HSP90B: 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.
Protein type: Chaperone; Heat shock protein
Chromosomal Location of Human Ortholog: 6p12
Cellular Component: signalosome; nucleoplasm; cell surface; membrane; mitochondrion; basolateral plasma membrane; brush border membrane; apical plasma membrane; cytoplasm; melanosome; inclusion body; cytosol
Molecular Function: protein binding; GTP binding; TPR domain binding; unfolded protein binding; nitric-oxide synthase regulator activity; double-stranded RNA binding; dATP binding; sulfonylurea receptor binding; protein kinase binding; kinase binding; ATP binding
Biological Process: axon guidance; positive regulation of nitric oxide biosynthetic process; positive regulation of protein import into nucleus, translocation; positive regulation of protein binding; protein folding; positive regulation of cell size; innate immune response; negative regulation of neuron apoptosis; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; response to salt stress; response to unfolded protein; placenta development
Show more