DNAJB4: A Key Co-Chaperone in Protein Quality Control and Stress Response
Comprehensive genomic, functional, and clinical overview of DNAJB4 (Hsp40 family member)
Gene Information Card
| Symbol | DNAJB4 |
|---|---|
| Full Name | DnaJ heat shock protein family (Hsp40) member B4 |
| Gene Type | Protein coding |
| Chromosomal Location | 1p31.1 |
| NCBI Gene ID | 11080 ncbi.nlm.nih.gov/gene/11080 |
| Ensembl ID | ENSG00000162614 |
| UniProt ID | Q9UDY4 |
| OMIM ID | 611339 |
| HGNC ID | 14885 |
| Aliases | HSPF1, HLJ1, DNAJB4, DnaJ homolog subfamily B member 4 |
Description
DNAJB4 encodes a member of the DnaJ/Hsp40 family of co-chaperones. The protein contains a conserved J-domain that interacts with Hsp70 chaperones to regulate protein folding, degradation, and stress responses. DNAJB4 is involved in cellular processes including protein quality control, apoptosis, and tumor suppression. It is downregulated in several cancers and implicated in neurodegenerative diseases.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Cancer (lung, breast, colorectal) | Loss of DNAJB4 expression reduces Hsp70-mediated protein folding and promotes tumor growth | COSMIC, ClinVar, literature |
| Neurodegeneration (Alzheimer's, Parkinson's) | Impaired chaperone activity leads to protein aggregation | UniProt, literature |
| Heat shock response | DNAJB4 is induced by heat stress to protect cells from proteotoxicity | NCBI, UniProt |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Testis | 12.5 | Medium |
| Brain | 8.3 | Low |
| Liver | 6.7 | Low |
| Heart | 5.2 | Low |
| Lung | 4.1 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HEK293 | 15.2 | High expression |
| HeLa | 10.8 | Moderate expression |
| A549 | 7.5 | Low expression |
| MCF7 | 6.3 | Low expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.287A>G (p.Asn96Ser) | Missense | 0.01% (gnomAD) | Unknown functional impact |
| c.1A>G (p.Met1?) | Start loss | Rare | Likely loss of function |
| c.424C>T (p.Arg142*) | Nonsense | Rare | Loss of function |
Mutation functional classification
Loss of Function (LOF)
Nonsense and start-loss mutations are predicted to cause loss of DNAJB4 protein function, impairing chaperone activity.
Gain of Function (GOF)
No gain-of-function mutations reported in curated databases.
Dominant Negative (DN)
No dominant-negative mutations documented.
View complete mutation data：
Gene Ontology (GO)
| • protein folding (GO:0006457) | • Hsp70 protein binding (GO:0030544) |
| • unfolded protein binding (GO:0051082) | • response to heat (GO:0009408) |
| • protein refolding (GO:0042026) | • cytoplasm (GO:0005737) |
Pathways
• Protein processing in endoplasmic reticulum (KEGG: hsa04141)
• Heat shock response (Reactome: R-HSA-3371556)
• Chaperone-mediated protein folding (Reactome: R-HSA-390466)
Protein Summary
DNAJB4 is a 337-amino acid co-chaperone with a conserved J-domain at the N-terminus. It stimulates the ATPase activity of Hsp70 chaperones, facilitating proper protein folding and preventing aggregation. The protein is localized in the cytoplasm and is upregulated under heat shock. It plays a role in tumor suppression by promoting apoptosis and inhibiting metastasis.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| DNAJB4 Knockout HEK293 Cell Line | EDJ-KQ3663 | Human | 11080 | Details Get a Quote |
| DNAJB4 Knockout A-549 Cell Line | EDJ-KQ25640 | Human | 11080 | Details Get a Quote |
| DNAJB4 Knockout HCT 116 Cell Line | EDJ-KQ25641 | Human | 11080 | Details Get a Quote |
| DNAJB4 Knockout HeLa Cell Line | EDJ-KQ25642 | Human | 11080 | Details Get a Quote |
