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Proteins/UNIPROT:Q14318
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)..
Function from UniProtKB (Q14318), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
1 row
114 statements
114 statements · 5 reference databases · Subject: FKBP8 · Sources: gene ontology, Hetionet, Reactome, UniProt, WikiPathways
2 reactions
10 names
Resolves to: FKBP8
[protein]-peptidylproline (omega=180)[protein]-peptidylproline (omega=0)
Catalysed by PPIH or FKBP9 or PPIB or FKBP2 or PPIF or NKTR or PPIC or PPIA or FKBP1A or FKBP1B or FKBP3 or FKBP4 and 16 more alternatives
Reaction pageDirection not assertedBalance undeterminable
Rhea RHEA:16237CC BY 4.0Reference data