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UniProtKB/Swiss-Prot entry O75190


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DNJB6_HUMAN
Primary accession number O75190
Secondary accession numbers A4D232 O95806 Q53EN8 Q59EF2 Q6FIC8 Q75MA2 Q9UIK6
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on October 18, 2001 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 83)
Name and origin of the protein
Protein name DnaJ homolog subfamily B member 6
Synonyms Heat shock protein J2
HSJ-2
MSJ-1
HHDJ1
MRJ
Gene name
Name: DNAJB6
Synonyms: HSJ2, MRJ, MSJ1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), INTERACTION WITH PTTG, AND TISSUE SPECIFICITY.
TISSUE=Testis;
DOI=10.1074/jbc.274.5.3151; PubMed=9915854 [NCBI, ExPASy, EBI, Israel, Japan]
Pei L.;
"Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells.";
J. Biol. Chem. 274:3151-3158(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M109613200; PubMed=11896048 [NCBI, ExPASy, EBI, Israel, Japan]
Chuang J.-Z., Zhou H., Zhu M., Li S.-H., Li X.-J., Sung C.-H.;
"Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently.";
J. Biol. Chem. 277:19831-19838(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
DOI=10.1023/A:1024916223616; PubMed=12974469 [NCBI, ExPASy, EBI, Israel, Japan]
Hanai R., Mashima K.;
"Characterization of two isoforms of a human DnaJ homologue, HSJ2.";
Mol. Biol. Rep. 30:149-153(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Pancreas;
Zhang J.S., Nelson M., Wang L., Smith D.I.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND TISSUE SPECIFICITY.
TISSUE=Testis;
DOI=10.1007/s100380050139; PubMed=10319584 [NCBI, ExPASy, EBI, Israel, Japan]
Seki N., Hattori A., Hayashi A., Kozuma S., Miyajima N., Saito T.;
"Cloning, tissue expression, and chromosomal assignment of human MRJ gene for a member of the DNAJ protein family.";
J. Hum. Genet. 44:185-189(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Zhang W., Wan T., Yuan Z., Cao X.;
"HSJ2, a novel human homologue of the bacterial heat-shock protein DnaJ.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
TISSUE=Aortic endothelium, and Kidney;
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Fetal kidney;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1083423; PubMed=12690205 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
TISSUE=Placenta, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
PROTEIN SEQUENCE OF 2-12; 48-60; 71-101; 208-242 AND 271-287, CLEAVAGE OF INITIATOR METHIONINE, LACK OF N-TERMINAL ACETYLATION, AND MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[14]
FUNCTION, INTERACTION WITH HSP70 AND KRT18, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M003492200; PubMed=10954706 [NCBI, ExPASy, EBI, Israel, Japan]
Izawa I., Nishizawa M., Ohtakara K., Ohtsuka K., Inada H., Inagaki M.;
"Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein.";
J. Biol. Chem. 275:34521-34527(2000).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. 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. Reduces huntingtin aggregation associated with HD. Also reduces cellular toxicity and caspase-3 activity.
  • SUBUNIT: Interacts with HSP70, KRT18 and PTTG.
  • INTERACTION:
    Q9HCU9:BRMS1; NbExp=1; IntAct=EBI-1053164, EBI-714781;
    P05783:KRT18; NbExp=3; IntAct=EBI-1053164, EBI-297888;
  • SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    NameA
    Isoform IDO75190-1
    This is the isoform sequence displayed in this entry.
    NameB
    Isoform IDO75190-2
    Features which should be applied to build the isoform sequence: VSP_001289, VSP_001290.
    NameC
    Synonymsa
    Isoform IDO75190-3
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_026180.
  • TISSUE SPECIFICITY: 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.
  • SIMILARITY: Contains 1 J domain.
  • SEQUENCE CAUTION:
    • Sequence=AAD16010.1; Type=Frameshift; Positions=197;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF080569; AAD16010.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB015798; BAA88769.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB015799; BAA88770.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF060703; AAF21257.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB014888; BAA32209.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF075601; AAD43194.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR533498; CAG38529.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209859; BAD93096.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223601; BAD97321.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136707; CAB66642.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC079306; AAS07392.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC079306; AAS07393.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH236954; EAL23923.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH236954; EAL23924.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000177; AAH00177.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002446; AAH02446.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00024523; -.
IPI00098523; -.
IPI00556073; -.
RefSeq NP_005485.1; -.
NP_490647.1; -.
UniGene Hs.490745
3D structure databases
HSSP P25685; 1HDJ. [HSSP ENTRY / PDB]
SMR O75190; 1-69.
ModBase O75190.
Protein-protein interaction databases
IntAct O75190; 9.
PTM databases
PhosphoSite O75190; -.
Organism-specific databases
GeneCards GC07P156822; -.
H-InvDB HIX0000154; -.
HIX0007259; -.
HIX0041121; -.
HGNC HGNC:14888; DNAJB6.
GenAtlas DNAJB6.
HPA CAB004670; -.
MIM 611332; gene. [NCBI / EBI]
PharmGKB PA27418; -.
Gene expression databases
ArrayExpress O75190; -.
Bgee O75190; -.
CleanEx HS_DNAJB6; -.
GermOnline ENSG00000105993; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0001671; Molecular function: ATPase activator activity (inferred from direct assay from UniProtKB).
GO:0051087; Molecular function: chaperone binding (inferred from direct assay from UniProtKB).
GO:0031072; Molecular function: heat shock protein binding (inferred from physical interaction from UniProtKB).
GO:0045109; Biological process: intermediate filament organization (inferred from direct assay from UniProtKB).
GO:0043154; Biological process: negative regulation of caspase activity (inferred from direct assay from UniProtKB).
GO:0006457; Biological process: protein folding (inferred from direct assay from UniProtKB).
GO:0006986; Biological process: response to unfolded protein (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001623; DnaJ_N.
IPR018253; Heat_shock_DnaJ_CS.
IPR015609; Hsp40/DnaJ_Rel.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
PANTHER PTHR11821; Hsp40/DnaJ_Rel; 1.
Pfam PF00226; DnaJ; 1.
Pfam graphical view of domain structure.
SMART SM00271; DnaJ; 1.
SMART graphical view of domain structure.
PROSITE PS00636; DNAJ_1; 1.
PS50076; DNAJ_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O75190; -.
Genome annotation databases
Ensembl ENSG00000105993; Homo sapiens. [Contig view]
GeneID 10049; -.
KEGG hsa:10049; -.
Phylogenomic databases
HOVERGEN O75190; -.
OMA O75190; NALPAQP.
Other
NextBio 37959; -.
SOURCE DNAJB6; Homo sapiens.
ProtoNet O75190.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Chaperone; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   326  325     DnaJ homolog subfamily B member 6. PRO_0000071025
DOMAIN   2    69  68     J. 
REGION   2   146  145     Interaction with HSP70. 
REGION   119   242  124     Interaction with KRT18. 
COMPBIAS   83   172  90     Gly/Phe-rich. 
MOD_RES   277   277        Phosphoserine. 
VAR_SEQ   232   241        VADDDALAEE -> KEQLLRLDNK (in isoform B). VSP_001289
VAR_SEQ   242   326        Missing (in isoform B). VSP_001290
VAR_SEQ   301   326        LKEGGKRKKQKQREESKKKKSTKGNH -> VQREAAVEQAQSETSLGARGQRGHK (in isoform C). VSP_026180
CONFLICT   128   128        G -> S (in Ref. 8; BAD97321). 
Sequence information
Length: 326 AA [This is the length of the unprocessed precursor] Molecular weight: 36087 Da [This is the MW of the unprocessed precursor] CRC64: ECF1628BF7A524F3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVDYYEVLGV QRHASPEDIK KAYRKLALKW HPDKNPENKE EAERKFKQVA EAYEVLSDAK 

        70         80         90        100        110        120 
KRDIYDKYGK EGLNGGGGGG SHFDSPFEFG FTFRNPDDVF REFFGGRDPF SFDFFEDPFE 

       130        140        150        160        170        180 
DFFGNRRGPR GSRSRGTGSF FSAFSGFPSF GSGFSSFDTG FTSFGSLGHG GLTSFSSTSF 

       190        200        210        220        230        240 
GGSGMGNFKS ISTSTKMVNG RKITTKRIVE NGQERVEVEE DGQLKSLTIN GVADDDALAE 

       250        260        270        280        290        300 
ERMRRGQNAL PAQPAGLRPP KPPRPASLLR HAPHCLSEEE GEQDRPRAPG PWDPLASAAG 

       310        320 
LKEGGKRKKQ KQREESKKKK STKGNH 

O75190 in FASTA format

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