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Q9UBS4

- DJB11_HUMAN

UniProt

Q9UBS4 - DJB11_HUMAN

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Protein
DnaJ homolog subfamily B member 11
Gene
DNAJB11, EDJ, ERJ3, HDJ9, PSEC0121, UNQ537/PRO1080
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. endoplasmic reticulum unfolded protein response Source: Reactome
  4. mRNA modification Source: Ensembl
  5. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:DNAJB11
Synonyms:EDJ, ERJ3, HDJ9
ORF Names:PSEC0121, UNQ537/PRO1080
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:14889. DNAJB11.

Subcellular locationi

Endoplasmic reticulum lumen
Note: Associated with the ER membrane in a C-terminally epitope-tagged construct.4 Publications

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531H → Q: Loss of HSPA5-binding, but no effect on interaction with denatured substrates. 1 Publication
Mutagenesisi169 – 1691C → S: Drastic loss of interaction with denatured substrates. 1 Publication
Mutagenesisi171 – 1711C → S: Drastic loss of interaction with denatured substrates. 1 Publication
Mutagenesisi193 – 1931C → S: Drastic loss of interaction with denatured substrates. 1 Publication
Mutagenesisi196 – 1961C → S: Drastic loss of interaction with denatured substrates. 1 Publication

Organism-specific databases

PharmGKBiPA27413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 By similarity
Add
BLAST
Chaini23 – 358336DnaJ homolog subfamily B member 11
PRO_0000007260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Phosphothreonine1 Publication
Glycosylationi261 – 2611N-linked (GlcNAc...)1 Publication

Post-translational modificationi

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 (1 Publication) 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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9UBS4.
PaxDbiQ9UBS4.
PeptideAtlasiQ9UBS4.
PRIDEiQ9UBS4.

2D gel databases

OGPiQ9UBS4.
REPRODUCTION-2DPAGEIPI00008454.

PTM databases

PhosphoSiteiQ9UBS4.

Expressioni

Tissue specificityi

Widely expressed.3 Publications

Inductioni

By endoplasmic reticulum stress-inducing agents such as thapsigargin and tunicamycin.2 Publications

Gene expression databases

ArrayExpressiQ9UBS4.
BgeeiQ9UBS4.
CleanExiHS_DNAJB11.
GenevestigatoriQ9UBS4.

Organism-specific databases

HPAiHPA010814.
HPA017051.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPA5P110212EBI-713113,EBI-354921

Protein-protein interaction databases

BioGridi119699. 55 interactions.
DIPiDIP-29678N.
IntActiQ9UBS4. 30 interactions.
MINTiMINT-1417807.
STRINGi9606.ENSP00000265028.

Structurei

3D structure databases

ProteinModelPortaliQ9UBS4.
SMRiQ9UBS4. Positions 22-343.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 9066J
Add
BLAST

Sequence similaritiesi

Contains 1 J domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0484.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiQ9UBS4.
KOiK09517.
OMAiKCNCRNE.
OrthoDBiEOG7Z3F59.
PhylomeDBiQ9UBS4.
TreeFamiTF105144.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view]
PfamiPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UBS4-1 [UniParc]FASTAAdd to Basket

« Hide

MAPQNLSTFC LLLLYLIGAV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL    50
QLHPDRNPDD PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS 100
SHGDIFSHFF GDFGFMFGGT PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF 150
VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL GPGRFQMTQE VVCDECPNVK 200
LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR FRIKVVKHPI 250
FERRGDDLYT NVTISLVESL VGFEMDITHL DGHKVHISRD KITRPGAKLW 300
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAREGIK QLLKQGSVQK 350
VYNGLQGY 358
Length:358
Mass (Da):40,514
Last modified:May 1, 2000 - v1
Checksum:i580CC4D66A06B734
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti264 – 2641I → V.2 Publications
Corresponds to variant rs8147 [ dbSNP | Ensembl ].
VAR_016092

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti247 – 2471K → R in CAG33377. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3277.1.
PIRiT52073.
RefSeqiNP_057390.1. NM_016306.5.
UniGeneiHs.317192.
Hs.712822.

Genome annotation databases

EnsembliENST00000265028; ENSP00000265028; ENSG00000090520.
ENST00000439351; ENSP00000414398; ENSG00000090520.
GeneIDi51726.
KEGGihsa:51726.
UCSCiuc003fqi.3. human.

Polymorphism databases

DMDMi18203497.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3277.1.
PIRi T52073.
RefSeqi NP_057390.1. NM_016306.5.
UniGenei Hs.317192.
Hs.712822.

3D structure databases

ProteinModelPortali Q9UBS4.
SMRi Q9UBS4. Positions 22-343.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119699. 55 interactions.
DIPi DIP-29678N.
IntActi Q9UBS4. 30 interactions.
MINTi MINT-1417807.
STRINGi 9606.ENSP00000265028.

PTM databases

PhosphoSitei Q9UBS4.

Polymorphism databases

DMDMi 18203497.

2D gel databases

OGPi Q9UBS4.
REPRODUCTION-2DPAGE IPI00008454.

Proteomic databases

MaxQBi Q9UBS4.
PaxDbi Q9UBS4.
PeptideAtlasi Q9UBS4.
PRIDEi Q9UBS4.

Protocols and materials databases

DNASUi 51726.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265028 ; ENSP00000265028 ; ENSG00000090520 .
ENST00000439351 ; ENSP00000414398 ; ENSG00000090520 .
GeneIDi 51726.
KEGGi hsa:51726.
UCSCi uc003fqi.3. human.

Organism-specific databases

CTDi 51726.
GeneCardsi GC03P186285.
HGNCi HGNC:14889. DNAJB11.
HPAi HPA010814.
HPA017051.
MIMi 611341. gene.
neXtProti NX_Q9UBS4.
PharmGKBi PA27413.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0484.
HOGENOMi HOG000226718.
HOVERGENi HBG066727.
InParanoidi Q9UBS4.
KOi K09517.
OMAi KCNCRNE.
OrthoDBi EOG7Z3F59.
PhylomeDBi Q9UBS4.
TreeFami TF105144.

Enzyme and pathway databases

Reactomei REACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSi DNAJB11. human.
GeneWikii DNAJB11.
GenomeRNAii 51726.
NextBioi 55780.
PROi Q9UBS4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UBS4.
Bgeei Q9UBS4.
CleanExi HS_DNAJB11.
Genevestigatori Q9UBS4.

Family and domain databases

Gene3Di 1.10.287.110. 1 hit.
InterProi IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view ]
Pfami PF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
[Graphical view ]
PRINTSi PR00625. JDOMAIN.
SMARTi SM00271. DnaJ. 1 hit.
[Graphical view ]
SUPFAMi SSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
PROSITEi PS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDJB11_HUMAN
AccessioniPrimary (citable) accession number: Q9UBS4
Secondary accession number(s): Q542Y5
, Q542Y9, Q6IAQ8, Q96JC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

1 Publication 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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