HSPB3 Gene - Small Heat Shock Protein B3
A member of the HSP20 family involved in muscle development and neuropathy
Gene Information Card
| Symbol | HSPB3 |
|---|---|
| Full Name | Heat Shock Protein Family B (Small) Member 3 |
| Gene Type | Protein coding |
| Chromosomal Location | 5q11.2 |
| NCBI Gene ID | 8988 ncbi.nlm.nih.gov/gene/8988 |
| Ensembl ID | ENSG00000169271 |
| UniProt ID | Q12988 |
| OMIM ID | 604624 |
| HGNC ID | 5248 |
| Aliases | HSP27, HSPL27, HMN2C, CMT2F |
Description
HSPB3 encodes a member of the small heat shock protein (sHSP) family, specifically the HSP20 subfamily. The protein acts as a molecular chaperone, protecting cells from stress-induced protein aggregation. It is predominantly expressed in skeletal muscle and heart, and plays a role in muscle fiber maintenance and peripheral nerve function. Mutations in HSPB3 are associated with Charcot-Marie-Tooth disease type 2F (CMT2F) and distal hereditary motor neuropathy type 2C (dHMN2C).
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Charcot-Marie-Tooth disease type 2F (CMT2F) | Missense mutations impair chaperone function, leading to axonal degeneration | ClinVar, OMIM |
| Distal hereditary motor neuropathy type 2C (dHMN2C) | Dominant-negative effect on protein stability and aggregation | OMIM, PubMed |
| Distal myopathy | Reduced chaperone activity causes protein aggregation in muscle | UniProt, literature |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Skeletal muscle | 12.5 | Medium |
| Heart | 8.2 | Medium |
| Brain | 1.3 | Low |
| Liver | 0.5 | Not detected |
| Kidney | 0.8 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | 2.1 | Low expression |
| HEK293 | 1.5 | Low expression |
| Skeletal muscle myoblasts | 15.0 | High expression |
| Cardiomyocytes | 9.8 | Medium expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.423G>A (p.Arg141His) | Missense | Rare | Dominant-negative; associated with CMT2F |
| c.404C>T (p.Pro135Leu) | Missense | Rare | Impaired chaperone activity; dHMN2C |
| c.451G>A (p.Gly151Ser) | Missense | Rare | Reduced solubility; neuropathy |
Mutation functional classification
Loss of Function (LOF)
Not clearly established; most mutations are dominant-negative.
Gain of Function (GOF)
Not reported.
Dominant Negative (DN)
p.Arg141His and p.Pro135Leu act via dominant-negative mechanism, disrupting oligomerization and chaperone function.
View complete mutation data：
Gene Ontology (GO)
| • structural constituent of eye lens (GO:0005212) | • protein folding (GO:0006457) |
| • response to heat (GO:0009408) | • cellular response to heat (GO:0034605) |
| • unfolded protein binding (GO:0051082) | • cytoplasm (GO:0005737) |
Pathways
• Cellular response to heat stress (Reactome: R-HSA-3371556)
• Chaperone-mediated protein folding (Reactome: R-HSA-390466)
Protein Summary
HSPB3 is a 150-amino-acid small heat shock protein (17 kDa) that forms oligomeric complexes. It functions as a molecular chaperone, preventing aggregation of denatured proteins under stress conditions. The protein contains a conserved alpha-crystallin domain and is highly expressed in muscle tissues. Mutations in HSPB3 disrupt its chaperone activity and oligomerization, leading to peripheral neuropathy and myopathy.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| HSPB3 Knockout HEK293 Cell Line | EDJ-KQ5744 | Human | 8988 | Details Get a Quote |
| HSPB3 Knockout HeLa Cell Line | EDJ-KQ55049 | Human | 8988 | Details Get a Quote |
| HSPB3 Knockout A-549 Cell Line | EDJ-KQ63532 | Human | 8988 | Details Get a Quote |
| HSPB3 Knockout HCT 116 Cell Line | EDJ-KQ72000 | Human | 8988 | Details Get a Quote |
