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Q9UBS4

- DJB11_HUMAN

UniProt

Q9UBS4 - DJB11_HUMAN

Protein

DnaJ homolog subfamily B member 11

Gene

DNAJB11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

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

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum lumen Source: Reactome
    3. membrane Source: UniProtKB
    4. nucleus Source: Ensembl

    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 – 2222By similarityAdd
    BLAST
    Chaini23 – 358336DnaJ homolog subfamily B member 11PRO_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 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.1 Publication

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 9066JPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 J domain.PROSITE-ProRule annotation

    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

    Experimental Info

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

    Natural variant

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

    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

    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: October 1, 2014
    This is version 133 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

    External Data

    Dasty 3