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 

Page IndexSequence and LinksUniProtKB CommentsGenetic AssociationsCTDGene Alleles
RNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther SpeciesGO Annotations
mRNA DescriptionsPathwaysOther NamesGeneReviewsModel InformationMethods
Data last updated: 2013-06-14

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr3:186,287,952-186,303,589)mRNA (may differ from genome)Protein (358 aa)
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Wikipedia

-  Comments and Description Text from UniProtKB
  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

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
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-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 38.46 RPKM in Thyroid
Total median expression: 964.98 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
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-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -315.55735-0.429 Picture PostScript Text
3' UTR -90.80392-0.232 Picture PostScript Text

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.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR002939 - DnaJ_C
IPR001623 - DnaJ_N
IPR018253 - Heat_shock_DnaJ_CS
IPR008971 - HSP40/DnaJ_pept-bd
IPR003095 - Hsp_DnaJ

Pfam Domains:
PF00226 - DnaJ domain
PF01556 - DnaJ C terminal domain

SCOP Domains:
46565 - Chaperone J-domain
49493 - HSP40/DnaJ peptide-binding domain

ModBase Predicted Comparative 3D Structure on Q9UBS4
FrontTopSide
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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.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologGenome BrowserGenome BrowserGenome BrowserGenome BrowserNo ortholog
Gene DetailsGene Details Gene DetailsGene Details 
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 RGDEnsemblFlyBaseWormBase 
 Protein SequenceProtein SequenceProtein SequenceProtein Sequence 
 AlignmentAlignmentAlignmentAlignment 

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0005515 protein binding
GO:0051082 unfolded protein binding

Biological Process:
GO:0006457 protein folding
GO:0032781 positive regulation of ATPase activity
GO:0036498 IRE1-mediated unfolded protein response

Cellular Component:
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0016020 membrane


-  Descriptions from all associated GenBank mRNAs
  BC046500 - Homo sapiens DnaJ (Hsp40) homolog, subfamily B, member 11, mRNA (cDNA clone IMAGE:4830954).
AK301292 - Homo sapiens cDNA FLJ56253 complete cds, highly similar to DnaJ homolog subfamily B member 11 precursor.
AK075430 - Homo sapiens cDNA PSEC0121 fis, clone PLACE1003085, highly similar to DnaJ homolog subfamily B member 11 precursor.
AF277317 - Homo sapiens PWP1-interacting protein 4 mRNA, complete cds.
AK075300 - Homo sapiens cDNA FLJ90819 fis, clone Y79AA1001264, highly similar to DnaJ homolog subfamily B member 11 precursor.
BC001144 - Homo sapiens DnaJ (Hsp40) homolog, subfamily B, member 11, mRNA (cDNA clone MGC:1169 IMAGE:3534756), complete cds.
AB028859 - Homo sapiens mRNA for hDj9, complete cds.
AY359043 - Homo sapiens clone DNA56047 DNAJB11 (UNQ537) mRNA, complete cds.
JD485011 - Sequence 466035 from Patent EP1572962.
JD223664 - Sequence 204688 from Patent EP1572962.
AF228505 - Homo sapiens ER-associated Hsp40 co-chaperone (EDJ) mRNA, complete cds.
JD127624 - Sequence 108648 from Patent EP1572962.
JD137797 - Sequence 118821 from Patent EP1572962.
AJ250137 - Homo sapiens mRNA for ERj3 protein (ERj3 gene).
DQ890601 - Synthetic construct clone IMAGE:100003231; FLH165118.01X; RZPDo839G02158D DnaJ (Hsp40) homolog, subfamily B, member 11 (DNAJB11) gene, encodes complete protein.
DQ893869 - Synthetic construct Homo sapiens clone IMAGE:100008329; FLH165114.01L; RZPDo839G02157D DnaJ (Hsp40) homolog, subfamily B, member 11 (DNAJB11) gene, encodes complete protein.
AB463574 - Synthetic construct DNA, clone: pF1KB6496, Homo sapiens DNAJB11 gene for DnaJ (Hsp40) homolog, subfamily B, member 11, without stop codon, in Flexi system.
KJ893980 - Synthetic construct Homo sapiens clone ccsbBroadEn_03374 DNAJB11 gene, encodes complete protein.
BT007063 - Homo sapiens DnaJ (Hsp40) homolog, subfamily B, member 11 mRNA, complete cds.
CR457096 - Homo sapiens full open reading frame cDNA clone RZPDo834G1011D for gene DNAJB11, DnaJ (Hsp40) homolog, subfamily B, member 11; complete cds, incl. stopcodon.
AK124289 - Homo sapiens cDNA FLJ42295 fis, clone TLIVE2008213, highly similar to DnaJ homolog subfamily B member 11 precursor.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein Q9UBS4 (Reactome details) participates in the following event(s):

R-HSA-381038 XBP1(S) activates chaperone genes
R-HSA-381070 IRE1alpha activates chaperones
R-HSA-381119 Unfolded Protein Response (UPR)
R-HSA-392499 Metabolism of proteins

-  Other Names for This Gene
  Alternate Gene Symbols: DJB11_HUMAN, EDJ, ERJ3, HDJ9, NM_016306, NP_057390, PSEC0121, Q542Y5, Q542Y9, Q6IAQ8, Q96JC6, Q9UBS4, UNQ537/PRO1080
UCSC ID: uc003fqi.3
RefSeq Accession: NM_016306
Protein: Q9UBS4 (aka DJB11_HUMAN)
CCDS: CCDS3277.1

-  GeneReviews for This Gene
  GeneReviews article(s) related to gene DNAJB11:
pkd-ad (Polycystic Kidney Disease, Autosomal Dominant)

-  Gene Model Information
 
category: coding nonsense-mediated-decay: no RNA accession: NM_016306.4
exon count: 10CDS single in 3' UTR: no RNA size: 1723
ORF size: 1077CDS single in intron: no Alignment % ID: 100.00
txCdsPredict score: 1760.50frame shift in genome: no % Coverage: 98.03
has start codon: yes stop codon in genome: no # of Alignments: 1
has end codon: yes retained intron: no # AT/AC introns 0
selenocysteine: no end bleed into intron: 0# strange splices: 0
Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.