Biology:DNAJB1
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
![]() Generic protein structure example |
DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.[1][2][3]
Interactions
DNAJB1 has been shown to interact with:
References
- ↑ "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2". Genomics 38 (3): 446–9. Mar 1997. doi:10.1006/geno.1996.0653. PMID 8975727.
- ↑ Ohtsuka K (Jan 1994). "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ". Biochem Biophys Res Commun 197 (1): 235–40. doi:10.1006/bbrc.1993.2466. PMID 8250930.
- ↑ "Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3337.
- ↑ "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Mol. Cells 16 (1): 84–91. Aug 2003. PMID 14503850.
- ↑ "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. Jun 1999. doi:10.1128/mcb.19.6.4535. PMID 10330192.
Further reading
- "Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.". Cell Struct. Funct. 17 (1): 77–86. 1992. doi:10.1247/csf.17.77. PMID 1586970.
- "A human homologue of the Escherichia coli DnaJ heat-shock protein.". Nucleic Acids Res. 19 (23): 6645. 1992. doi:10.1093/nar/19.23.6645. PMID 1754405.
- "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. 1996. doi:10.1002/j.1460-2075.1996.tb00660.x. PMID 8670798.
- "Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain.". J. Mol. Biol. 260 (2): 224–35. 1996. doi:10.1006/jmbi.1996.0394. PMID 8764402.
- "Molecular chaperones as HSF1-specific transcriptional repressors.". Genes Dev. 12 (5): 654–66. 1998. doi:10.1101/gad.12.5.654. PMID 9499401.
- "Characterization of HSE sequences in human Hsp40 gene: structural and promoter analysis.". Biochim. Biophys. Acta 1397 (1): 43–55. 1998. doi:10.1016/S0167-4781(97)00208-X. PMID 9545528.
- "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. 1998. doi:10.1016/S0092-8674(00)81588-3. PMID 9727490.
- "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. 1999. doi:10.1074/jbc.274.6.3797. PMID 9920933.
- "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. 1999. doi:10.1128/mcb.19.6.4535. PMID 10330192.
- "Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells.". J. Biol. Chem. 274 (51): 36757–63. 2000. doi:10.1074/jbc.274.51.36757. PMID 10593983.
- "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70.". J. Biol. Chem. 275 (32): 24728–34. 2000. doi:10.1074/jbc.M002021200. PMID 10816573.
- "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature.". Cell Stress Chaperones 5 (2): 98–112. 2001. PMID 11147971.
- "Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages.". Am. J. Physiol. Renal Physiol. 281 (2): F326–36. 2001. doi:10.1152/ajprenal.2001.281.2.F326. PMID 11457725.
- "FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity.". EMBO J. 20 (16): 4478–89. 2001. doi:10.1093/emboj/20.16.4478. PMID 11500375.
- "HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor.". J. Biol. Chem. 277 (14): 11873–81. 2002. doi:10.1074/jbc.M111445200. PMID 11809754.
- "Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1.". J. Biol. Chem. 277 (16): 14060–7. 2002. doi:10.1074/jbc.M111576200. PMID 11821413.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "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. 2003. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
- Honeyman, Joshua N et al. (2014). "Detection of a Recurrent DNAJB1-PRKACA Chimeric Transcript in Fibrolamellar Hepatocellular Carcinoma.". Science 343 (6174): 1010–1014. doi:10.1126/science.1249484. PMID 24578576.