DNAJC14 Gene - Function, Mutations, and Disease Associations | NCBI, UniProt, ClinVar

DNAJC14 encodes a member of the DnaJ/Hsp40 family of co-chaperones, characterized by a conserved J-domain that interacts with Hsp70 chaperones. The protein localizes to the endoplasmic reticulum (ER) membrane and functions in protein folding, quality control, and the unfolded protein response (UPR). It also plays a role in modulating viral replication, particularly for flaviviruses such as dengue and Zika virus, by interacting with viral nonstructural proteins. DNAJC14 is implicated in ER stress-related diseases, including cancer and neurodegenerative disorders.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Unfolded Protein Response (UPR) - REACTOME R-HSA-381119

• Endoplasmic Reticulum Stress Pathway - KEGG hsa04141

• Protein Processing in Endoplasmic Reticulum - KEGG hsa04141

DNAJC14 is a 504-amino acid protein with an N-terminal J-domain, a central glycine/phenylalanine-rich region, and a C-terminal domain that anchors it to the ER membrane. It acts as a co-chaperone for BiP (Hsp70) to facilitate protein folding and degradation of misfolded proteins. The protein also contains a thioredoxin-like domain, suggesting oxidoreductase activity. DNAJC14 is essential for ER homeostasis and is hijacked by flaviviruses to support their replication cycle.