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Q99KV1

- DJB11_MOUSE

UniProt

Q99KV1 - DJB11_MOUSE

Protein

DnaJ homolog subfamily B member 11

Gene

Dnajb11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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 By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. unfolded protein binding Source: MGI

    GO - Biological processi

    1. mRNA modification Source: MGI
    2. protein folding Source: InterPro

    Keywords - Molecular functioni

    Chaperone

    Enzyme and pathway databases

    ReactomeiREACT_106572. 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
    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
    Gene namesi
    Name:Dnajb11
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1915088. Dnajb11.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222By similarityAdd
    BLAST
    Chaini23 – 358336DnaJ homolog subfamily B member 11PRO_0000007261Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei188 – 1881PhosphothreonineBy similarity
    Glycosylationi261 – 2611N-linked (GlcNAc...)Curated

    Post-translational modificationi

    Contains high-mannose Endo H-sensitive carbohydrates.By similarity
    Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular disulfide bonds. The preferential partner for each Cys is not known By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ99KV1.
    PaxDbiQ99KV1.
    PRIDEiQ99KV1.

    2D gel databases

    REPRODUCTION-2DPAGEQ99KV1.

    PTM databases

    PhosphoSiteiQ99KV1.

    Expressioni

    Gene expression databases

    BgeeiQ99KV1.
    CleanExiMM_DNAJB11.
    GenevestigatoriQ99KV1.

    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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi212468. 2 interactions.
    DIPiDIP-60531N.
    IntActiQ99KV1. 4 interactions.
    MINTiMINT-1847287.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99KV1.
    SMRiQ99KV1. Positions 18-343.
    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.
    GeneTreeiENSGT00490000043321.
    HOGENOMiHOG000226718.
    HOVERGENiHBG066727.
    InParanoidiQ99KV1.
    KOiK09517.
    OMAiLFITFDV.
    OrthoDBiEOG7Z3F59.
    PhylomeDBiQ99KV1.
    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.

    Q99KV1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPQNLSTFC LLLLYLIGTV 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 FRIKVVKHRI 250
    FERRGDDLYT NVTVSLVEAL VGFEMDITHL DGHKVHISRD KITRPGAKLW 300
    KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAKEGIK QLLKQGPVQK 350
    VYNGLQGY 358
    Length:358
    Mass (Da):40,555
    Last modified:June 1, 2001 - v1
    Checksum:iE53CE0B3DF7465B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91F → L in BAC35956. (PubMed:16141072)Curated
    Sequence conflicti88 – 881T → A in AAH18282. (PubMed:15489334)Curated
    Sequence conflicti217 – 2171R → L in AAL17676. (PubMed:11584023)Curated
    Sequence conflicti240 – 2401R → P in AAL17676. (PubMed:11584023)Curated
    Sequence conflicti255 – 2551G → E in BAC35956. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY054981 mRNA. Translation: AAL17676.1.
    AK050500 mRNA. Translation: BAC34293.1.
    AK075785 mRNA. Translation: BAC35956.1.
    AK075953 mRNA. Translation: BAC36079.1.
    AK148511 mRNA. Translation: BAE28593.1.
    AK166730 mRNA. Translation: BAE38977.1.
    CT027991 Genomic DNA. Translation: CAO78022.1.
    BC003999 mRNA. Translation: AAH03999.1.
    BC018282 mRNA. Translation: AAH18282.1.
    BC040747 mRNA. Translation: AAH40747.1.
    CCDSiCCDS28070.1.
    RefSeqiNP_001177733.1. NM_001190804.1.
    NP_001177734.1. NM_001190805.1.
    NP_080676.3. NM_026400.5.
    UniGeneiMm.37516.
    Mm.477367.

    Genome annotation databases

    EnsembliENSMUST00000004574; ENSMUSP00000004574; ENSMUSG00000004460.
    ENSMUST00000166487; ENSMUSP00000126828; ENSMUSG00000004460.
    ENSMUST00000178320; ENSMUSP00000137542; ENSMUSG00000004460.
    GeneIDi67838.
    KEGGimmu:67838.
    UCSCiuc007yso.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY054981 mRNA. Translation: AAL17676.1 .
    AK050500 mRNA. Translation: BAC34293.1 .
    AK075785 mRNA. Translation: BAC35956.1 .
    AK075953 mRNA. Translation: BAC36079.1 .
    AK148511 mRNA. Translation: BAE28593.1 .
    AK166730 mRNA. Translation: BAE38977.1 .
    CT027991 Genomic DNA. Translation: CAO78022.1 .
    BC003999 mRNA. Translation: AAH03999.1 .
    BC018282 mRNA. Translation: AAH18282.1 .
    BC040747 mRNA. Translation: AAH40747.1 .
    CCDSi CCDS28070.1.
    RefSeqi NP_001177733.1. NM_001190804.1.
    NP_001177734.1. NM_001190805.1.
    NP_080676.3. NM_026400.5.
    UniGenei Mm.37516.
    Mm.477367.

    3D structure databases

    ProteinModelPortali Q99KV1.
    SMRi Q99KV1. Positions 18-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212468. 2 interactions.
    DIPi DIP-60531N.
    IntActi Q99KV1. 4 interactions.
    MINTi MINT-1847287.

    PTM databases

    PhosphoSitei Q99KV1.

    2D gel databases

    REPRODUCTION-2DPAGE Q99KV1.

    Proteomic databases

    MaxQBi Q99KV1.
    PaxDbi Q99KV1.
    PRIDEi Q99KV1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000004574 ; ENSMUSP00000004574 ; ENSMUSG00000004460 .
    ENSMUST00000166487 ; ENSMUSP00000126828 ; ENSMUSG00000004460 .
    ENSMUST00000178320 ; ENSMUSP00000137542 ; ENSMUSG00000004460 .
    GeneIDi 67838.
    KEGGi mmu:67838.
    UCSCi uc007yso.2. mouse.

    Organism-specific databases

    CTDi 51726.
    MGIi MGI:1915088. Dnajb11.

    Phylogenomic databases

    eggNOGi COG0484.
    GeneTreei ENSGT00490000043321.
    HOGENOMi HOG000226718.
    HOVERGENi HBG066727.
    InParanoidi Q99KV1.
    KOi K09517.
    OMAi LFITFDV.
    OrthoDBi EOG7Z3F59.
    PhylomeDBi Q99KV1.
    TreeFami TF105144.

    Enzyme and pathway databases

    Reactomei REACT_106572. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi DNAJB11. mouse.
    NextBioi 325665.
    PROi Q99KV1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99KV1.
    CleanExi MM_DNAJB11.
    Genevestigatori Q99KV1.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Pancreas.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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].
      Strain: Czech II and FVB/N.
      Tissue: Colon and Mammary tumor.
    5. "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.
    6. "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: SUBCELLULAR LOCATION, INTERACTION WITH DENATURED SUBSTRATES.

    Entry informationi

    Entry nameiDJB11_MOUSE
    AccessioniPrimary (citable) accession number: Q99KV1
    Secondary accession number(s): A6X957
    , Q543I7, Q8BK79, Q8VCY1, Q8VHB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    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.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3