FunctionServes as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity.
Tissue specificityWidely expressed.
Sequence similaritiesContains 1 J domain.
Post-translational modificationsContains high-mannose Endo H-sensitive carbohydrates. Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular disulfide bonds. The preferential partner for each Cys is not known. Thr-188 was reported (PubMed:17525332) to be phosphorylated upon DNA damage by ATM or ATR; however as this position has been shown to be in the ER lumen, the in vivo relevance is not proven.
Cellular localizationEndoplasmic reticulum lumen. Associated with the ER membrane in a C-terminally epitope-tagged construct.
DnaJ (Hsp40) homolog subfamily B member 11 antibody
DnaJ homolog subfamily B member 11 antibody
DnaJ protein homolog 9 antibody
ER associated DNAJ antibody
ER associated dnaJ protein 3 antibody
ER associated Hsp40 co chaperone antibody
ER-associated DNAJ antibody
ER-associated dnaJ protein 3 antibody
ER-associated Hsp40 co-chaperone antibody
Human DnaJ protein 9 antibody
PWP1 interacting protein 4 antibody
PWP1-interacting protein 4 antibody
Anti-DNAJB11 antibody images
Western blot - DNAJB11 antibody (ab75107)
All lanes : Anti-DNAJB11 antibody (ab75107) at 1/500 dilution
Lane 1 : extracts from HeLa cells Lane 2 : extracts from HUVEC
cells Lane 3 : extracts from COLO cells Lane 4 : extracts from MCF-7 cells Lane 5 : extracts from HeLa cells with immunising peptide at 10 µg
Lysates/proteins at 30 µg per lane.
Predicted band size : 40 kDa Observed band size : 40 kDa