DNAJB1

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DnaJ (Hsp40) homolog, subfamily B, member 1
PDB rendering based on 1hdj.
Available structures: 1hdj
Identifiers
Symbols DNAJB1; HSPF1; Hdj1; Hsp40
External IDs OMIM: 604572 MGI: 1931874 HomoloGene: 55957
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3337 81489
Ensembl ENSG00000132002 ENSMUSG00000005483
Uniprot P25685 Q3TIT6
Refseq NM_006145 (mRNA)
NP_006136 (protein)		 NM_018808 (mRNA)
NP_061278 (protein)
Location Chr 19: 14.49 - 14.49 Mb Chr 8: 86.5 - 86.5 Mb
Pubmed search [1] [2]

DnaJ (Hsp40) homolog, subfamily B, member 1, also known as DNAJB1, is a human gene.1


References

  1. ^ "Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1".

Further reading

  • Hattori H, Liu YC, Tohnai I, et al. (1992). "Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.". Cell Struct. Funct. 17 (1): 77–86. PMID 1586970. 
  • Raabe T, Manley JL (1992). "A human homologue of the Escherichia coli DnaJ heat-shock protein.". Nucleic Acids Res. 19 (23): 6645. PMID 1754405. 
  • Ohtsuka K (1994). "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ.". Biochem. Biophys. Res. Commun. 197 (1): 235–40. PMID 8250930. 
  • Freeman BC, Morimoto RI (1996). "The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.". EMBO J. 15 (12): 2969–79. PMID 8670798. 
  • Qian YQ, Patel D, Hartl FU, McColl DJ (1996). "Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain.". J. Mol. Biol. 260 (2): 224–35. doi:10.1006/jmbi.1996.0394. PMID 8764402. 
  • Hata M, Okumura K, Seto M, Ohtsuka K (1997). "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2.". Genomics 38 (3): 446–9. doi:10.1006/geno.1996.0653. PMID 8975727. 
  • Shi Y, Mosser DD, Morimoto RI (1998). "Molecular chaperones as HSF1-specific transcriptional repressors.". Genes Dev. 12 (5): 654–66. PMID 9499401. 
  • Hata M, Ohtsuka K (1998). "Characterization of HSE sequences in human Hsp40 gene: structural and promoter analysis.". Biochim. Biophys. Acta 1397 (1): 43–55. PMID 9545528. 
  • Zou J, Guo Y, Guettouche T, et al. (1998). "Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1.". Cell 94 (4): 471–80. PMID 9727490. 
  • Melville MW, Tan SL, Wambach M, et al. (1999). "The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity.". J. Biol. Chem. 274 (6): 3797–803. PMID 9920933. 
  • Ballinger CA, Connell P, Wu Y, et al. (1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.". Mol. Cell. Biol. 19 (6): 4535–45. PMID 10330192. 
  • Michels AA, Kanon B, Bensaude O, Kampinga HH (2000). "Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells.". J. Biol. Chem. 274 (51): 36757–63. PMID 10593983. 
  • Terada K, Mori M (2000). "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70.". J. Biol. Chem. 275 (32): 24728–34. doi:10.1074/jbc.M002021200. PMID 10816573. 
  • 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. 
  • Kuncewicz T, Balakrishnan P, Snuggs MB, Kone BC (2001). "Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages.". Am. J. Physiol. Renal Physiol. 281 (2): F326–36. PMID 11457725. 
  • Pang Q, Keeble W, Christianson TA, et al. (2001). "FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity.". EMBO J. 20 (16): 4478–89. doi:10.1093/emboj/20.16.4478. PMID 11500375. 
  • Hernández MP, Chadli A, Toft DO (2002). "HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor.". J. Biol. Chem. 277 (14): 11873–81. doi:10.1074/jbc.M111445200. PMID 11809754. 
  • Anwar A, Siegel D, Kepa JK, Ross D (2002). "Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1.". J. Biol. Chem. 277 (16): 14060–7. doi:10.1074/jbc.M111576200. PMID 11821413. 
  • 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. 
  • Reuter TY, Medhurst AL, Waisfisz Q, et al. (2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport.". Exp. Cell Res. 289 (2): 211–21. PMID 14499622. 
v • d • e
Chaperones
Heat shock proteins/Chaperonins
Hsp10/GroES · Hsp27 · Hsp47 · HSP60/GroEL

Hsp40/DnaJ (A1, A2, A3, B1, B2, B11, B4, B6, B9, C1, C3, C5, C6, C7, C10, C11, C13, C14, C19)

Hsp70 (1A, 1B, 1L, 2, 4, 4L, 5, 6, 7, 8, 9, 12A, 14)
Hsp90 (α1, α2, β, ER, TRAP1)
Other
 This article on a gene on chromosome 19 is a stub. You can help Wikipedia by expanding it.

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