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. Homodimer. Interacts with p53/TP53. Forms a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1 and DNAJC7. Interacts with FKBP4. Belongs to the heat shock protein 90 family. Note: This description may include information from UniProtKB.
Molecular Function: ATP binding; ATP-dependent protein binding; cadherin binding; double-stranded RNA binding; heat shock protein binding; histone deacetylase binding; kinase binding; nitric-oxide synthase regulator activity; peptide binding; protein binding; protein dimerization activity; protein homodimerization activity; RNA binding; TPR domain binding
Biological Process: chaperone-mediated protein complex assembly; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; neutrophil degranulation; positive regulation of cell differentiation; positive regulation of nitric oxide biosynthetic process; positive regulation of phosphoprotein phosphatase activity; positive regulation of telomerase activity; positive regulation of transforming growth factor beta receptor signaling pathway; protein stabilization; regulation of protein ubiquitination; telomere maintenance via telomerase; virion attachment to host cell surface receptor; xenobiotic metabolic process