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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.
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| Protein type: Chaperone; EC 5.2.1.8; Isomerase; Membrane protein, integral; Mitochondrial |
| Chromosomal Location of Human Ortholog: 19p13.11 |
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Cellular Component:
cytosol; endoplasmic reticulum; integral component of endoplasmic reticulum membrane; mitochondrial membrane; mitochondrion; protein-containing complex
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Molecular Function:
disordered domain specific binding; identical protein binding; metal ion binding; peptidyl-prolyl cis-trans isomerase activity; protein binding
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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
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Reference #:
Q14318
(UniProtKB)
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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
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Gene Symbols: FKBP8
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Molecular weight:
44,562 Da
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Basal Isoelectric point:
4.78
Predict pI for various phosphorylation states
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