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Protein

DnaJ homolog subfamily B member 11

Gene

DNAJB11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciZFISH:ENSG00000090520-MONOMER.
ReactomeiR-HSA-381038. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:14889. DNAJB11.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum chaperone complex Source: Ensembl
  • endoplasmic reticulum lumen Source: Reactome
  • membrane Source: UniProtKB
  • nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi53H → Q: Loss of HSPA5-binding, but no effect on interaction with denatured substrates. 1 Publication1
Mutagenesisi169C → S: Drastic loss of interaction with denatured substrates. 1 Publication1
Mutagenesisi171C → S: Drastic loss of interaction with denatured substrates. 1 Publication1
Mutagenesisi193C → S: Drastic loss of interaction with denatured substrates. 1 Publication1
Mutagenesisi196C → S: Drastic loss of interaction with denatured substrates. 1 Publication1

Organism-specific databases

DisGeNETi51726.
OpenTargetsiENSG00000090520.
PharmGKBiPA27413.

Polymorphism and mutation databases

BioMutaiDNAJB11.
DMDMi18203497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
ChainiPRO_000000726023 – 358DnaJ homolog subfamily B member 11Add BLAST336

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei188PhosphothreonineCombined sources1
Glycosylationi261N-linked (GlcNAc...)1 Publication1

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 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

EPDiQ9UBS4.
MaxQBiQ9UBS4.
PaxDbiQ9UBS4.
PeptideAtlasiQ9UBS4.
PRIDEiQ9UBS4.
TopDownProteomicsiQ9UBS4.

2D gel databases

OGPiQ9UBS4.
REPRODUCTION-2DPAGEIPI00008454.

PTM databases

iPTMnetiQ9UBS4.
PhosphoSitePlusiQ9UBS4.

Expressioni

Tissue specificityi

Widely expressed.3 Publications

Inductioni

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

Gene expression databases

BgeeiENSG00000090520.
CleanExiHS_DNAJB11.
GenevisibleiQ9UBS4. HS.

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
HSPA5P110213EBI-713113,EBI-354921
slrPQ8ZQQ24EBI-713113,EBI-10712653From a different organism.

Protein-protein interaction databases

BioGridi119699. 83 interactors.
DIPiDIP-29678N.
IntActiQ9UBS4. 44 interactors.
MINTiMINT-1417807.
STRINGi9606.ENSP00000265028.

Structurei

3D structure databases

ProteinModelPortaliQ9UBS4.
SMRiQ9UBS4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 90JPROSITE-ProRule annotationAdd BLAST66

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0713. Eukaryota.
COG0484. LUCA.
GeneTreeiENSGT00860000133716.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiQ9UBS4.
KOiK09517.
OMAiRDEMEYP.
OrthoDBiEOG091G0GWF.
PhylomeDBiQ9UBS4.
TreeFamiTF105144.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
InterProiIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 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

        10         20         30         40         50
MAPQNLSTFC LLLLYLIGAV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL
60 70 80 90 100
QLHPDRNPDD PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS
110 120 130 140 150
SHGDIFSHFF GDFGFMFGGT PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF
160 170 180 190 200
VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL GPGRFQMTQE VVCDECPNVK
210 220 230 240 250
LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR FRIKVVKHPI
260 270 280 290 300
FERRGDDLYT NVTISLVESL VGFEMDITHL DGHKVHISRD KITRPGAKLW
310 320 330 340 350
KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAREGIK QLLKQGSVQK

VYNGLQGY
Length:358
Mass (Da):40,514
Last modified:May 1, 2000 - v1
Checksum:i580CC4D66A06B734
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti247K → R in CAG33377 (Ref. 8) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_016092264I → V.2 PublicationsCorresponds to variant rs8147dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9UBS4.
SMRiQ9UBS4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119699. 83 interactors.
DIPiDIP-29678N.
IntActiQ9UBS4. 44 interactors.
MINTiMINT-1417807.
STRINGi9606.ENSP00000265028.

PTM databases

iPTMnetiQ9UBS4.
PhosphoSitePlusiQ9UBS4.

Polymorphism and mutation databases

BioMutaiDNAJB11.
DMDMi18203497.

2D gel databases

OGPiQ9UBS4.
REPRODUCTION-2DPAGEIPI00008454.

Proteomic databases

EPDiQ9UBS4.
MaxQBiQ9UBS4.
PaxDbiQ9UBS4.
PeptideAtlasiQ9UBS4.
PRIDEiQ9UBS4.
TopDownProteomicsiQ9UBS4.

Protocols and materials databases

DNASUi51726.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265028; ENSP00000265028; ENSG00000090520.
ENST00000439351; ENSP00000414398; ENSG00000090520.
GeneIDi51726.
KEGGihsa:51726.
UCSCiuc003fqi.4. human.

Organism-specific databases

CTDi51726.
DisGeNETi51726.
GeneCardsiDNAJB11.
HGNCiHGNC:14889. DNAJB11.
HPAiHPA010814.
HPA017051.
MIMi611341. gene.
neXtProtiNX_Q9UBS4.
OpenTargetsiENSG00000090520.
PharmGKBiPA27413.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0713. Eukaryota.
COG0484. LUCA.
GeneTreeiENSGT00860000133716.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiQ9UBS4.
KOiK09517.
OMAiRDEMEYP.
OrthoDBiEOG091G0GWF.
PhylomeDBiQ9UBS4.
TreeFamiTF105144.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000090520-MONOMER.
ReactomeiR-HSA-381038. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSiDNAJB11. human.
GeneWikiiDNAJB11.
GenomeRNAii51726.
PROiQ9UBS4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000090520.
CleanExiHS_DNAJB11.
GenevisibleiQ9UBS4. HS.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
InterProiIPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 155 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

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.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.