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The protein encoded by FKBP7 belongs to the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family.
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observed changes in activity of six rER-resident PPIases, cyclophilin B (show PPIB Proteins) (encoded by the PPIB (show PPIB Proteins) gene), FKBP13 (FKBP2 (show FKBP2 Proteins)), FKBP19 (FKBP11 (show FKBP11 Proteins)), FKBP22 (FKBP14 (show FKBP14 Proteins)), FKBP23 (FKBP7), and FKBP65 (FKBP10 (show FKBP10 Proteins)), due to posttranslational modifications of proline residues in the substrate.
RUNX1 (show RUNX1 Proteins) and FKBP7, involved in erythropoesis and muscle protein synthesis, respectively, are related to change in cardiorespiratory fitness in response to exercise.
FKBP23 is demonstrated to mediate functions of BiP (show HSPA5 Proteins) by catalyzing the Pro(117)cis (show CISH Proteins)/trans conformational interconversion in the ATPase domain of BiP (show HSPA5 Proteins).
mFKBP23 binds to immunoglobulin binding protein (mBiP (show MBIP Proteins),Hsp70 (show HSP70 Proteins)); the binding of the C-terminus is Ca(2 (show CA2 Proteins)+)-dependent and the switch point is between 2 and 3 mM, no binding being detected at high concentration of calcium
In this study, we demonstrate the ability of mFKBP23 to modulate the ATPase activity of BiP (show HSPA5 Proteins), and that the bound mFKBP23, but not the free mFKBP23, can suppress the ATPase activity of mBiP (show MBIP Proteins) through its PPIase (show NKTR Proteins) activity.
binds to Grp78 (Bip (show HSPA5 Proteins)) in endoplasmic reticulum.
The protein encoded by this gene belongs to the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. Members of this family exhibit PPIase activity and function as molecular chaperones. A similar protein in mouse is located in the endoplasmic reticulum and binds calcium.
, peptidyl-prolyl cis-trans isomerase FKBP7
, FK506-binding protein 7
, FK506 binding protein 7
, FK506 binding protein 23
, PPIase FKBP7
, 23 kDa FK506-binding protein
, 23 kDa FKBP
, FK506-binding protein 23