DnaJ homolog subfamily B member 11; APOBEC1-binding protein 2; ABBP-2; DnaJ protein homolog 9; ER-associated DNAJ; ER-associated Hsp40 co-chaperone; ER-associated dnaJ protein 3; ERdj3; ERj3p; HEDJ; Human DnaJ protein 9; hDj-9; PWP1-interacting protein 4 (DNAJB11, EDJ, ERJ3, HDJ9, PSEC0121, UNQ537/PRO1080)
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Function
- co-chaperone for HSPA5
- binds directly to both unfolded proteins that are substrates for ERAD & nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed
- may help recruiting HSPA5 & other chaperones to the substrate
- stimulates HSPA5 ATPase activity
- Thr-188 was reported to be phosphorylated upon DNA damage by ATM or ATR[2]; however as this position is in the ER lumen, & the in vivo relevance is unknown
- part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 & very small amounts of ERP29, but not, or at very low levels, CALR nor CANX
- binds to denatured substrates (ATP-independent)
- interacts via the J domain with HSPA5 (ATP-dependent)
Structure
- contains high-mannose endo H-sensitive carbohydrates
- Cys-169, Cys-171, Cys-193 & Cys-196 form intramolecular disulfide bonds
- the preferential partner for each Cys is not known
- contains 1 J domain
Compartment
- endoplasmic reticulum lumen
- associated with the ER membrane in a C-terminally epitope-tagged construct
Expression
- widely expressed
- induced by ER stress-inducing agents such as thapsigargin & tunicamycin