ID:FKBP8_HUMAN DESCRIPTION: RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP8; Short=PPIase FKBP8; EC=5.2.1.8; AltName: Full=38 kDa FK506-binding protein; Short=38 kDa FKBP; Short=FKBP-38; Short=hFKBP38; AltName: Full=FK506-binding protein 8; Short=FKBP-8; AltName: Full=FKBPR38; AltName: Full=Rotamase; 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. CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0). COFACTOR: Calcium. SUBUNIT: 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. INTERACTION: P00533:EGFR; NbExp=3; IntAct=EBI-724839, EBI-297353; Q5T4F4:ZFYVE27; NbExp=4; IntAct=EBI-724839, EBI-3892947; SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein; Cytoplasmic side (By similarity). TISSUE SPECIFICITY: Widely expressed. Highest levels seen in the brain. MISCELLANEOUS: Binds the immunosuppressant FK506 only in its calmodulin/calcium activated form. SIMILARITY: Contains 1 PPIase FKBP-type domain. SIMILARITY: Contains 3 TPR repeats. CAUTION: It is uncertain whether Met-1 or Met-58 is the initiator. SEQUENCE CAUTION: Sequence=AAB00102.1; Type=Miscellaneous discrepancy; Note=The first part of the cDNA maps to the same locus, but in opposite orientation; Sequence=AAH09966.1; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=CAD98028.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q14318
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.