HSP90AB1 (Heat Shock Protein 90 Alpha Family Class B Member 1)
A constitutively expressed molecular chaperone essential for protein folding, stability, and cellular stress response; implicated in cancer and neurodegeneration.
Gene Information Card
| Symbol | HSP90AB1 |
|---|---|
| Full Name | Heat shock protein 90 alpha family class B member 1 |
| Gene Type | Protein coding |
| Chromosomal Location | 6p21.1 |
| NCBI Gene ID | 3326 ncbi.nlm.nih.gov/gene/3326 |
| Ensembl ID | ENSG00000096384 |
| UniProt ID | P08238 |
| OMIM ID | 140572 |
| HGNC ID | 5258 |
| Aliases | HSP90B, HSPC2, HSPCB, HSP90, HSP90-beta, 90kDa heat shock protein beta |
Description
HSP90AB1 encodes the beta isoform of the heat shock protein 90 (HSP90) family, a constitutively expressed molecular chaperone that facilitates the proper folding, stabilization, and maturation of client proteins involved in cell cycle control, signal transduction, and stress response. Unlike the stress-inducible alpha isoform (HSP90AA1), HSP90AB1 is constitutively expressed under normal conditions and plays a critical role in maintaining protein homeostasis. It functions as a homodimer and interacts with co-chaperones to regulate the activity of kinases, steroid hormone receptors, and transcription factors. HSP90AB1 is implicated in various cancers and neurodegenerative disorders, making it a target for therapeutic intervention.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Cancer (multiple types) | Overexpression of HSP90AB1 stabilizes oncogenic client proteins (e.g., HER2, EGFR, BCR-ABL), promoting tumor cell survival and proliferation. | High expression in tumor tissues; HSP90 inhibitors show antitumor activity in clinical trials. |
| Neurodegenerative diseases (e.g., Alzheimer's, Parkinson's) | HSP90AB1 modulates the aggregation and clearance of misfolded proteins (e.g., tau, alpha-synuclein), influencing disease progression. | Increased HSP90 levels in affected brain regions; inhibition reduces protein aggregation in models. |
| Viral infections | HSP90AB1 is hijacked by viruses to stabilize viral proteins and facilitate replication. | Interaction with viral proteins (e.g., influenza, hepatitis B) demonstrated in vitro. |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Brain | 18.2 | High |
| Heart | 15.7 | High |
| Liver | 12.3 | Medium |
| Kidney | 11.8 | Medium |
| Lung | 10.5 | Medium |
| Testis | 9.4 | Medium |
| Skeletal Muscle | 8.1 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa (cervical cancer) | 25.3 | High expression; used in HSP90 studies |
| A549 (lung cancer) | 22.1 | High expression; associated with drug resistance |
| MCF7 (breast cancer) | 20.8 | High expression; supports estrogen receptor signaling |
| HEK293 (embryonic kidney) | 18.5 | Moderate expression; common for recombinant protein production |
| K562 (leukemia) | 16.2 | Moderate expression; BCR-ABL stabilization |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1124A>G (p.Asn375Ser) | Missense | Rare (<0.1%) | Alters ATP-binding affinity; reduced chaperone activity in vitro. |
| c.1483C>T (p.Arg495Cys) | Missense | Rare (<0.1%) | Impairs client protein interaction; potential loss-of-function. |
| c.1873G>A (p.Val625Met) | Missense | Rare (<0.1%) | Unknown functional effect; reported in cancer samples. |
Mutation functional classification
Loss of Function (LOF)
Mutations that reduce ATP binding or disrupt co-chaperone interaction lead to impaired chaperone activity, affecting client protein folding and stability.
Gain of Function (GOF)
No clear gain-of-function mutations reported; overexpression is more common in disease.
Dominant Negative (DN)
Some mutations may act dominant-negative by forming inactive heterodimers with wild-type HSP90, reducing overall chaperone function.
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 | • protein stabilization |
Pathways
• HSP90 chaperone cycle
• PI3K-Akt signaling pathway
• MAPK signaling pathway
• Estrogen signaling pathway
• Proteasome-mediated ubiquitin-dependent protein catabolic process
• Cellular response to stress
Protein Summary
HSP90AB1 encodes a 724-amino acid protein (molecular weight ~83 kDa) that functions as a homodimer. Each monomer consists of an N-terminal ATP-binding domain, a middle domain, and a C-terminal dimerization domain. The protein undergoes ATP-dependent conformational changes that facilitate client protein maturation. It interacts with co-chaperones such as HOP, CDC37, and p23 to regulate the folding of kinases, steroid receptors, and transcription factors. Post-translational modifications include phosphorylation and acetylation, which modulate its activity. HSP90AB1 is ubiquitously expressed and essential for cell viability under stress conditions.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| HSP90AB1 Knockout HEK293 Cell Line | EDJ-KQ201 | Human | 3326 | Details Get a Quote |
| HSP90AB1 Knockout A-549 Cell Line | EDJ-KQ22308 | Human | 3326 | Details Get a Quote |
| HSP90AB1 Knockout HCT 116 Cell Line | EDJ-KQ22309 | Human | 3326 | Details Get a Quote |
| HSP90AB1 Knockout HeLa Cell Line | EDJ-KQ22310 | Human | 3326 | Details Get a Quote |
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