HSPB7: Small Heat Shock Protein B7
Cardiovascular and muscular small heat shock protein with chaperone activity
Gene Information Card
| Symbol | HSPB7 |
|---|---|
| Full Name | Heat Shock Protein Family B (Small) Member 7 |
| Gene Type | Protein coding |
| Chromosomal Location | 1p36.13 |
| NCBI Gene ID | 27129 ncbi.nlm.nih.gov/gene/27129 |
| Ensembl ID | ENSG00000173641 |
| UniProt ID | Q9UBY9 |
| OMIM ID | 610212 |
| HGNC ID | 5249 |
| Aliases | cvHsp, HSP27-3, FLJ32733 |
Description
HSPB7 encodes a member of the small heat shock protein family (sHSP). The protein functions as a molecular chaperone, protecting cells from stress-induced protein aggregation. It is highly expressed in cardiac and skeletal muscle and plays a critical role in maintaining sarcomere integrity and cardiac function. Mutations in HSPB7 are associated with dilated cardiomyopathy and myofibrillar myopathy.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Dilated cardiomyopathy | Impaired chaperone activity leads to protein aggregation and sarcomere dysfunction | ClinVar, OMIM #610212 |
| Myofibrillar myopathy | Loss of chaperone function causes desmin aggregation and myofibril disorganization | ClinVar, OMIM #610212 |
| Heart failure | Reduced HSPB7 expression correlates with cardiac remodeling | NCBI Gene, PubMed |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Heart | 58.2 | High |
| Skeletal muscle | 42.1 | High |
| Liver | 1.3 | Low |
| Brain | 0.8 | Low |
| Kidney | 2.1 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| Cardiomyocytes (AC16) | 62.5 | High expression |
| Skeletal muscle myoblasts (HSMM) | 45.0 | High expression |
| HeLa | 3.2 | Low expression |
| HEK293 | 2.8 | Low expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.423C>G (p.Cys141Trp) | Missense | Rare | Impaired chaperone activity; associated with dilated cardiomyopathy |
| c.311G>A (p.Arg104His) | Missense | Rare | Reduced protein stability; linked to myofibrillar myopathy |
| c.1A>G (p.Met1Val) | Start loss | Very rare | Loss of protein expression; pathogenic in cardiomyopathy |
Mutation functional classification
Loss of Function (LOF)
Missense mutations (e.g., Cys141Trp) reduce chaperone activity and promote protein aggregation.
Gain of Function (GOF)
Not reported for HSPB7.
Dominant Negative (DN)
Mutant HSPB7 may interfere with wild-type chaperone function in heterozygous state.
View complete mutation data：
Gene Ontology (GO)
Pathways
• Cellular response to heat stress (Reactome: R-HSA-3371556)
• Chaperone-mediated protein folding (Reactome: R-HSA-390466)
• Protein processing in endoplasmic reticulum (KEGG: hsa04141)
Protein Summary
HSPB7 (cvHsp) is a 170-amino-acid small heat shock protein with a conserved alpha-crystallin domain. It forms oligomeric complexes and functions as an ATP-independent chaperone, preventing aggregation of denatured proteins. It is predominantly expressed in cardiac and skeletal muscle, where it localizes to the Z-disc and intercalated discs. Post-translational modifications include phosphorylation, which modulates its chaperone activity and subcellular localization.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| HSPB7 Knockout HEK293 Cell Line | EDJ-KQ8687 | Human | 27129 | Details Get a Quote |
| HSPB7 Knockout HeLa Cell Line | EDJ-KQ56009 | Human | 27129 | Details Get a Quote |
| HSPB7 Knockout A-549 Cell Line | EDJ-KQ64497 | Human | 27129 | Details Get a Quote |
| HSPB7 Knockout HCT 116 Cell Line | EDJ-KQ72954 | Human | 27129 | Details Get a Quote |
