Acts as a co-chaperone of HSP90AA1 . Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity . Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins . Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins .
Subcellular locations: Cytoplasm, Cytosol, Endoplasmic reticulum
May transiently interact with the endoplasmic reticulum.
Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta.