DnaJ heat shock protein family member B11 (DNAJB11)

DnaJ heat shock protein family member B11 (DNAJB11, also known as ERdj3) is a soluble glycoprotein localized in the lumen of the endoplasmic reticulum (ER), where it acts as an Hsp40 family co-chaperone[4]. It contains a conserved J-domain and coordinates proteostasis by binding misfolded secretory proteins in the ER and delivering them to the Hsp70 chaperone BiP for ATP-dependent folding or degradation[1][2][3][4]. DNAJB11 typically assembles as a tetramer, unlike most Hsp40 co-chaperones, a property that is important for its function in substrate binding and interaction with BiP[2][3]. Its activities also include regulating the ER stress response, ensuring proper assembly of secretory proteins (such as immunoglobulin chains, epithelial sodium channel, and glucocerebrosidase), and participating in protein translocation via interaction with Sec61[1][2]. As a central player in ER protein quality control, dysregulation of DNAJB11 may contribute to diseases associated with protein aggregation or defective secretion[2]. Its status as a therapeutic target is primarily due to its essential role in proteostasis rather than as a direct drug target; currently, no drugs targeting DNAJB11 are described in publicly available data[4].

Other names

DnaJ homolog subfamily B member 11EDJERJ3HDJ9PSEC0121UNQ537/PRO1080ABBP-2ERdj3ERj3phDj-9HEDJAPOBEC1-binding protein 2DnaJ protein homolog 9ER-associated DNAJER-associated Hsp40 co-chaperoneEndoplasmic reticulum DNA J domain-containing protein 3Human DnaJ protein 9PWP1-interacting protein 4ABBP2DJ9PKD6PRO1080