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O75190 (DNJB6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily B member 6
Alternative name(s):
HHDJ1
Heat shock protein J2
Short name=HSJ-2
MRJ
MSJ-1
Gene names
Name:DNAJB6
Synonyms:HSJ2, MRJ, MSJ1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.16 Ref.19 Ref.22

Subunit structure

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. Ref.1 Ref.16 Ref.22

Subcellular location

Cytoplasmperinuclear region. Nucleus. CytoplasmmyofibrilsarcomereZ line Ref.16 Ref.22.

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. Ref.1 Ref.2 Ref.5 Ref.22

Domain

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

Involvement in disease

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.
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 (Ref.22). Ref.22 Ref.24

Sequence similarities

Contains 1 J domain.

Sequence caution

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

The sequence BAD93096.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Limb-girdle muscular dystrophy
   Molecular functionChaperone
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

chorio-allantoic fusion

Inferred from electronic annotation. Source: Ensembl

chorion development

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

intermediate filament organization

Inferred from direct assay Ref.16. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of ATPase activity

Inferred from direct assay Ref.2. Source: GOC

protein folding

Inferred from direct assay Ref.2. Source: UniProtKB

protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

syncytiotrophoblast cell differentiation involved in labyrinthine layer development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from direct assay Ref.22. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionATPase activator activity

Inferred from direct assay Ref.2. Source: UniProtKB

DNA binding

Inferred from electronic annotation. Source: Ensembl

chaperone binding

Inferred from direct assay Ref.2. Source: UniProtKB

heat shock protein binding

Inferred from direct assay Ref.16. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: O75190-1)

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.
Isoform B (identifier: O75190-2)

The sequence of this isoform differs from the canonical sequence as follows:
     232-241: VADDDALAEE → KEQLLRLDNK
     242-326: Missing.
Isoform C (identifier: O75190-3)

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.
Isoform D (identifier: O75190-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDA → MPHPRILKRP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 326325DnaJ homolog subfamily B member 6
PRO_0000071025

Regions

Domain2 – 6968J
Region2 – 146145Interaction with HSP70
Region119 – 242124Interaction with KRT18
Compositional bias83 – 17290Gly/Phe-rich
Compositional bias155 – 19440Ser-rich

Amino acid modifications

Modified residue2771Phosphoserine Ref.17 Ref.21

Natural variations

Alternative sequence1 – 5959MVDYY…VLSDA → MPHPRILKRP in isoform D.
VSP_053894
Alternative sequence232 – 24110VADDDALAEE → KEQLLRLDNK in isoform B.
VSP_001289
Alternative sequence242 – 32685Missing in isoform B.
VSP_001290
Alternative sequence301 – 32626LKEGG…TKGNH → VQREAAVEQAQSETSLGARG QRGHK in isoform C.
VSP_026180
Natural variant891F → I in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. Ref.22
VAR_067833
Natural variant931F → L in LGMD1E; the mutation results in inefficient inhibition of protein aggregation by isoform B. Ref.22 Ref.24
VAR_067834
Natural variant961P → R in LGMD1E. Ref.24
VAR_067835

Experimental info

Sequence conflict1281G → S in BAD97321. Ref.9
Sequence conflict3031E → G in BAF85714. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: ECF1628BF7A524F3

FASTA32636,087
        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 

« Hide

Isoform B [UniParc].

Checksum: CD5A49CAB66C2E16
Show »

FASTA24126,900
Isoform C (a) [UniParc].

Checksum: 01F47DA9A87EBC74
Show »

FASTA32535,714
Isoform D [UniParc].

Checksum: 97C70A8C1DF2CACC
Show »

FASTA27730,369

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6 cause limb-girdle muscular dystrophy."
Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H., Screen M., McDonald K., Stajich J.M., Mahjneh I., Vihola A., Raheem O., Penttila S., Lehtinen S., Huovinen S., Palmio J., Tasca G., Ricci E., Hackman P. expand/collapse author list , Hauser M., Katsanis N., Udd B.
Nat. Genet. 44:450-455(2012) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_005485.1. NM_005494.2.
NP_490647.1. NM_058246.3.
UniGeneHs.188591.
Hs.490745.

3D structure databases

ProteinModelPortalO75190.
SMRO75190. Positions 1-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115360. 22 interactions.
IntActO75190. 26 interactions.
MINTMINT-4713234.

PTM databases

PhosphoSiteO75190.

Proteomic databases

PaxDbO75190.
PRIDEO75190.

Protocols and materials databases

DNASU10049.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262177; ENSP00000262177; ENSG00000105993. [O75190-1]
ENST00000429029; ENSP00000397556; ENSG00000105993. [O75190-2]
ENST00000452797; ENSP00000402270; ENSG00000105993.
GeneID10049.
KEGGhsa:10049.
UCSCuc003wnj.3. human. [O75190-2]
uc003wnk.3. human. [O75190-1]

Organism-specific databases

CTD10049.
GeneCardsGC07P157128.
HGNCHGNC:14888. DNAJB6.
HPACAB004670.
HPA024258.
MIM603511. phenotype.
611332. gene.
neXtProtNX_O75190.
Orphanet34516. Autosomal dominant limb-girdle muscular dystrophy type 1D.
PharmGKBPA27418.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0484.
HOVERGENHBG066998.
InParanoidO75190.
KOK09512.
OMANPFEFGF.
PhylomeDBO75190.
TreeFamTF105142.

Gene expression databases

ArrayExpressO75190.
BgeeO75190.
CleanExHS_DNAJB6.
GenevestigatorO75190.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
InterProIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNAJB6. human.
GeneWikiDNAJB6.
GenomeRNAi10049.
NextBio35464742.
PROO75190.
SOURCESearch...

Entry information

Entry nameDNJB6_HUMAN
AccessionPrimary (citable) accession number: O75190
Secondary accession number(s): A4D232 expand/collapse secondary AC list , A8K7D8, A8KAG0, B4DN73, E9PCZ2, O95806, Q53EN8, Q59EF2, Q6FIC8, Q75MA2, Q9UIK6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 18, 2001
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM