3.0
Summary
| Name |  FKBP8
|
| Full Name | Peptidyl-prolyl cis-trans isomerase FKBP8 |
| Synonyms | PPIase FKBP8, 38 kDa FK506-binding protein, 38 kDa FKBP, FKBP-38, hFKBP38, FK506-binding protein 8, FKBP-8, FKBPR38, Rotamase | FKBP38 |
| Primary ID | Q14318 |
| Links |  -  -  |
| Type | protein |
| Relations | 3 |
| 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. |
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Relations
| Regulator | Mechanism | target | score ℹ | |
|---|---|---|---|---|
| + | RHEB | down-regulates 
binding
|
FKBP8 | 0.552 |
| Publications: | 1 | Organism: | Homo Sapiens | |
| + | FKBP8 | down-regulates
binding
|
MTOR | 0.582 |
| Publications: | 1 | Organism: | Homo Sapiens | |
| + | RHEB | down-regulates activity
gtpase-activating protein
|
FKBP8 | 0.552 |
| Publications: | 1 | Organism: | Homo Sapiens | |