| Post Translational Modifications | Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. |
| Function | Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis. Involved in the inhibition of viral infection by influenza A viruses (IAV). |
| Protein Name | Peptidyl-Prolyl Cis-Trans Isomerase Fkbp8Ppiase Fkbp838 Kda Fk506-Binding Protein38 Kda FkbpFkbp-38Hfkbp38Fk506-Binding Protein 8Fkbp-8Fkbpr38Rotamase |
| Database Links | Reactome: R-HSA-5689880 |
| Cellular Localisation | MitochondrionMitochondrion MembraneSingle-Pass Membrane ProteinCytoplasmic SideIsoform 1: Mitochondrion MembraneIsoform 3: Mitochondrion Membrane |
| Alternative Protein Names | Peptidyl-Prolyl Cis-Trans Isomerase Fkbp8 proteinPpiase Fkbp8 protein38 Kda Fk506-Binding Protein protein38 Kda Fkbp proteinFkbp-38 proteinHfkbp38 proteinFk506-Binding Protein 8 proteinFkbp-8 proteinFkbpr38 proteinRotamase proteinFKBP8 proteinFKBP38 protein |
Information sourced from Uniprot.org