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{{Infobox_gene}}
{{PBB_Controls
'''DnaJ homolog subfamily B member 6''' is a [[protein]] that in humans is encoded by the ''DNAJB6'' [[gene]].<ref name="pmid10319584">{{cite journal |vauthors=Seki N, Hattori A, Hayashi A, Kozuma S, Miyajima N, Saito T | title = Cloning, tissue expression, and chromosomal assignment of human MRJ gene for a member of the DNAJ protein family | journal = J Hum Genet | volume = 44 | issue = 3 | pages = 185–9 |date=June 1999 | pmid = 10319584 | pmc =  | doi = 10.1007/s100380050139 }}</ref><ref name="pmid9915854">{{cite journal | author = Pei L | title = Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells | journal = J Biol Chem | volume = 274 | issue = 5 | pages = 3151–8 |date=March 1999 | pmid = 9915854 | pmc = | doi =10.1074/jbc.274.5.3151  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10049| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = DnaJ (Hsp40) homolog, subfamily B, member 6
| HGNCid = 14888
| Symbol = DNAJB6
| AltSymbols =; HSJ2; DKFZp566D0824; FLJ42837; HHDJ1; HSJ-2; MGC1152; MGC117297; MRJ; MSJ-1
| OMIM = 
| ECnumber = 
| Homologene = 38058
| MGIid = 1344381
| GeneAtlas_image1 = PBB_GE_DNAJB6_208811_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DNAJB6_209015_s_at_tn.png
| Function = {{GNF_GO|id=GO:0031072 |text = heat shock protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10049
    | Hs_Ensembl = ENSG00000105993
    | Hs_RefseqProtein = NP_005485
    | Hs_RefseqmRNA = NM_005494
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 156844025
    | Hs_GenLoc_end = 156901553
    | Hs_Uniprot = O75190
    | Mm_EntrezGene = 23950
    | Mm_Ensembl = ENSMUSG00000029131
    | Mm_RefseqmRNA = NM_001037940
    | Mm_RefseqProtein = NP_001033029
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 30066776
    | Mm_GenLoc_end = 30117245
    | Mm_Uniprot = Q3TE94
  }}
}}
'''DnaJ (Hsp40) homolog, subfamily B, member 6''', also known as '''DNAJB6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10049| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10049| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
DNAJB6 has been shown to [[Protein-protein interaction|interact]] with [[Keratin 18]].<ref name="pmid10954706">{{cite journal |vauthors=Izawa I, Nishizawa M, Ohtakara K, Ohtsuka K, Inada H, Inagaki M | title = Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein | journal = J. Biol. Chem. | volume = 275 | issue = 44 | pages = 34521–7 | year = 2000 | pmid = 10954706 | doi = 10.1074/jbc.M003492200 }}</ref> It has been also shown that the aggregation of Aβ42 (a process involved in e.g. Alzheimer's disease) is retarded by DNAJB6 in a concentration-dependent manner, extending to very low sub-stoichiometric molar ratios of chaperone to peptide.<ref name="pmid25217638">{{cite journal |author1=Månsson, C |author2=Arosio, P |author3=Hussein, R |author4=Kampinga, H H |author5=Hashem, R M |author6=Boelens, W C |author7=Emanuelsson, C | title = Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation. | journal = J. Biol. Chem. | volume = 289 | issue = 45 | pages = 31066–76 | year = 2014 | pmid = 25217638 | doi =10.1074/jbc.M114.595124 | pmc=4223311}}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
| citations =
*{{cite journal  | author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |name-list-format=vanc| author2=Yoshitomo-Nakagawa K | author3=Maruyama K  | display-authors=3  | last4=Suyama  | first4=Akira  | last5=Sugano  | first5=Sumio }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | author=Izawa I |title=Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34521–7 |year= 2000 |pmid= 10954706 |doi= 10.1074/jbc.M003492200  |name-list-format=vanc| author2=Nishizawa M  | author3=Ohtakara K  | display-authors=3  | last4=Ohtsuka  | first4=K  | last5=Inada  | first5=H  | last6=Inagaki  | first6=M }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948  }}
*{{cite journal | author=Seki N, Hattori A, Hayashi A, ''et al.'' |title=Cloning, tissue expression, and chromosomal assignment of human MRJ gene for a member of the DNAJ protein family. |journal=J. Hum. Genet. |volume=44 |issue= 3 |pages= 185-9 |year= 1999 |pmid= 10319584 |doi=  }}
*{{cite journal  |vauthors=Ohtsuka K, Hata M |title=Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature |journal=Cell Stress Chaperones |volume=5 |issue= 2 |pages= 98–112 |year= 2001 |pmid= 11147971 |doi=10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2  | pmc=312896  | issn=1466-1268  }}
*{{cite journal  | author=Izawa I, Nishizawa M, Ohtakara K, ''et al.'' |title=Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein. |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34521-7 |year= 2000 |pmid= 10954706 |doi= 10.1074/jbc.M003492200 }}
*{{cite journal  | author=Wiemann S |title=Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R | pmc=311072  |name-list-format=vanc| author2=Weil B  | author3=Wellenreuther R  | display-authors=3  | last4=Gassenhuber  | first4=J | last5=Glassl  | first5=S  | last6=Ansorge  | first6=W  | last7=Böcher  | first7=M  | last8=Blöcker  | first8=H  | last9=Bauersachs  | first9=S }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | author=Chuang JZ |title=Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19831–8 |year= 2002 |pmid= 11896048 |doi= 10.1074/jbc.M109613200 |name-list-format=vanc| author2=Zhou H  | author3=Zhu M  | display-authors=3  | last4=Li  | first4=SH  | last5=Li  | first5=XJ  | last6=Sung  | first6=CH }}
*{{cite journal  | author=Ohtsuka K, Hata M |title=Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature. |journal=Cell Stress Chaperones |volume=5 |issue= 2 |pages= 98-112 |year= 2001 |pmid= 11147971 |doi= }}
*{{cite journal  | author=Farinha CM |title=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 |journal=Biochem. J. |volume=366 |issue= Pt 3 |pages= 797–806 |year= 2002 |pmid= 12069690 |doi= 10.1042/BJ20011717  | pmc=1222832  |name-list-format=vanc| author2=Nogueira P  | author3=Mendes F  | display-authors=3  | last4=Penque  | first4=Deborah  | last5=Amaral | first5=Margarida }}
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD | last6=Collins | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Chuang JZ, Zhou H, Zhu M, ''et al.'' |title=Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19831-8 |year= 2002 |pmid= 11896048 |doi= 10.1074/jbc.M109613200 }}
*{{cite journal  | author=Scherer SW |title=Human Chromosome 7: DNA Sequence and Biology |journal=Science |volume=300 |issue= 5620 |pages= 767–72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423  | pmc=2882961 |name-list-format=vanc| author2=Cheung J  | author3=MacDonald JR  | display-authors=3  | last4=Osborne  | first4=LR  | last5=Nakabayashi  | first5=K  | last6=Herbrick  | first6=JA  | last7=Carson  | first7=AR  | last8=Parker-Katiraee  | first8=L  | last9=Skaug  | first9=J }}
*{{cite journal | author=Farinha CM, Nogueira P, Mendes F, ''et al.'' |title=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. |journal=Biochem. J. |volume=366 |issue= Pt 3 |pages= 797-806 |year= 2002 |pmid= 12069690 |doi= 10.1042/BJ20011717 }}
*{{cite journal  | author=Hillier LW |title=The DNA sequence of human chromosome 7 |journal=Nature |volume=424 |issue= 6945 |pages= 157–64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 |name-list-format=vanc| author2=Fulton RS  | author3=Fulton LA  | display-authors=3  | last4=Graves  | first4=Tina A.  | last5=Pepin  | first5=Kymberlie H.  | last6=Wagner-Mcpherson  | first6=Caryn  | last7=Layman | first7=Dan  | last8=Maas  | first8=Jason  | last9=Jaeger  | first9=Sara }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Hanai R, Mashima K |title=Characterization of two isoforms of a human DnaJ homologue, HSJ2 |journal=Mol. Biol. Rep. |volume=30 |issue= 3 |pages= 149–53 |year= 2004 |pmid= 12974469 |doi=10.1023/A:1024916223616  }}
*{{cite journal | author=Scherer SW, Cheung J, MacDonald JR, ''et al.'' |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767-72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423 }}
*{{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285  |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{cite journal  | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal  | author=Liu Y |title=[Cloning of a DnaJ homolog chaperon PBP and its subcellular localization] |journal=Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi |volume=19 |issue= 6 |pages= 531–4 |year= 2004 |pmid= 15182641 |doi=  |name-list-format=vanc| author2=Zhu MC  | author3=Wang YJ  | display-authors=3  | last4=Zhan  | first4=Z  | last5=Liu  | first5=CG  }}
*{{cite journal | author=Hanai R, Mashima K |title=Characterization of two isoforms of a human DnaJ homologue, HSJ2. |journal=Mol. Biol. Rep. |volume=30 |issue= 3 |pages= 149-53 |year= 2004 |pmid= 12974469 |doi=  }}
*{{cite journal  |vauthors=Berruti G, Martegani E |title=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 |journal=Biol. Reprod. |volume=72 |issue= 1 |pages= 14–21 |year= 2005 |pmid= 15342353 |doi= 10.1095/biolreprod.104.030866 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334  | pmc=528928 |doi= 10.1101/gr.2596504  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal | author=Liu Y, Zhu MC, Wang YJ, ''et al.'' |title=[Cloning of a DnaJ homolog chaperon PBP and its subcellular localization] |journal=Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi |volume=19 |issue= 6 |pages= 531-4 |year= 2004 |pmid= 15182641 |doi=  }}
*{{cite journal  | author=Wiemann S |title=From ORFeome to Biology: A Functional Genomics Pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336  | pmc=528930 |doi= 10.1101/gr.2576704  |name-list-format=vanc| author2=Arlt D  | author3=Huber W  | display-authors=3  | last4=Wellenreuther  | first4=R  | last5=Schleeger  | first5=S  | last6=Mehrle  | first6=A  | last7=Bechtel  | first7=S  | last8=Sauermann  | first8=M  | last9=Korf  | first9=U }}
*{{cite journal | author=Berruti G, Martegani E |title=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. |journal=Biol. Reprod. |volume=72 |issue= 1 |pages= 14-21 |year= 2005 |pmid= 15342353 |doi= 10.1095/biolreprod.104.030866 }}
*{{cite journal  | author=Rual JF |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209  |name-list-format=vanc| author2=Venkatesan K  | author3=Hao T  | display-authors=3  | last4=Hirozane-Kishikawa  | first4=Tomoko  | last5=Dricot  | first5=Amélie  | last6=Li  | first6=Ning  | last7=Berriz  | first7=Gabriel F.  | last8=Gibbons  | first8=Francis D.  | last9=Dreze  | first9=Matija }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  |vauthors=Dai YS, Xu J, Molkentin JD |title=The DnaJ-Related Factor Mrj Interacts with Nuclear Factor of Activated T Cells c3 and Mediates Transcriptional Repression through Class II Histone Deacetylase Recruitment |journal=Mol. Cell. Biol. |volume=25 |issue= 22 |pages= 9936–48 |year= 2005 |pmid= 16260608 |doi= 10.1128/MCB.25.22.9936-9948.2005  | pmc=1280278 }}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal | author=Dai YS, Xu J, Molkentin JD |title=The DnaJ-related factor Mrj interacts with nuclear factor of activated T cells c3 and mediates transcriptional repression through class II histone deacetylase recruitment. |journal=Mol. Cell. Biol. |volume=25 |issue= 22 |pages= 9936-48 |year= 2005 |pmid= 16260608 |doi= 10.1128/MCB.25.22.9936-9948.2005 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC genome browser|DNAJB6}}
* {{UCSC gene details|DNAJB6}}
 
{{Chaperones}}
 
[[Category:Heat shock proteins]]
[[Category:Co-chaperones]]

Latest revision as of 15:37, 18 October 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

DnaJ homolog subfamily B member 6 is a protein that in humans is encoded by the DNAJB6 gene.[1][2][3]

Function

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.[3]

Interactions

DNAJB6 has been shown to interact with Keratin 18.[4] It has been also shown that the aggregation of Aβ42 (a process involved in e.g. Alzheimer's disease) is retarded by DNAJB6 in a concentration-dependent manner, extending to very low sub-stoichiometric molar ratios of chaperone to peptide.[5]

References

  1. ↑ Seki N, Hattori A, Hayashi A, Kozuma S, Miyajima N, Saito T (June 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. doi:10.1007/s100380050139. PMID 10319584.
  2. ↑ Pei L (March 1999). "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells". J Biol Chem. 274 (5): 3151–8. doi:10.1074/jbc.274.5.3151. PMID 9915854.
  3. ↑ 3.0 3.1 "Entrez Gene: DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6".
  4. ↑ Izawa I, Nishizawa M, Ohtakara K, Ohtsuka K, Inada H, Inagaki M (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.
  5. ↑ Månsson, C; Arosio, P; Hussein, R; Kampinga, H H; Hashem, R M; Boelens, W C; Emanuelsson, C (2014). "Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation". J. Biol. Chem. 289 (45): 31066–76. doi:10.1074/jbc.M114.595124. PMC 4223311. PMID 25217638.

Further reading

External links

Retrieved from "https://www.wikidoc.org/index.php?title=DNAJB6&oldid=1533754"