ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9UBS4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DJB11_HUMAN
Primary accession number Q9UBS4
Secondary accession numbers Q542Y5 Q542Y9 Q6IAQ8 Q96JC6
Integrated into Swiss-Prot on October 18, 2001
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 68)
Name and origin of the protein
Protein name DnaJ homolog subfamily B member 11 [Precursor]
Synonyms ER-associated dnaJ protein 3
ERj3p
ERdj3
ER-associated Hsp40 co-chaperone
ER-associated DNAJ
HEDJ
hDj9
PWP1-interacting protein 4
APOBEC1-binding protein 2
ABBP-2
Gene name
Name: DNAJB11
Synonyms: EDJ, ERJ3
ORFNames: PSEC0121, UNQ537/PRO1080
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11147971 [NCBI, ExPASy, EBI, Israel, Japan]
Ohtsuka K., Hata M.;
"Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature.";
Cell Stress Chaperones 5:98-112(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA5, TISSUE SPECIFICITY, AND GLYCOSYLATION.
TISSUE=Skeletal muscle;
DOI=10.1074/jbc.M000739200; PubMed=10827079 [NCBI, ExPASy, EBI, Israel, Japan]
Yu M., Haslam R.H.A., Haslam D.B.;
"HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells.";
J. Biol. Chem. 275:24984-24992(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND GLYCOSYLATION.
TISSUE=Placenta;
DOI=10.1515/BC.2004.043; PubMed=15195998 [NCBI, ExPASy, EBI, Israel, Japan]
Bies C., Blum R., Dudek J., Nastainczyk W., Oberhauser S., Jung M., Zimmermann R.;
"Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p.";
Biol. Chem. 385:389-395(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-264.
TISSUE=Tonsil;
Honore B.;
"hPWP1-interacting protein 4.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-264.
TISSUE=Placenta, and Retinoblastoma;
DOI=10.1093/dnares/12.2.117; PubMed=16303743 [NCBI, ExPASy, EBI, Israel, Japan]
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
TISSUE SPECIFICITY.
DOI=10.1074/jbc.M109215200; PubMed=11584023 [NCBI, ExPASy, EBI, Israel, Japan]
Lau P.P., Villanueva H., Kobayashi K., Nakamuta M., Chang B.H.-J., Chan L.;
"A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editing.";
J. Biol. Chem. 276:46445-46452(2001).
[12]
COMPONENT OF A CHAPERONE COMPLEX.
DOI=10.1091/mbc.E02-05-0311; PubMed=12475965 [NCBI, ExPASy, EBI, Israel, Japan]
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[13]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=15544163 [NCBI, ExPASy, EBI, Israel, Japan]
Nakanishi K., Kamiguchi K., Torigoe T., Nabeta C., Hirohashi Y., Asanuma H., Tobioka H., Koge N., Harada O., Tamura Y., Nagano H., Yano S., Chiba S., Matsumoto H., Sato N.;
"Localization and function in endoplasmic reticulum stress tolerance of ERdj3, a new member of Hsp40 family protein.";
Cell Stress Chaperones 9:253-264(2004).
[14]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, GLYCOSYLATION, INTERACTION WITH DENATURED SUBSTRATES, AND MUTAGENESIS OF HIS-53.
DOI=10.1091/mbc.E04-05-0434; PubMed=15525676 [NCBI, ExPASy, EBI, Israel, Japan]
Shen Y., Hendershot L.M.;
"ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates.";
Mol. Biol. Cell 16:40-50(2005).
[15]
MUTAGENESIS OF CYS-169; CYS-171; CYS-193 AND CYS-196, AND INTERACTION WITH DENATURED SUBSTRATES.
DOI=10.1016/j.abb.2007.10.001; PubMed=17976514 [NCBI, ExPASy, EBI, Israel, Japan]
Marcus N.Y., Marcus R.A., Schmidt B.Z., Haslam D.B.;
"Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions.";
Arch. Biochem. Biophys. 468:147-158(2007).
[16]
POSSIBLE PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
Comments
  • 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 a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, 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.
  • INTERACTION:
    O60496:DOK2; NbExp=1; IntAct=EBI-713113, EBI-1046024;
  • SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Associated with the ER membrane in a C-terminally epitope-tagged construct.
  • TISSUE SPECIFICITY: Widely expressed.
  • INDUCTION: By ER 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.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB028859; BAA88307.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF228505; AAF61711.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250137; CAB65118.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF277317; AAK69110.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY359043; AAQ89402.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007063; AAP35712.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457096; CAG33377.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075300; BAC11533.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075430; BAC11617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471052; EAW78190.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001144; AAH01144.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T52073; T52073.
RefSeq NP_057390.1; -.
UniGene Hs.317192
3D structure databases
HSSP P25685; 1HDJ. [HSSP ENTRY / PDB]
ModBase Q9UBS4.
Protein-protein interaction databases
IntAct Q9UBS4; -.
PTM databases
PhosphoSite Q9UBS4; -.
2D gel databases
OGP Q9UBS4; -.
REPRODUCTION-2DPAGE IPI00008454; -.
Organism-specific databases
H-InvDB HIX0003932; -.
HGNC HGNC:14889; DNAJB11.
GenAtlas DNAJB11.
HPA HPA010814; -.
HPA017051; -.
MIM 611341; gene. [NCBI / EBI]
PharmGKB PA27413; -.
GeneCards Q9UBS4.
Gene expression databases
ArrayExpress Q9UBS4; -.
CleanEx HS_DNAJB11; -.
GermOnline ENSG00000090520; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR002939; DnaJ_C.
IPR001623; DnaJ_N.
IPR015609; Hsp40/DnaJ_Rel.
IPR003095; Hsp_DnaJ.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
PANTHER PTHR11821; Hsp40/DnaJ_Rel; 1.
Pfam PF00226; DnaJ; 1.
PF01556; DnaJ_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00625; DNAJPROTEIN.
SMART SM00271; DnaJ; 1.
SMART graphical view of domain structure.
PROSITE PS00636; DNAJ_1; 1.
PS50076; DNAJ_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9UBS4.
Proteomic databases
PeptideAtlas Q9UBS4; -.
Genome annotation databases
Ensembl ENSG00000090520; Homo sapiens. [Contig view]
GeneID 51726; -.
KEGG hsa:51726; -.
Phylogenomic databases
HOVERGEN Q9UBS4; -.
Other
SOURCE DNAJB11; Homo sapiens.
ProtoNet Q9UBS4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chaperone; Endoplasmic reticulum; Glycoprotein; Polymorphism; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    22  22     By similarity. 
CHAIN   23   358  336     DnaJ homolog subfamily B member 11. PRO_0000007260
DOMAIN   25    90  66     J. 
CARBOHYD   261   261        N-linked (GlcNAc...) (Probable). 
VARIANT   264   264  1     I -> V (in dbSNP:rs8147 [NCBI]). VAR_016092 
MUTAGEN   53    53        H->Q: Loss of HSPA5-binding, but no effect on interaction with denatured substrates. 
MUTAGEN   169   169        C->S: Drastic loss of interaction with denatured substrates. 
MUTAGEN   171   171        C->S: Drastic loss of interaction with denatured substrates. 
MUTAGEN   193   193        C->S: Drastic loss of interaction with denatured substrates. 
MUTAGEN   196   196        C->S: Drastic loss of interaction with denatured substrates. 
CONFLICT   247   247        K -> R (in Ref. 7; CAG33377). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 40514 Da [This is the MW of the unprocessed precursor] CRC64: 580CC4D66A06B734 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPQNLSTFC LLLLYLIGAV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD 

        70         80         90        100        110        120 
PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT 

       130        140        150        160        170        180 
PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL 

       190        200        210        220        230        240 
GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR 

       250        260        270        280        290        300 
FRIKVVKHPI FERRGDDLYT NVTISLVESL VGFEMDITHL DGHKVHISRD KITRPGAKLW 

       310        320        330        340        350 
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAREGIK QLLKQGSVQK VYNGLQGY 

Q9UBS4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!