Human Gene DNAJB11 (uc003fqi.3) Description and Page Index
Description: Homo sapiens DnaJ (Hsp40) homolog, subfamily B, member 11 (DNAJB11), mRNA. 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]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: SRR1163657.516430.1, SRR5189664.111512.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcript (Including UTRs) Position: hg19 chr3:186,287,952-186,303,589 Size: 15,638 Total Exon Count: 10 Strand: + Coding Region Position: hg19 chr3:186,288,687-186,303,197 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.
Genetic Association Studies of Complex Diseases and Disorders
Genetic Association Database (archive): DNAJB11 CDC HuGE Published Literature: DNAJB11
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
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
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.