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
Chromosomal Location of mouse Ortholog: 12 F1|12 60.75 cM
Cellular Component:  apical plasma membrane; axonal growth cone; basolateral plasma membrane; brush border membrane; cell surface; collagen-containing extracellular matrix; cytoplasm; cytosol; dendritic growth cone; intracellular anatomical structure; membrane; mitochondrion; myelin sheath; neuronal cell body; nucleoplasm; nucleus; perinuclear region of cytoplasm; plasma membrane; protein-containing complex; sperm flagellum; sperm mitochondrial sheath; sperm plasma membrane
Molecular Function:  ATP binding; ATP hydrolysis activity; ATP-dependent protein folding chaperone; CTP binding; dATP binding; disordered domain specific binding; DNA polymerase binding; GTP binding; GTPase binding; histone deacetylase binding; hydrolase activity; identical protein binding; mRNA binding; nitric-oxide synthase regulator activity; nucleotide binding; protein binding; protein folding chaperone; protein homodimerization activity; protein phosphatase binding; protein tyrosine kinase binding; Rho GDP-dissociation inhibitor binding; scaffold protein binding; sulfonylurea receptor binding; tau protein binding; TPR domain binding; transmembrane transporter binding; ubiquitin protein ligase binding; unfolded protein binding; UTP binding
Biological Process:  activation of innate immune response; axon extension; cellular response to heat; cellular response to virus; central nervous system neuron axonogenesis; chaperone-mediated protein complex assembly; establishment of cell polarity; neuron migration; nitric oxide biosynthetic process; positive regulation of cell size; positive regulation of cytotoxic T cell differentiation; positive regulation of defense response to virus by host; positive regulation of interferon-beta production; positive regulation of lamellipodium assembly; positive regulation of nitric oxide biosynthetic process; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein catabolic process; positive regulation of protein import into nucleus; positive regulation of protein kinase B signaling; positive regulation of protein phosphorylation; positive regulation of protein polymerization; positive regulation of tau-protein kinase activity; positive regulation of telomerase activity; protein folding; protein insertion into mitochondrial outer membrane; protein refolding; protein stabilization; regulation of apoptotic process; regulation of postsynaptic membrane neurotransmitter receptor levels; regulation of protein localization; regulation of protein ubiquitination; response to unfolded protein; telomerase holoenzyme complex assembly; telomere maintenance via telomerase
Reference #:  P07901 (UniProtKB)
Alt. Names/Synonyms: 86kDa; 89kDa; AL024080; AL024147; Heat shock 86 kDa; heat shock protein 1, alpha; heat shock protein 90, alpha (cytosolic), class A member 1; heat shock protein 90kDa alpha (cytosolic), class A member 1; Heat shock protein HSP 90-alpha; heat shock protein, 1; heat shock protein, 86 kDa 1; heat shock protein, 89 kDa; HS90A; Hsp; HSP 86; hsp4; HSP86; Hsp86-1; Hsp89; Hsp90; HSP90A; Hsp90aa1; Hspca; OTTMUSP00000021333; OTTMUSP00000021334; TSTA; Tumor-specific transplantation 86 kDa antigen
Gene Symbols: Hsp90aa1
Molecular weight: 84,788 Da
Basal Isoelectric point: 4.93  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:  AlphaFold  |  STRING  |  Reactome  |  BioGPS  |  Pfam  |  RCSB PDB  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein