HSP90AA1 (HSP90 Alpha Family Class A Member 1)
A molecular chaperone essential for protein folding, stability, and cellular stress response, implicated in cancer and neurodegenerative disorders.
Gene Information Card
| Symbol | HSP90AA1 |
|---|---|
| Full Name | Heat shock protein 90 alpha family class A member 1 |
| Gene Type | protein-coding |
| Chromosomal Location | 14q32.31 |
| NCBI Gene ID | 3320 ncbi.nlm.nih.gov/gene/3320 |
| Ensembl ID | ENSG00000080824 |
| UniProt ID | P07900 |
| OMIM ID | 140571 |
| HGNC ID | 5253 |
| Aliases | HSP90A, HSPC1, HSPCA, HSPCAL1, HSP90N, EL52, HEL-S-65p |
Description
HSP90AA1 encodes a member of the heat shock protein 90 family, a highly conserved molecular chaperone that facilitates proper folding, stabilization, and function of numerous client proteins involved in cell cycle control, signal transduction, and stress response. It is constitutively expressed and induced by environmental stress. HSP90AA1 plays a critical role in maintaining cellular homeostasis and is implicated in cancer progression and neurodegeneration.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Cancer (multiple types) | HSP90AA1 overexpression stabilizes oncogenic client proteins (e.g., HER2, EGFR, BCR-ABL), promoting tumor cell survival and proliferation. | COSMIC; multiple studies |
| Neurodegenerative disorders (e.g., Alzheimer's, Parkinson's) | HSP90AA1 modulates the aggregation and clearance of misfolded proteins (e.g., tau, alpha-synuclein), influencing disease progression. | UniProt; literature |
| Infectious diseases (e.g., viral infections) | HSP90AA1 is hijacked by viruses for replication and assembly; inhibition can reduce viral load. | UniProt; literature |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Brain | High | High expression in cerebral cortex and cerebellum |
| Heart | Moderate | Moderate expression in cardiac muscle |
| Liver | High | High expression in hepatocytes |
| Kidney | Moderate | Moderate expression in renal tubules |
| Testis | High | High expression in spermatocytes |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | High | Cervical cancer cell line; high HSP90AA1 expression |
| MCF7 | High | Breast cancer cell line; high expression |
| A549 | Moderate | Lung cancer cell line; moderate expression |
| HEK293 | High | Embryonic kidney cells; high expression |
| K562 | Moderate | Chronic myeloid leukemia; moderate expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.184G>A (p.Asp62Asn) | Missense | Rare | May affect ATPase activity; clinical significance uncertain |
| c.719A>G (p.Asn240Ser) | Missense | Rare | Potential impact on chaperone function; not well characterized |
| c.1102C>T (p.Arg368Cys) | Missense | Rare | Reported in cancer; functional impact unknown |
| c.1505A>G (p.Glu502Gly) | Missense | Rare | Observed in population databases; no disease association confirmed |
Mutation functional classification
Loss of Function (LOF)
Complete loss-of-function mutations are rare and likely lethal due to essential chaperone activity; partial loss may impair protein folding and stress response.
Gain of Function (GOF)
Gain-of-function mutations are not well documented; overexpression is more common in cancer rather than activating mutations.
Dominant Negative (DN)
Dominant-negative mutations have been suggested in some studies, potentially interfering with dimerization and chaperone function, but evidence is limited.
View complete mutation data：
Gene Ontology (GO)
| • ATP binding | • ATP hydrolysis activity |
| • chaperone binding | • protein folding |
| • response to heat | • cellular response to unfolded protein |
| • signal transduction | • regulation of cell cycle |
Pathways
• PI3K-Akt signaling pathway
• MAPK signaling pathway
• Estrogen signaling pathway
• Proteasome-mediated ubiquitin-dependent protein catabolic process
• Chaperone-mediated autophagy
• HSP90 chaperone cycle for steroid hormone receptors (e.g.
• glucocorticoid receptor)
Protein Summary
The HSP90AA1 protein is a homodimeric molecular chaperone with ATPase activity. It associates with co-chaperones (e.g., HOP, p23, CDC37) to facilitate client protein maturation. It is essential for the stability and function of many kinases, transcription factors, and steroid hormone receptors. Post-translational modifications include phosphorylation and acetylation, which regulate its activity. HSP90AA1 is a target for cancer therapy; inhibitors like geldanamycin and 17-AAG are under investigation.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| HSP90AA1 Knockout HEK293 Cell Line | EDJ-KQ200 | Human | 3320 | Details Get a Quote |
| HSP90AA1 Knockout A-549 Cell Line | EDJ-KQ19537 | Human | 3320 | Details Get a Quote |
| HSP90AA1 Knockout HCT 116 Cell Line | EDJ-KQ19538 | Human | 3320 | Details Get a Quote |
| HSP90AA1 Knockout HeLa Cell Line | EDJ-KQ19539 | Human | 3320 | Details Get a Quote |
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