AHSA1
Function
Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155).
Post-translational modifications
Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1.
Sequence Similarities
Belongs to the AHA1 family.
Tissue Specificity
Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta.
Cellular localization
- Cytoplasm
- Cytosol
- Endoplasmic reticulum
- May transiently interact with the endoplasmic reticulum.
Alternative names
C14orf3, HSPC322, AHSA1, Activator of 90 kDa heat shock protein ATPase homolog 1, AHA1, p38