DNAJB6

From Wikipedia, the free encyclopedia

DnaJ (Hsp40) homolog, subfamily B, member 6

Identifiers

DNAJB6; HSJ2; DKFZp566D0824; FLJ42837; HHDJ1; HSJ-2; MGC1152; MGC117297; MRJ; MSJ-1

External IDs

Gene ontology
Molecular Function:	• heat shock protein binding
Cellular Component:	• cellular_component
Biological Process:	• protein folding • response to unfolded protein

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005494 (mRNA)
NP_005485 (protein)

NM_001037940 (mRNA)
NP_001033029 (protein)

Location

Chr 7: 156.84 - 156.9 Mb

Chr 5: 30.07 - 30.12 Mb

Pubmed search

[1]

[2]

DnaJ (Hsp40) homolog, subfamily B, member 6, also known as DNAJB6, is a human gene.^[1]

This gene encodes a member of the DNAJ protein family. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. This family member may also play a role in polyglutamine aggregation in specific neurons. Alternative splicing of this gene results in multiple transcript variants; however, not all variants have been fully described.^[1]

[edit] References

^ ^a ^b Entrez Gene: DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6.

[edit] Further reading

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Seki N, Hattori A, Hayashi A, et al. (1999). "Cloning, tissue expression, and chromosomal assignment of human MRJ gene for a member of the DNAJ protein family.". J. Hum. Genet. 44 (3): 185–9. PMID 10319584.
Izawa I, Nishizawa M, Ohtakara K, et al. (2000). "Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein.". J. Biol. Chem. 275 (44): 34521–7. doi:10.1074/jbc.M003492200. PMID 10954706.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. PMID 11076863.
Ohtsuka K, Hata M (2001). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature.". Cell Stress Chaperones 5 (2): 98–112. PMID 11147971.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166.
Chuang JZ, Zhou H, Zhu M, et al. (2002). "Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently.". J. Biol. Chem. 277 (22): 19831–8. doi:10.1074/jbc.M109613200. PMID 11896048.
Farinha CM, Nogueira P, Mendes F, et al. (2002). "The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70.". Biochem. J. 366 (Pt 3): 797–806. doi:10.1042/BJ20011717. PMID 12069690.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology.". Science 300 (5620): 767–72. doi:10.1126/science.1083423. PMID 12690205.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7.". Nature 424 (6945): 157–64. doi:10.1038/nature01782. PMID 12853948.
Hanai R, Mashima K (2004). "Characterization of two isoforms of a human DnaJ homologue, HSJ2.". Mol. Biol. Rep. 30 (3): 149–53. PMID 12974469.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Liu Y, Zhu MC, Wang YJ, et al. (2004). "[Cloning of a DnaJ homolog chaperon PBP and its subcellular localization]". Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 19 (6): 531–4. PMID 15182641.
Berruti G, Martegani E (2005). "The deubiquitinating enzyme mUBPy interacts with the sperm-specific molecular chaperone MSJ-1: the relation with the proteasome, acrosome, and centrosome in mouse male germ cells.". Biol. Reprod. 72 (1): 14–21. doi:10.1095/biolreprod.104.030866. PMID 15342353.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMID 15489336.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Dai YS, Xu J, Molkentin JD (2005). "The DnaJ-related factor Mrj interacts with nuclear factor of activated T cells c3 and mediates transcriptional repression through class II histone deacetylase recruitment.". Mol. Cell. Biol. 25 (22): 9936–48. doi:10.1128/MCB.25.22.9936-9948.2005. PMID 16260608.