- Table of Content
Acts as a co-chaperone of HSP90AA1 (PubMed:29127155).Activates the ATPase activity of HSP90AA1 resulting in increase in its chaperone activity (PubMed:29127155).
Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a mutual regulatory mechanism for chaperoning of client proteins (PubMed:27353360). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a mutual regulatory mechanism for chaperoning of client proteins (PubMed:29127155).
|Sequence:||14; NC_000014.9 (77457867..77469472)|
Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta.
Cytoplasm, cytosol. Endoplasmic reticulum. May transiently interact with the endoplasmic reticulum.