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O75190

- DNJB6_HUMAN

UniProt

O75190 - DNJB6_HUMAN

Protein

DnaJ homolog subfamily B member 6

Gene

DNAJB6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (18 Oct 2001)
      Previous versions | rss
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    Functioni

    Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity.4 Publications

    GO - Molecular functioni

    1. ATPase activator activity Source: UniProtKB
    2. chaperone binding Source: UniProtKB
    3. DNA binding Source: Ensembl
    4. heat shock protein binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. unfolded protein binding Source: UniProt

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. chorio-allantoic fusion Source: Ensembl
    3. chorion development Source: Ensembl
    4. extracellular matrix organization Source: Ensembl
    5. intermediate filament organization Source: UniProtKB
    6. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    7. negative regulation of inclusion body assembly Source: UniProt
    8. negative regulation of transcription, DNA-templated Source: Ensembl
    9. positive regulation of ATPase activity Source: GOC
    10. protein folding Source: UniProtKB
    11. protein localization to nucleus Source: Ensembl
    12. syncytiotrophoblast cell differentiation involved in labyrinthine layer development Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DnaJ homolog subfamily B member 6
    Alternative name(s):
    HHDJ1
    Heat shock protein J2
    Short name:
    HSJ-2
    MRJ
    MSJ-1
    Gene namesi
    Name:DNAJB6
    Synonyms:HSJ2, MRJ, MSJ1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:14888. DNAJB6.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleus Source: UniProtKB
    5. perinuclear region of cytoplasm Source: UniProtKB
    6. Z disc Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Limb-girdle muscular dystrophy 1E (LGMD1E) [MIM:603511]: An autosomal dominant myopathy characterized by adult onset of proximal muscle weakness, beginning in the hip girdle region and later progressing to the shoulder girdle region.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. There is evidence that LGMD1E is caused by dysfunction of isoform B (PubMed:22366786).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891F → I in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. 1 Publication
    VAR_067833
    Natural varianti93 – 931F → L in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. 2 Publications
    VAR_067834
    Natural varianti96 – 961P → R in LGMD1E. 1 Publication
    VAR_067835

    Keywords - Diseasei

    Disease mutation, Limb-girdle muscular dystrophy

    Organism-specific databases

    MIMi603511. phenotype.
    Orphaneti34516. Autosomal dominant limb-girdle muscular dystrophy type 1D.
    PharmGKBiPA27418.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 326325DnaJ homolog subfamily B member 6PRO_0000071025Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei277 – 2771Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75190.
    PaxDbiO75190.
    PRIDEiO75190.

    PTM databases

    PhosphoSiteiO75190.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest levels in testis and brain, and lower levels in heart, spleen, intestine, ovary, placenta, lung, kidney, pancreas, thymus, prostate, skeletal muscle, liver and leukocytes. In testis, expressed in germ cells in the earlier stages of differentiation pathway as well as in spermatids. In brain, expressed at a higher level in hippocampus and thalamus and a lower level in amygdala, substantia nigra, corpus callosum and caudate nucleus.4 Publications

    Gene expression databases

    ArrayExpressiO75190.
    BgeeiO75190.
    CleanExiHS_DNAJB6.
    GenevestigatoriO75190.

    Organism-specific databases

    HPAiCAB004670.
    HPA024258.

    Interactioni

    Subunit structurei

    Homooligomer. Interacts with BAG3, HSPB8 and STUB1. Interacts with ALKBH1 By similarity. Interacts with HSP70, KRT18 and PTTG. Isoform B interacts with histone deacetylases HDAC4, HDAC6, and SIRT2, HDAC activity is required for antiaggregation.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRMS1Q9HCU92EBI-1053164,EBI-714781
    DYSFO759232EBI-1053164,EBI-2799016
    KRT18P057836EBI-1053164,EBI-297888
    MLF1P583402EBI-1053164,EBI-721328
    MLF2Q157733EBI-1053164,EBI-1051875
    SGCGQ133262EBI-1053164,EBI-5357343

    Protein-protein interaction databases

    BioGridi115360. 21 interactions.
    IntActiO75190. 38 interactions.
    MINTiMINT-4713234.

    Structurei

    3D structure databases

    ProteinModelPortaliO75190.
    SMRiO75190. Positions 1-105.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 6968JPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 146145Interaction with HSP70Add
    BLAST
    Regioni119 – 242124Interaction with KRT18Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi83 – 17290Gly/Phe-richAdd
    BLAST
    Compositional biasi155 – 19440Ser-richAdd
    BLAST

    Domaini

    The antiaggregation activity of isoform B resides in the serine-rich region and the C-terminus.

    Sequence similaritiesi

    Contains 1 J domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0484.
    HOVERGENiHBG066998.
    InParanoidiO75190.
    KOiK09512.
    OMAiNPFEFGF.
    PhylomeDBiO75190.
    TreeFamiTF105142.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    InterProiIPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    [Graphical view]
    PfamiPF00226. DnaJ. 1 hit.
    [Graphical view]
    PRINTSiPR00625. JDOMAIN.
    SMARTiSM00271. DnaJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46565. SSF46565. 1 hit.
    PROSITEiPS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: O75190-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVDYYEVLGV QRHASPEDIK KAYRKLALKW HPDKNPENKE EAERKFKQVA    50
    EAYEVLSDAK KRDIYDKYGK EGLNGGGGGG SHFDSPFEFG FTFRNPDDVF 100
    REFFGGRDPF SFDFFEDPFE DFFGNRRGPR GSRSRGTGSF FSAFSGFPSF 150
    GSGFSSFDTG FTSFGSLGHG GLTSFSSTSF GGSGMGNFKS ISTSTKMVNG 200
    RKITTKRIVE NGQERVEVEE DGQLKSLTIN GVADDDALAE ERMRRGQNAL 250
    PAQPAGLRPP KPPRPASLLR HAPHCLSEEE GEQDRPRAPG PWDPLASAAG 300
    LKEGGKRKKQ KQREESKKKK STKGNH 326
    Length:326
    Mass (Da):36,087
    Last modified:October 18, 2001 - v2
    Checksum:iECF1628BF7A524F3
    GO
    Isoform B (identifier: O75190-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         232-241: VADDDALAEE → KEQLLRLDNK
         242-326: Missing.

    Show »
    Length:241
    Mass (Da):26,900
    Checksum:iCD5A49CAB66C2E16
    GO
    Isoform C (identifier: O75190-3) [UniParc]FASTAAdd to Basket

    Also known as: a

    The sequence of this isoform differs from the canonical sequence as follows:
         301-326: LKEGGKRKKQKQREESKKKKSTKGNH → VQREAAVEQAQSETSLGARGQRGHK

    Note: No experimental confirmation available.

    Show »
    Length:325
    Mass (Da):35,714
    Checksum:i01F47DA9A87EBC74
    GO
    Isoform D (identifier: O75190-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDA → MPHPRILKRP

    Note: No experimental confirmation available.

    Show »
    Length:277
    Mass (Da):30,369
    Checksum:i97C70A8C1DF2CACC
    GO

    Sequence cautioni

    The sequence AAD16010.1 differs from that shown. Reason: Frameshift at position 197.
    The sequence BAD93096.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281G → S in BAD97321. 1 PublicationCurated
    Sequence conflicti303 – 3031E → G in BAF85714. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891F → I in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. 1 Publication
    VAR_067833
    Natural varianti93 – 931F → L in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. 2 Publications
    VAR_067834
    Natural varianti96 – 961P → R in LGMD1E. 1 Publication
    VAR_067835

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5959MVDYY…VLSDA → MPHPRILKRP in isoform D. CuratedVSP_053894Add
    BLAST
    Alternative sequencei232 – 24110VADDDALAEE → KEQLLRLDNK in isoform B. 10 PublicationsVSP_001289
    Alternative sequencei242 – 32685Missing in isoform B. 10 PublicationsVSP_001290Add
    BLAST
    Alternative sequencei301 – 32626LKEGG…TKGNH → VQREAAVEQAQSETSLGARG QRGHK in isoform C. 4 PublicationsVSP_026180Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF080569 mRNA. Translation: AAD16010.1. Frameshift.
    AB015798 mRNA. Translation: BAA88769.1.
    AB015799 mRNA. Translation: BAA88770.1.
    AF060703 mRNA. Translation: AAF21257.1.
    AB014888 mRNA. Translation: BAA32209.1.
    AF075601 mRNA. Translation: AAD43194.1.
    CR533498 mRNA. Translation: CAG38529.1.
    AB209859 mRNA. Translation: BAD93096.1. Different initiation.
    AK223601 mRNA. Translation: BAD97321.1.
    AK291953 mRNA. Translation: BAF84642.1.
    AK293025 mRNA. Translation: BAF85714.1.
    AK297796 mRNA. Translation: BAG60135.1.
    AL136707 mRNA. Translation: CAB66642.1.
    AC006372 Genomic DNA. No translation available.
    AC079306 Genomic DNA. Translation: AAS07392.1.
    AC079306 Genomic DNA. Translation: AAS07393.1.
    CH236954 Genomic DNA. Translation: EAL23923.1.
    CH236954 Genomic DNA. Translation: EAL23924.1.
    CH471149 Genomic DNA. Translation: EAX04570.1.
    BC000177 mRNA. Translation: AAH00177.1.
    BC002446 mRNA. Translation: AAH02446.1.
    CCDSiCCDS47755.1. [O75190-2]
    CCDS5946.1. [O75190-1]
    RefSeqiNP_005485.1. NM_005494.2. [O75190-2]
    NP_490647.1. NM_058246.3. [O75190-1]
    UniGeneiHs.188591.
    Hs.490745.

    Genome annotation databases

    EnsembliENST00000262177; ENSP00000262177; ENSG00000105993. [O75190-1]
    ENST00000429029; ENSP00000397556; ENSG00000105993. [O75190-2]
    GeneIDi10049.
    KEGGihsa:10049.
    UCSCiuc003wnj.3. human. [O75190-2]
    uc003wnk.3. human. [O75190-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF080569 mRNA. Translation: AAD16010.1 . Frameshift.
    AB015798 mRNA. Translation: BAA88769.1 .
    AB015799 mRNA. Translation: BAA88770.1 .
    AF060703 mRNA. Translation: AAF21257.1 .
    AB014888 mRNA. Translation: BAA32209.1 .
    AF075601 mRNA. Translation: AAD43194.1 .
    CR533498 mRNA. Translation: CAG38529.1 .
    AB209859 mRNA. Translation: BAD93096.1 . Different initiation.
    AK223601 mRNA. Translation: BAD97321.1 .
    AK291953 mRNA. Translation: BAF84642.1 .
    AK293025 mRNA. Translation: BAF85714.1 .
    AK297796 mRNA. Translation: BAG60135.1 .
    AL136707 mRNA. Translation: CAB66642.1 .
    AC006372 Genomic DNA. No translation available.
    AC079306 Genomic DNA. Translation: AAS07392.1 .
    AC079306 Genomic DNA. Translation: AAS07393.1 .
    CH236954 Genomic DNA. Translation: EAL23923.1 .
    CH236954 Genomic DNA. Translation: EAL23924.1 .
    CH471149 Genomic DNA. Translation: EAX04570.1 .
    BC000177 mRNA. Translation: AAH00177.1 .
    BC002446 mRNA. Translation: AAH02446.1 .
    CCDSi CCDS47755.1. [O75190-2 ]
    CCDS5946.1. [O75190-1 ]
    RefSeqi NP_005485.1. NM_005494.2. [O75190-2 ]
    NP_490647.1. NM_058246.3. [O75190-1 ]
    UniGenei Hs.188591.
    Hs.490745.

    3D structure databases

    ProteinModelPortali O75190.
    SMRi O75190. Positions 1-105.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115360. 21 interactions.
    IntActi O75190. 38 interactions.
    MINTi MINT-4713234.

    PTM databases

    PhosphoSitei O75190.

    Proteomic databases

    MaxQBi O75190.
    PaxDbi O75190.
    PRIDEi O75190.

    Protocols and materials databases

    DNASUi 10049.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262177 ; ENSP00000262177 ; ENSG00000105993 . [O75190-1 ]
    ENST00000429029 ; ENSP00000397556 ; ENSG00000105993 . [O75190-2 ]
    GeneIDi 10049.
    KEGGi hsa:10049.
    UCSCi uc003wnj.3. human. [O75190-2 ]
    uc003wnk.3. human. [O75190-1 ]

    Organism-specific databases

    CTDi 10049.
    GeneCardsi GC07P157128.
    GeneReviewsi DNAJB6.
    HGNCi HGNC:14888. DNAJB6.
    HPAi CAB004670.
    HPA024258.
    MIMi 603511. phenotype.
    611332. gene.
    neXtProti NX_O75190.
    Orphaneti 34516. Autosomal dominant limb-girdle muscular dystrophy type 1D.
    PharmGKBi PA27418.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0484.
    HOVERGENi HBG066998.
    InParanoidi O75190.
    KOi K09512.
    OMAi NPFEFGF.
    PhylomeDBi O75190.
    TreeFami TF105142.

    Miscellaneous databases

    ChiTaRSi DNAJB6. human.
    GeneWikii DNAJB6.
    GenomeRNAii 10049.
    NextBioi 35464742.
    PROi O75190.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75190.
    Bgeei O75190.
    CleanExi HS_DNAJB6.
    Genevestigatori O75190.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    InterProi IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    [Graphical view ]
    Pfami PF00226. DnaJ. 1 hit.
    [Graphical view ]
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    PROSITEi PS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells."
      Pei L.
      J. Biol. Chem. 274:3151-3158(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), INTERACTION WITH PTTG, TISSUE SPECIFICITY.
      Tissue: Testis.
    2. "Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently."
      Chuang J.-Z., Zhou H., Zhu M., Li S.-H., Li X.-J., Sung C.-H.
      J. Biol. Chem. 277:19831-19838(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY.
    3. "Characterization of two isoforms of a human DnaJ homologue, HSJ2."
      Hanai R., Mashima K.
      Mol. Biol. Rep. 30:149-153(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
    4. Zhang J.S., Nelson M., Wang L., Smith D.I.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
      Tissue: Pancreas.
    5. "Cloning, tissue expression, and chromosomal assignment of human MRJ gene for a member of the DNAJ protein family."
      Seki N., Hattori A., Hayashi A., Kozuma S., Miyajima N., Saito T.
      J. Hum. Genet. 44:185-189(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), TISSUE SPECIFICITY.
      Tissue: Testis.
    6. "HSJ2, a novel human homologue of the bacterial heat-shock protein DnaJ."
      Zhang W., Wan T., Yuan Z., Cao X.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    7. "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] (ISOFORM B).
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; B AND C).
      Tissue: Uterus.
    9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
      Tissue: Aortic endothelium and Kidney.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
      Tissue: Fetal kidney.
    11. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    14. "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] (ISOFORMS A AND B).
      Tissue: Placenta and Skin.
    15. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 48-60; 71-101; 208-242 AND 271-287, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    16. "Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein."
      Izawa I., Nishizawa M., Ohtakara K., Ohtsuka K., Inada H., Inagaki M.
      J. Biol. Chem. 275:34521-34527(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSP70 AND KRT18, SUBCELLULAR LOCATION.
    17. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation."
      Hageman J., Rujano M.A., van Waarde M.A., Kakkar V., Dirks R.P., Govorukhina N., Oosterveld-Hut H.M., Lubsen N.H., Kampinga H.H.
      Mol. Cell 37:355-369(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS SUPPRESSOR OF PROTEIN AGGREGATION.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: FUNCTION IN INHIBITION OF HUNTINGTIN AGGREGATION, SUBUNIT, INTERACTION WITH BAG3; HSPB8 AND STUB1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANTS LGMD1E ILE-89 AND LEU-93, CHARACTERIZATION OF VARIANTS LGMD1E ILE-89 AND LEU-93.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Exome sequencing reveals DNAJB6 mutations in dominantly-inherited myopathy."
      Harms M.B., Sommerville R.B., Allred P., Bell S., Ma D., Cooper P., Lopate G., Pestronk A., Weihl C.C., Baloh R.H.
      Ann. Neurol. 71:407-416(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LGMD1E LEU-93 AND ARG-96.

    Entry informationi

    Entry nameiDNJB6_HUMAN
    AccessioniPrimary (citable) accession number: O75190
    Secondary accession number(s): A4D232
    , A8K7D8, A8KAG0, B4DN73, E9PCZ2, O95806, Q53EN8, Q59EF2, Q6FIC8, Q75MA2, Q9UIK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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