Heat Shock Protein 90, Co-Chaperone P23 (HSP90AA1) Protein

The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]

HSP90A: a molecular chaperone of the heat shock protein 90 family. Has ATPase activity. Known to interact with a wide variety of proteins including steroid hormone receptors, neuropeptide Y, FKBP51/54, and FKBP52. G protein-coupled receptor kinases are stabilized by interacting with HSP 90. Hsp70 and Hsp90 promote tau solubility and tau binding to microtubules, reducing insoluble tau phosphorylation of tau.

Protein type: Heat shock protein; Chaperone

Chromosomal Location of Human Ortholog: 14q32.33

Cellular Component: nucleoplasm; mitochondrion; membrane; cytoplasm; extracellular region; plasma membrane; melanosome; nucleus; cytosol

Molecular Function: identical protein binding; protein binding; protein homodimerization activity; TPR domain binding; unfolded protein binding; nitric-oxide synthase regulator activity; ATPase activity; nucleotide binding; ATP binding

Biological Process: receptor-mediated endocytosis; axon guidance; positive regulation of nitric oxide biosynthetic process; organelle organization and biogenesis; signal transduction; nitric oxide metabolic process; protein import into mitochondrial outer membrane; response to unfolded protein; mitochondrial transport; innate immune response; protein refolding; regulation of nitric-oxide synthase activity; mitotic cell cycle; chaperone-mediated protein complex assembly; G2/M transition of mitotic cell cycle; vascular endothelial growth factor receptor signaling pathway