MGP Database

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MGP005239

UniProt Annotations

Entry Information
Gene NameDnaJ (Hsp40) homolog, subfamily B, member 11
Protein EntryDJB11_HUMAN
UniProt IDQ9UBS4
SpeciesHuman
Comments
Comment typeDescription
CautionPubMed:11584023 reported a cytosolic, as well as nuclear subcellular location. This result was obtained using an N- terminally GFP-tagged construct which most probably affected signal peptide-driven targeting to the ER. As a consequence, the in vivo revelance of the observed interaction with APOBEC1, a nuclear protein, is dubious. This holds true for the interaction with PWP1. {ECO:0000305}.
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. {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15525676}.
InductionBy endoplasmic reticulum stress-inducing agents such as thapsigargin and tunicamycin. {ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:15544163}.
InteractionP11021:HSPA5; NbExp=2; IntAct=EBI-713113, EBI-354921;
PtmContains high-mannose Endo H-sensitive carbohydrates.
PtmCys-169, Cys-171, Cys-193 and Cys-196 form intramolecular disulfide bonds. The preferential partner for each Cys is not known.
PtmThr-188 was reported 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. {ECO:0000269|PubMed:17525332}.
SimilarityContains 1 J domain. {ECO:0000255|PROSITE- ProRule:PRU00286}.
Subcellular LocationEndoplasmic reticulum lumen {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15195998, ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:15544163}. Note=Associated with the ER membrane in a C-terminally epitope- tagged construct.
SubunitPart of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Binds to denatured substrates in an ATP- independent manner. Interacts via the J domain with HSPA5 in an ATP-dependent manner. {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:15525676, ECO:0000269|PubMed:17976514}.
Tissue SpecificityWidely expressed. {ECO:0000269|PubMed:10827079, ECO:0000269|PubMed:11584023, ECO:0000269|PubMed:15525676}.
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