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Q9D832

- DNJB4_MOUSE

UniProt

Q9D832 - DNJB4_MOUSE

Protein

DnaJ homolog subfamily B member 4

Gene

Dnajb4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Probable chaperone.By similarity

    GO - Biological processi

    1. protein folding Source: InterPro

    Keywords - Molecular functioni

    Chaperone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DnaJ homolog subfamily B member 4
    Gene namesi
    Name:Dnajb4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1914285. Dnajb4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleus Source: Ensembl
    3. plasma membrane Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 337336DnaJ homolog subfamily B member 4PRO_0000071022Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei122 – 1221PhosphoserineBy similarity
    Modified residuei148 – 1481PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9D832.
    PaxDbiQ9D832.
    PRIDEiQ9D832.

    PTM databases

    PhosphoSiteiQ9D832.

    Expressioni

    Gene expression databases

    BgeeiQ9D832.
    CleanExiMM_DNAJB4.
    GenevestigatoriQ9D832.

    Interactioni

    Subunit structurei

    Homodimer. The C-terminal section interacts with the C-terminal tail of OPRM1. Interacts also with SDIM1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9D832. 3 interactions.
    MINTiMINT-4093222.
    STRINGi10090.ENSMUSP00000029669.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D832.
    SMRiQ9D832. Positions 1-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 6865JPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 J domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2214.
    GeneTreeiENSGT00720000108438.
    HOGENOMiHOG000226718.
    HOVERGENiHBG066727.
    InParanoidiQ9D832.
    KOiK09510.
    OMAiIEFDVSF.
    OrthoDBiEOG7TF79F.
    PhylomeDBiQ9D832.
    TreeFamiTF105141.

    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. 2 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.

    Q9D832-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKDYYHILG IDKGATDEDV KKAYRKQALK FHPDKNKSPQ AEEKFKEVAE    50
    AYEVLSDPKK REIYDQFGEE GLKGGAGGTD GQGGTFRYTF HGDPHATFAA 100
    FFGGSNPFEI FFGRRMGGGR DSEEMEIDGD PFSAFGFSMN GYPRDRNSVG 150
    PSRLKQDPPI IHELKVSLEE IYSGCTKRMK ISRKRLNPDG RSYRSEDKIL 200
    TIEIKKGWKE GTKITFPREG DETPNSIPAD IVFVIKDKEH PKFKRDGSNI 250
    VYTAKISLRE ALCGCSLNVP TMDGRNLPMS VTDIVKPGMR RRVIGYGLPF 300
    PKNPDQRGDL LIEFDVSFPD VISAASKEIL RKHLPAS 337
    Length:337
    Mass (Da):37,782
    Last modified:June 1, 2001 - v1
    Checksum:iBEE4A0E25BCEEFF4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661Q → L in BAB24608. (PubMed:16141072)Curated
    Sequence conflicti151 – 1511P → T in BAB24608. (PubMed:16141072)Curated
    Sequence conflicti329 – 3291I → S in BAB24608. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK006478 mRNA. Translation: BAB24608.1.
    AK008537 mRNA. Translation: BAB25729.1.
    AK028049 mRNA. Translation: BAC25720.1.
    AK136240 mRNA. Translation: BAE22891.1.
    AK162194 mRNA. Translation: BAE36783.1.
    BC017161 mRNA. Translation: AAH17161.1.
    CCDSiCCDS17915.1.
    RefSeqiNP_080202.1. NM_025926.4.
    NP_081563.2. NM_027287.4.
    XP_006501982.1. XM_006501919.1.
    XP_006501983.1. XM_006501920.1.
    UniGeneiMm.458538.
    Mm.46746.

    Genome annotation databases

    EnsembliENSMUST00000029669; ENSMUSP00000029669; ENSMUSG00000028035.
    ENSMUST00000050073; ENSMUSP00000053916; ENSMUSG00000028035.
    ENSMUST00000144950; ENSMUSP00000114356; ENSMUSG00000028035.
    GeneIDi67035.
    KEGGimmu:67035.
    UCSCiuc008rsq.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK006478 mRNA. Translation: BAB24608.1 .
    AK008537 mRNA. Translation: BAB25729.1 .
    AK028049 mRNA. Translation: BAC25720.1 .
    AK136240 mRNA. Translation: BAE22891.1 .
    AK162194 mRNA. Translation: BAE36783.1 .
    BC017161 mRNA. Translation: AAH17161.1 .
    CCDSi CCDS17915.1.
    RefSeqi NP_080202.1. NM_025926.4.
    NP_081563.2. NM_027287.4.
    XP_006501982.1. XM_006501919.1.
    XP_006501983.1. XM_006501920.1.
    UniGenei Mm.458538.
    Mm.46746.

    3D structure databases

    ProteinModelPortali Q9D832.
    SMRi Q9D832. Positions 1-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9D832. 3 interactions.
    MINTi MINT-4093222.
    STRINGi 10090.ENSMUSP00000029669.

    PTM databases

    PhosphoSitei Q9D832.

    Proteomic databases

    MaxQBi Q9D832.
    PaxDbi Q9D832.
    PRIDEi Q9D832.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029669 ; ENSMUSP00000029669 ; ENSMUSG00000028035 .
    ENSMUST00000050073 ; ENSMUSP00000053916 ; ENSMUSG00000028035 .
    ENSMUST00000144950 ; ENSMUSP00000114356 ; ENSMUSG00000028035 .
    GeneIDi 67035.
    KEGGi mmu:67035.
    UCSCi uc008rsq.2. mouse.

    Organism-specific databases

    CTDi 11080.
    MGIi MGI:1914285. Dnajb4.

    Phylogenomic databases

    eggNOGi COG2214.
    GeneTreei ENSGT00720000108438.
    HOGENOMi HOG000226718.
    HOVERGENi HBG066727.
    InParanoidi Q9D832.
    KOi K09510.
    OMAi IEFDVSF.
    OrthoDBi EOG7TF79F.
    PhylomeDBi Q9D832.
    TreeFami TF105141.

    Miscellaneous databases

    NextBioi 323364.
    PROi Q9D832.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D832.
    CleanExi MM_DNAJB4.
    Genevestigatori Q9D832.

    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. 2 hits.
    PROSITEi PS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Cerebellum, Egg, Small intestine and Testis.
    2. "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: Eye.

    Entry informationi

    Entry nameiDNJB4_MOUSE
    AccessioniPrimary (citable) accession number: Q9D832
    Secondary accession number(s): Q3TS92, Q9D9U2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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