Description
Product Characteristics:
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. 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.Tissue specificity: Widely expressed. Highest levels seen in the brain.
Subcellular location: Cytoplasm
Synonyms: 38 kDa FK 506 binding protein homolog, 38 kDa FK506-binding protein, 38 kDa FKBP, 38 kDa antibody FK506 binding protein 8, FK506 binding protein 8, 38 kDa, FK506 binding protein, 38 kDa, FK506-binding protein 8, FKBP 38, FKBP-38, FKBP-8, FKBP8, FKBP8_HUMAN, FKBPR38, hFKBP38, Peptidyl-prolyl cis-trans isomerase FKBP8, PPIase FKBP8, Rotamase, Sam11.
Target Information: The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. Unlike the other members of the family, this encoded protein does not seem to have PPIase/rotamase activity. It may have a role in neurons associated with memory function. [provided by RefSeq, Jul 2008]