Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P63037

- DNJA1_MOUSE

UniProt

P63037 - DNJA1_MOUSE

Protein

DnaJ homolog subfamily A member 1

Gene

Dnaja1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (31 Aug 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV By similarity. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi134 – 1341Zinc 1By similarity
    Metal bindingi137 – 1371Zinc 1By similarity
    Metal bindingi150 – 1501Zinc 2By similarity
    Metal bindingi153 – 1531Zinc 2By similarity
    Metal bindingi177 – 1771Zinc 2By similarity
    Metal bindingi180 – 1801Zinc 2By similarity
    Metal bindingi193 – 1931Zinc 1By similarity
    Metal bindingi196 – 1961Zinc 1By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri121 – 20585CR-typeAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. chaperone binding Source: UniProtKB
    3. Hsp70 protein binding Source: UniProtKB
    4. low-density lipoprotein particle receptor binding Source: MGI
    5. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. androgen receptor signaling pathway Source: MGI
    2. DNA damage response, detection of DNA damage Source: Ensembl
    3. negative regulation of apoptotic process Source: UniProtKB
    4. negative regulation of JUN kinase activity Source: UniProtKB
    5. positive regulation of apoptotic process Source: UniProtKB
    6. protein folding Source: InterPro
    7. protein localization to mitochondrion Source: UniProtKB
    8. regulation of protein transport Source: UniProtKB
    9. response to heat Source: InterPro
    10. spermatogenesis Source: MGI
    11. sperm motility Source: MGI

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DnaJ homolog subfamily A member 1
    Alternative name(s):
    DnaJ protein homolog 2
    Heat shock 40 kDa protein 4
    Heat shock protein J2
    Short name:
    HSJ-2
    Gene namesi
    Name:Dnaja1
    Synonyms:Dnaj2, Hsj2, Hspf4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1270129. Dnaja1.

    Subcellular locationi

    Membrane By similarity; Lipid-anchor By similarity. Cytoplasm By similarity. Microsome By similarity. Mitochondrion By similarity. Nucleus By similarity. Cytoplasmperinuclear region By similarity
    Note: Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria By similarity.By similarity

    GO - Cellular componenti

    1. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 394394DnaJ homolog subfamily A member 1PRO_0000071009Add
    BLAST
    Propeptidei395 – 3973Removed in mature formBy similarityPRO_0000396753

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661N6-acetyllysineBy similarity
    Modified residuei83 – 831PhosphoserineBy similarity
    Modified residuei335 – 3351PhosphoserineBy similarity
    Modified residuei381 – 3811PhosphotyrosineBy similarity
    Modified residuei394 – 3941Cysteine methyl esterBy similarity
    Lipidationi394 – 3941S-farnesyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP63037.
    PaxDbiP63037.
    PRIDEiP63037.

    Expressioni

    Gene expression databases

    ArrayExpressiP63037.
    BgeeiP63037.
    CleanExiMM_DNAJA1.
    GenevestigatoriP63037.

    Interactioni

    Subunit structurei

    Identified in a complex with HSPA1B and BAX.1 Publication

    Protein-protein interaction databases

    BioGridi200446. 7 interactions.
    DIPiDIP-32350N.
    IntActiP63037. 11 interactions.
    MINTiMINT-1858917.

    Structurei

    3D structure databases

    ProteinModelPortaliP63037.
    SMRiP63037. Positions 1-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 6863JAdd
    BLAST
    Repeati134 – 1418CXXCXGXG motif
    Repeati150 – 1578CXXCXGXG motif
    Repeati177 – 1848CXXCXGXG motif
    Repeati193 – 2008CXXCXGXG motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi75 – 9622Gly-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CR-type zinc finger.Curated
    Contains 1 J domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri121 – 20585CR-typeAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0484.
    HOGENOMiHOG000226718.
    HOVERGENiHBG066727.
    InParanoidiP63037.
    KOiK09502.
    OMAiGMQVRIQ.
    OrthoDBiEOG7XM2XK.
    PhylomeDBiP63037.
    TreeFamiTF105141.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    2.10.230.10. 1 hit.
    HAMAPiMF_01152. DnaJ.
    InterProiIPR012724. DnaJ.
    IPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    IPR001305. HSP_DnaJ_Cys-rich_dom.
    [Graphical view]
    PfamiPF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    PF00684. DnaJ_CXXCXGXG. 1 hit.
    [Graphical view]
    PRINTSiPR00625. JDOMAIN.
    SMARTiSM00271. DnaJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 3 hits.
    SSF57938. SSF57938. 1 hit.
    PROSITEiPS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    PS51188. ZF_CR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P63037-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ    50
    AYEVLADSKK RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGGRMQR 100
    ERRGKNVVHQ LSVTLEDLYN GATRKLALQK NVICDKCEGR GGKKGAVECC 150
    PNCRGTGMQI RIHQIGPGMV QQIQSVCMEC QGHGERISPK DRCKSCNGRK 200
    IVREKKILEV HIDKGMKDGQ KITFHGEGDQ EPGLEPGDII IVLDQKDHAV 250
    FTRRGEDLFM CMDIQLVEAL CGFQKPISTL DNRTIVITSH PGQIVKHGDI 300
    KCVLNEGMPI YRRPYEKGRL IIEFKVNFPE NGFLSPDKLS LLEKLLPERK 350
    EVEETDEMDQ VELVDFDPNQ ERRRHYNGEA YEDDEHHPRG GVQCQTS 397
    Length:397
    Mass (Da):44,868
    Last modified:August 31, 2004 - v1
    Checksum:i1783CE3D5C4CD558
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF055664 mRNA. Translation: AAC78597.1.
    AK083046 mRNA. Translation: BAC38744.1.
    BC057876 mRNA. Translation: AAH57876.1.
    CCDSiCCDS18049.1.
    RefSeqiNP_001158143.1. NM_001164671.1.
    NP_001158144.1. NM_001164672.1.
    NP_032324.1. NM_008298.5.
    UniGeneiMm.27897.

    Genome annotation databases

    EnsembliENSMUST00000030118; ENSMUSP00000030118; ENSMUSG00000028410.
    ENSMUST00000164233; ENSMUSP00000129730; ENSMUSG00000028410.
    GeneIDi15502.
    KEGGimmu:15502.
    UCSCiuc008sht.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF055664 mRNA. Translation: AAC78597.1 .
    AK083046 mRNA. Translation: BAC38744.1 .
    BC057876 mRNA. Translation: AAH57876.1 .
    CCDSi CCDS18049.1.
    RefSeqi NP_001158143.1. NM_001164671.1.
    NP_001158144.1. NM_001164672.1.
    NP_032324.1. NM_008298.5.
    UniGenei Mm.27897.

    3D structure databases

    ProteinModelPortali P63037.
    SMRi P63037. Positions 1-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200446. 7 interactions.
    DIPi DIP-32350N.
    IntActi P63037. 11 interactions.
    MINTi MINT-1858917.

    Proteomic databases

    MaxQBi P63037.
    PaxDbi P63037.
    PRIDEi P63037.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030118 ; ENSMUSP00000030118 ; ENSMUSG00000028410 .
    ENSMUST00000164233 ; ENSMUSP00000129730 ; ENSMUSG00000028410 .
    GeneIDi 15502.
    KEGGi mmu:15502.
    UCSCi uc008sht.2. mouse.

    Organism-specific databases

    CTDi 3301.
    MGIi MGI:1270129. Dnaja1.

    Phylogenomic databases

    eggNOGi COG0484.
    HOGENOMi HOG000226718.
    HOVERGENi HBG066727.
    InParanoidi P63037.
    KOi K09502.
    OMAi GMQVRIQ.
    OrthoDBi EOG7XM2XK.
    PhylomeDBi P63037.
    TreeFami TF105141.

    Miscellaneous databases

    ChiTaRSi DNAJA1. mouse.
    NextBioi 288400.
    PROi P63037.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63037.
    Bgeei P63037.
    CleanExi MM_DNAJA1.
    Genevestigatori P63037.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    2.10.230.10. 1 hit.
    HAMAPi MF_01152. DnaJ.
    InterProi IPR012724. DnaJ.
    IPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    IPR001305. HSP_DnaJ_Cys-rich_dom.
    [Graphical view ]
    Pfami PF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    PF00684. DnaJ_CXXCXGXG. 1 hit.
    [Graphical view ]
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 3 hits.
    SSF57938. SSF57938. 1 hit.
    PROSITEi PS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    PS51188. ZF_CR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A DnaJ-like gene, Hsj2, maps to mouse chromosome 5, at approximately 24 cM from the centromere."
      Royaux I., Minner F., Goffinet A.M., de Rouvroit C.L.
      Genomics 53:415-415(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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: Spinal cord.
    3. "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: FVB/N.
      Tissue: Mammary tumor.
    4. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 106-124 AND 375-389, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    5. "hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria."
      Gotoh T., Terada K., Oyadomari S., Mori M.
      Cell Death Differ. 11:390-402(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH HSPA1B AND BAX.

    Entry informationi

    Entry nameiDNJA1_MOUSE
    AccessioniPrimary (citable) accession number: P63037
    Secondary accession number(s): P54102
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: August 31, 2004
    Last modified: October 1, 2014
    This is version 100 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, Direct protein sequencing, 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