 6 antibodyAnti-Ff1 Antigen antibodyAnti-Fk506-Binding Protein 5 antibodyAnti-Fkbp-5 antibodyAnti-Fkbp54 antibodyAnti-P54 antibodyAnti-Hsp90-Binding Immunophilin antibodyAnti-Rotamase antibodyAnti-FKBP5 antibodyAnti-AIG6 antibodyAnti-FKBP51 antibody |
Information sourced from Uniprot.org
