DnaJ homolog subfamily B member 6 is a protein that in humans is encoded by the DNAJB6 gene.

DNAJB6
Identifiers
AliasesDNAJB6, Dnajb6, Mrj, mDj4, DJ4, DnaJ, HHDJ1, HSJ-2, HSJ2, LGMD1D, LGMD1E, MSJ-1, DnaJ heat shock protein family (Hsp40) member B6, LGMDD1
External IDsOMIM: 611332; MGI: 1344381; HomoloGene: 38058; GeneCards: DNAJB6; OMA:DNAJB6 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005494
NM_058246
NM_001363676

RefSeq (protein)

NP_005485
NP_490647
NP_001350605

Location (UCSC)Chr 7: 157.34 – 157.42 MbChr 5: 29.94 – 30.02 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

[5][6][7]

Function

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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.[7]

Interactions

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DNAJB6 has been shown to interact with keratin 18.[8] 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.[9] Dominant mutations in DNAJB6 have also been found to cause a late-onset muscle disease termed limb-girdle muscular dystrophy type D1 (LGMDD1), which is characterized by protein aggregation and vacuolar myopathology.[10]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105993Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029131Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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". Journal of Human Genetics. 44 (3): 185–9. doi:10.1007/s100380050139. PMID 10319584.
  6. ^ Pei L (January 1999). "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells". The Journal of Biological Chemistry. 274 (5): 3151–8. doi:10.1074/jbc.274.5.3151. PMID 9915854.
  7. ^ a b "Entrez Gene: DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6".
  8. ^ Izawa I, Nishizawa M, Ohtakara K, Ohtsuka K, Inada H, Inagaki M (November 2000). "Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein". The Journal of Biological Chemistry. 275 (44): 34521–7. doi:10.1074/jbc.M003492200. PMID 10954706.
  9. ^ Månsson C, Arosio P, Hussein R, Kampinga HH, Hashem RM, Boelens WC, Dobson CM, Knowles TP, Linse S, Emanuelsson C (November 2014). "Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation". The Journal of Biological Chemistry. 289 (45): 31066–76. doi:10.1074/jbc.M114.595124. PMC 4223311. PMID 25217638.
  10. ^ Bengoechea R, Findlay AR, Bhadra AK, Shao H, Stein KC, Pittman SK, Daw JA, Gestwicki JE, True HL, Weihl CC (August 2020). "Inhibition of DNAJ-HSP70 interaction improves strength in muscular dystrophy". The Journal of Clinical Investigation. 130 (8): 4470–4485. doi:10.1172/JCI136167. PMC 7410071. PMID 32427588.

Further reading

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