HSPB1 (Heat Shock Protein Family B (Small) Member 1)
A small heat shock protein involved in stress response, cytoskeletal stability, and neuroprotection; mutations cause Charcot-Marie-Tooth disease type 2F and distal hereditary motor neuropathy.
Gene Information Card
| Symbol | HSPB1 |
|---|---|
| Full Name | Heat Shock Protein Family B (Small) Member 1 |
| Gene Type | Protein coding |
| Chromosomal Location | 7q11.23 |
| NCBI Gene ID | 3315 ncbi.nlm.nih.gov/gene/3315 |
| Ensembl ID | ENSG00000106211 |
| UniProt ID | P04792 |
| OMIM ID | 602195 |
| HGNC ID | 5246 |
| Aliases | HSP27, HSP28, Hsp25, CMT2F, DKFZp686P2033 |
Description
HSPB1 encodes a small heat shock protein (sHSP) of 27 kDa (HSP27) that functions as a molecular chaperone, protecting cells from stress-induced protein aggregation. It regulates actin dynamics, inhibits apoptosis, and modulates oxidative stress. Mutations in HSPB1 cause Charcot-Marie-Tooth disease type 2F (CMT2F) and distal hereditary motor neuropathy (dHMN).
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Charcot-Marie-Tooth disease type 2F | Missense mutations impair chaperone function and cause axonal degeneration | ClinVar, OMIM |
| Distal hereditary motor neuropathy | Dominant mutations disrupt neurofilament assembly and axonal transport | ClinVar, OMIM |
| Peripheral neuropathy | Gain-of-function mutations lead to protein aggregation and neuronal toxicity | ClinVar |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Skeletal muscle | 62.3 | High |
| Heart | 45.1 | High |
| Brain | 12.8 | Medium |
| Liver | 8.5 | Low |
| Kidney | 6.2 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | 35.4 | Ubiquitous expression |
| HEK293 | 28.7 | Moderate expression |
| SH-SY5Y | 18.9 | Neuronal cell line |
| MCF7 | 22.1 | Breast cancer cell line |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.379C>T (p.Arg127Trp) | Missense | Rare | Dominant; causes CMT2F |
| c.404C>T (p.Ser135Phe) | Missense | Rare | Dominant; causes dHMN |
| c.451C>T (p.Arg151Cys) | Missense | Rare | Dominant; causes CMT2F |
| c.545G>A (p.Arg182Gly) | Missense | Rare | Dominant; causes CMT2F |
Mutation functional classification
Loss of Function (LOF)
Not clearly established; most mutations are dominant negative or gain-of-function.
Gain of Function (GOF)
Mutations (e.g., p.Arg127Trp, p.Ser135Phe) increase aggregation propensity and impair neurofilament assembly.
Dominant Negative (DN)
Mutant HSP27 interferes with wild-type chaperone activity, reducing cytoprotection.
View complete mutation data：
Gene Ontology (GO)
Pathways
• Cellular response to heat stress (R-HSA-3371556)
• Chaperone-mediated protein folding (R-HSA-390466)
• Apoptosis regulation (R-HSA-109581)
Protein Summary
HSP27 is a 205-amino-acid small heat shock protein that forms large oligomers. It acts as an ATP-independent chaperone, preventing protein aggregation under stress. It also stabilizes actin filaments, inhibits caspase activation, and modulates the cellular redox state. Phosphorylation at Ser15, Ser78, and Ser82 regulates its oligomerization and function.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| HSPB1 Knockout HEK293 Cell Line | EDJ-KQ674 | Human | 3315 | Details Get a Quote |
| HSPB1 Knockout A-549 Cell Line | EDJ-KQ19206 | Human | 3315 | Details Get a Quote |
| HSPB1 Knockout HCT 116 Cell Line | EDJ-KQ19207 | Human | 3315 | Details Get a Quote |
| HSPB1 Knockout HeLa Cell Line | EDJ-KQ19208 | Human | 3315 | Details Get a Quote |
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