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. There are 2 major cytosolic HSP90 proteins, HSP90AA1 ., an inducible form, and HSP90AB1, a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum and mitochondria.
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Protein Aliases: epididymis luminal secretory protein 52; epididymis secretory sperm binding protein Li 65p; Heat shock 86 kDa; heat shock 90kD protein 1, alpha; heat shock 90kD protein 1, alpha-like 4; heat shock 90kD protein, alpha-like 4; heat shock 90kDa protein 1, alpha; heat shock protein 1, alpha; heat shock protein 86; heat shock protein 90kDa alpha (cytosolic), class A member 1; heat shock protein 90kDa alpha family class A member 1; Heat shock protein HSP 90-alpha; HSP 86; LAP-2; Lipopolysaccharide-associated protein 2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38
Gene Aliases: EL52; HEL-S-65p; HSP86; Hsp89; HSP89A; Hsp90; HSP90A; HSP90AA1; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; LAP-2; LAP2