FKBP8 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. Widely expressed. Highest levels seen in the brain. Highly abundant in the retina. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Chaperone; EC; Isomerase; Membrane protein, integral; Mitochondrial
Chromosomal Location of Human Ortholog: 19p13.11
Cellular Component:  cytosol; endoplasmic reticulum; integral component of endoplasmic reticulum membrane; mitochondrial membrane; mitochondrion; protein-containing complex
Molecular Function:  disordered domain specific binding; identical protein binding; metal ion binding; peptidyl-prolyl cis-trans isomerase activity; protein binding
Biological Process:  apoptotic process; camera-type eye development; cell fate specification; dorsal/ventral neural tube patterning; intracellular signal transduction; multicellular organism growth; negative regulation of apoptotic process; negative regulation of protein phosphorylation; positive regulation of BMP signaling pathway; protein peptidyl-prolyl isomerization; smoothened signaling pathway; viral process
Reference #:  Q14318 (UniProtKB)
Alt. Names/Synonyms: 38 kDa FK506-binding protein; 38 kDa FKBP; FK506 binding protein 8, 38kDa; FK506-binding protein 8; FK506-binding protein 8 (38kD); FKBP prolyl isomerase 8; FKBP-38; FKBP-8; FKBP38; FKBP8; FKBPR38; hFKBP38; Peptidyl-prolyl cis-trans isomerase FKBP8; PPIase FKBP8; Rotamase
Gene Symbols: FKBP8
Molecular weight: 44,562 Da
Basal Isoelectric point: 4.78  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

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