DNAJB6

Protein-coding gene in the species Homo sapiens
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
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for DNAJB6
Genomic location for DNAJB6
Band7q36.3Start157,335,381 bp[1]
End157,417,439 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for DNAJB6
Genomic location for DNAJB6
Band5|5 B1Start29,940,686 bp[2]
End30,023,132 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gonad

  • ganglionic eminence

  • gastrocnemius muscle

  • skin of abdomen

  • muscle of thigh

  • skin of leg

  • C1 segment

  • popliteal artery

  • tibial arteries

  • ventricular zone
Top expressed in
  • zygote

  • spermatocyte

  • spermatid

  • morula

  • neural layer of retina

  • primary visual cortex

  • superior frontal gyrus

  • dentate gyrus of hippocampal formation granule cell

  • seminiferous tubule

  • muscle of thigh
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • chaperone binding
  • heat shock protein binding
  • unfolded protein binding
  • protein binding
  • ATPase activator activity
  • identical protein binding
  • DNA binding
Cellular component
  • cytoplasm
  • cytosol
  • membrane
  • nucleoplasm
  • Z disc
  • perinuclear region of cytoplasm
  • nucleus
Biological process
  • intermediate filament organization
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
  • negative regulation of inclusion body assembly
  • regulation of protein localization
  • protein folding
  • regulation of cellular response to heat
  • positive regulation of ATP-dependent activity
  • actin cytoskeleton organization
  • extracellular matrix organization
  • protein localization to nucleus
  • negative regulation of transcription, DNA-templated
  • chorio-allantoic fusion
  • syncytiotrophoblast cell differentiation involved in labyrinthine layer development
  • chorion development
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10049

23950

Ensembl

ENSG00000105993

ENSMUSG00000029131

UniProt

O75190

O54946

RefSeq (mRNA)

NM_005494
NM_058246
NM_001363676

NM_001037940
NM_001037941
NM_001127367
NM_011847
NM_001359198

NM_001378835

RefSeq (protein)

NP_005485
NP_490647
NP_001350605

NP_001033029
NP_001033030
NP_001120839
NP_035977
NP_001346127

NP_001365764

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

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

[5][6][7]

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.[7]

Interactions

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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105993 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029131 – Ensembl, 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

  • Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • 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.
  • Hartley JL, Temple GF, Brasch MA (November 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Ohtsuka K, Hata M (April 2000). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature". Cell Stress & Chaperones. 5 (2): 98–112. doi:10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2 (inactive 31 January 2024). PMC 312896. PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of January 2024 (link)
  • Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Chuang JZ, Zhou H, Zhu M, Li SH, Li XJ, Sung CH (May 2002). "Characterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independently". The Journal of Biological Chemistry. 277 (22): 19831–8. doi:10.1074/jbc.M109613200. PMID 11896048.
  • Farinha CM, Nogueira P, Mendes F, Penque D, Amaral MD (September 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". The Biochemical Journal. 366 (Pt 3): 797–806. doi:10.1042/BJ20011717. PMC 1222832. PMID 12069690.
  • Hanai R, Mashima K (September 2003). "Characterization of two isoforms of a human DnaJ homologue, HSJ2". Molecular Biology Reports. 30 (3): 149–53. doi:10.1023/A:1024916223616. PMID 12974469. S2CID 24105834.
  • Liu Y, Zhu MC, Wang YJ, Zhan Z, Liu CG (November 2003). "[Cloning of a DnaJ homolog chaperon PBP and its subcellular localization]". Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi = Chinese Journal of Cellular and Molecular Immunology. 19 (6): 531–4. PMID 15182641.
  • Berruti G, Martegani E (January 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". Biology of Reproduction. 72 (1): 14–21. doi:10.1095/biolreprod.104.030866. PMID 15342353.
  • Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (October 2004). "From ORFeome to biology: a functional genomics pipeline". Genome Research. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Dai YS, Xu J, Molkentin JD (November 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". Molecular and Cellular Biology. 25 (22): 9936–48. doi:10.1128/MCB.25.22.9936-9948.2005. PMC 1280278. PMID 16260608.
  • Linse S, Thalberg K, Knowles TP (2021). "The unhappy chaperone". QRB Discovery. 2. Cambridge University Press: e7. doi:10.1017/qrd.2021.5. PMC 10392682. PMID 37529680.

External links

  • v
  • t
  • e
Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targetingUbiquitin
(ubiquitylation)Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other