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Q9UBS4 (DJB11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily B member 11
Alternative name(s):
APOBEC1-binding protein 2
Short name=ABBP-2
DnaJ protein homolog 9
ER-associated DNAJ
ER-associated Hsp40 co-chaperone
Endoplasmic reticulum DNA J domain-containing protein 3
Short name=ER-resident protein ERdj3
Short name=ERdj3
Short name=ERj3p
HEDJ
Human DnaJ protein 9
Short name=hDj-9
PWP1-interacting protein 4
Gene names
Name:DNAJB11
Synonyms:EDJ, ERJ3, HDJ9
ORF Names:PSEC0121, UNQ537/PRO1080
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Ref.2 Ref.14

Subunit structure

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. Ref.2 Ref.14 Ref.15

Subcellular location

Endoplasmic reticulum lumen. Note: Associated with the ER membrane in a C-terminally epitope-tagged construct. Ref.2 Ref.3 Ref.13 Ref.14

Tissue specificity

Widely expressed. Ref.2 Ref.11 Ref.14

Induction

By endoplasmic reticulum stress-inducing agents such as thapsigargin and tunicamycin. Ref.13 Ref.14

Post-translational modification

Contains high-mannose Endo H-sensitive carbohydrates.

Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular disulfide bonds. The preferential partner for each Cys is not known.

Thr-188 was reported (Ref.16) 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.

Sequence similarities

Contains 1 J domain.

Caution

Ref.11 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSPA5P110212EBI-713113,EBI-354921

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 358336DnaJ homolog subfamily B member 11
PRO_0000007260

Regions

Domain25 – 9066J

Amino acid modifications

Modified residue1881Phosphothreonine Ref.16
Glycosylation2611N-linked (GlcNAc...) Ref.17

Natural variations

Natural variant2641I → V. Ref.4 Ref.6
Corresponds to variant rs8147 [ dbSNP | Ensembl ].
VAR_016092

Experimental info

Mutagenesis531H → Q: Loss of HSPA5-binding, but no effect on interaction with denatured substrates. Ref.14
Mutagenesis1691C → S: Drastic loss of interaction with denatured substrates. Ref.15
Mutagenesis1711C → S: Drastic loss of interaction with denatured substrates. Ref.15
Mutagenesis1931C → S: Drastic loss of interaction with denatured substrates. Ref.15
Mutagenesis1961C → S: Drastic loss of interaction with denatured substrates. Ref.15
Sequence conflict2471K → R in CAG33377. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q9UBS4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 580CC4D66A06B734

FASTA35840,514
        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 

« Hide

References

« Hide 'large scale' references
[1]"Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature."
Ohtsuka K., Hata M.
Cell Stress Chaperones 5:98-112(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells."
Yu M., Haslam R.H.A., Haslam D.B.
J. Biol. Chem. 275:24984-24992(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA5, TISSUE SPECIFICITY, GLYCOSYLATION.
Tissue: Skeletal muscle.
[3]"Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p."
Bies C., Blum R., Dudek J., Nastainczyk W., Oberhauser S., Jung M., Zimmermann R.
Biol. Chem. 385:389-395(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, GLYCOSYLATION.
Tissue: Placenta.
[4]"hPWP1-interacting protein 4."
Honore B.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-264.
Tissue: Tonsil.
[5]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
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. expand/collapse author list , 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.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
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. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-264.
Tissue: Placenta and Retinoblastoma.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[11]"A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editing."
Lau P.P., Villanueva H., Kobayashi K., Nakamuta M., Chang B.H.-J., Chan L.
J. Biol. Chem. 276:46445-46452(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[13]"Localization and function in endoplasmic reticulum stress tolerance of ERdj3, a new member of Hsp40 family protein."
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.
Cell Stress Chaperones 9:253-264(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION.
[14]"ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates."
Shen Y., Hendershot L.M.
Mol. Biol. Cell 16:40-50(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, GLYCOSYLATION, INTERACTION WITH DENATURED SUBSTRATES, MUTAGENESIS OF HIS-53.
[15]"Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions."
Marcus N.Y., Marcus R.A., Schmidt B.Z., Haslam D.B.
Arch. Biochem. Biophys. 468:147-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-169; CYS-171; CYS-193 AND CYS-196, INTERACTION WITH DENATURED SUBSTRATES.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261.
Tissue: Liver.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028859 mRNA. Translation: BAA88307.1.
AF228505 mRNA. Translation: AAF61711.1.
AJ250137 mRNA. Translation: CAB65118.1.
AF277317 mRNA. Translation: AAK69110.1.
AY359043 mRNA. Translation: AAQ89402.1.
AK075300 mRNA. Translation: BAC11533.1.
AK075430 mRNA. Translation: BAC11617.1.
BT007063 mRNA. Translation: AAP35712.1.
CR457096 mRNA. Translation: CAG33377.1.
CH471052 Genomic DNA. Translation: EAW78190.1.
BC001144 mRNA. Translation: AAH01144.1.
CCDSCCDS3277.1.
PIRT52073.
RefSeqNP_057390.1. NM_016306.5.
UniGeneHs.317192.
Hs.712822.

3D structure databases

ProteinModelPortalQ9UBS4.
SMRQ9UBS4. Positions 22-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119699. 56 interactions.
DIPDIP-29678N.
IntActQ9UBS4. 30 interactions.
MINTMINT-1417807.
STRING9606.ENSP00000265028.

PTM databases

PhosphoSiteQ9UBS4.

Polymorphism databases

DMDM18203497.

2D gel databases

OGPQ9UBS4.
REPRODUCTION-2DPAGEIPI00008454.

Proteomic databases

MaxQBQ9UBS4.
PaxDbQ9UBS4.
PeptideAtlasQ9UBS4.
PRIDEQ9UBS4.

Protocols and materials databases

DNASU51726.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265028; ENSP00000265028; ENSG00000090520.
ENST00000439351; ENSP00000414398; ENSG00000090520.
GeneID51726.
KEGGhsa:51726.
UCSCuc003fqi.3. human.

Organism-specific databases

CTD51726.
GeneCardsGC03P186285.
HGNCHGNC:14889. DNAJB11.
HPAHPA010814.
HPA017051.
MIM611341. gene.
neXtProtNX_Q9UBS4.
PharmGKBPA27413.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0484.
HOGENOMHOG000226718.
HOVERGENHBG066727.
InParanoidQ9UBS4.
KOK09517.
OMAKCNCRNE.
OrthoDBEOG7Z3F59.
PhylomeDBQ9UBS4.
TreeFamTF105144.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9UBS4.
BgeeQ9UBS4.
CleanExHS_DNAJB11.
GenevestigatorQ9UBS4.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
InterProIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view]
PfamPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNAJB11. human.
GeneWikiDNAJB11.
GenomeRNAi51726.
NextBio55780.
PROQ9UBS4.
SOURCESearch...

Entry information

Entry nameDJB11_HUMAN
AccessionPrimary (citable) accession number: Q9UBS4
Secondary accession number(s): Q542Y5 expand/collapse secondary AC list , Q542Y9, Q6IAQ8, Q96JC6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM