Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.
Belongs to the heat shock protein 90 family.
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.
ISGylated. S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.
Cytoplasm. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.