38 kDa FK506-binding protein ; 38 kDa FKBP ; FK506-binding protein 8 ; FKBP-8 ; FKBPR38 ; Rotamase ; FKBP38
Categories
Elisa
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.
Specificity
Natural and recombinant Human Peptidyl-prolyl cis-trans isomerase FKBP8
Subcellular Location
Mitochondrion membrane Single-pass membrane protein Cytoplasmic side
Homomultimers or heteromultimers (Potential). Forms heterodimer with calmodulin. When activated by calmodulin and calcium, interacts with the BH4 domain of BCL2 and weakly with BCLX isoform Bcl-X(L). Does not bind and inhibit calcineurin. Interacts with HCV NS5A. Interacts with ZFYVE27; may negatively regulate ZFYVE27 phosphorylation.