Human Gene DNAJB11 (ENST00000439351.5) from GENCODE V44
Description: Serves 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. (from UniProt Q9UBS4) RefSeq Summary (NM_016306): This gene encodes a soluble glycoprotein of the endoplasmic reticulum (ER) lumen that functions as a co-chaperone of binding immunoglobulin protein, a 70 kilodalton heat shock protein chaperone required for the proper folding and assembly of proteins in the ER. The encoded protein contains a highly conserved J domain of about 70 amino acids with a characteristic His-Pro-Asp (HPD) motif and may regulate the activity of binding immunoglobulin protein by stimulating ATPase activity. [provided by RefSeq, Mar 2014]. Gencode Transcript: ENST00000439351.5 Gencode Gene: ENSG00000090520.12 Transcript (Including UTRs) Position: hg38 chr3:186,567,403-186,585,800 Size: 18,398 Total Exon Count: 11 Strand: + Coding Region Position: hg38 chr3:186,570,898-186,585,408 Size: 14,511 Coding Exon Count: 10
ID:DJB11_HUMAN DESCRIPTION: RecName: Full=DnaJ homolog subfamily B member 11; AltName: Full=APOBEC1-binding protein 2; Short=ABBP-2; AltName: Full=DnaJ protein homolog 9; AltName: Full=ER-associated DNAJ; AltName: Full=ER-associated Hsp40 co-chaperone; AltName: Full=ER-associated dnaJ protein 3; Short=ERdj3; Short=ERj3p; AltName: Full=HEDJ; AltName: Full=Human DnaJ protein 9; Short=hDj-9; AltName: Full=PWP1-interacting protein 4; Flags: Precursor; FUNCTION: Serves 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. SUBUNIT: Part 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. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Associated with the ER membrane in a C-terminally epitope-tagged construct. TISSUE SPECIFICITY: Widely expressed. INDUCTION: By endoplasmic reticulum stress-inducing agents such as thapsigargin and tunicamycin. PTM: Contains high-mannose Endo H-sensitive carbohydrates. PTM: Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular disulfide bonds. The preferential partner for each Cys is not known. PTM: 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. SIMILARITY: Contains 1 J domain. CAUTION: PubMed: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.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9UBS4
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
