HSP90A a molecular chaperone of the heat shock protein 90 family that promotes the maturation, structural maintenance and proper regulation of specific target proteins. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. 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. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein
Cellular Component: 
Reference #:  P46633 (UniProtKB)
Alt. Names/Synonyms: Heat shock protein HSP 90-alpha; HS90A; HS9A; HSP 86; HSP90A; HSPCA
Gene Symbols: Hsp90aa1
Molecular weight: 84,849 Da
Basal Isoelectric point: 4.96  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Inhibition of Apoptosis
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

Cross-references to other databases:  STRING  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept