Heat Shock Protein 90kDa Alpha A2 (HSP90aA2)

HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress.

HSP90AA2 is a cytosolic HSP90 protein. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1) and mitochondria (TRAP1) . Like other HSP90 proteins, the 757-amino acid HSP90AA2 protein has a highly conserved N-terminal domain, a charged domain, a middle domain involved in ATPase activity, a second charged domain, and a C-terminal domain. It also has a 4-helical cytokine motif and a gln-rich region.