Biology:DNAJB1
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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]
A fusion protein of DNAJB1 and PRKACA drives fibrolamellar hepatocellular carcinoma, a type of rare liver cancer.[4]
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): 446–449. December 1996. doi:10.1006/geno.1996.0653. PMID 8975727.
- ↑ "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ". Biochemical and Biophysical Research Communications 197 (1): 235–240. November 1993. doi:10.1006/bbrc.1993.2466. PMID 8250930. Bibcode: 1993BBRC..197..235O.
- ↑ "Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3337.
- ↑ "Oncogenic Addiction of Fibrolamellar Hepatocellular Carcinoma to the Fusion Kinase DNAJB1-PRKACA". Clinical Cancer Research 29 (1): 271–278. January 2023. doi:10.1158/1078-0432.CCR-22-1851. PMID 36302174.
- ↑ "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Molecules and Cells 16 (1): 84–91. August 2003. doi:10.1016/S1016-8478(23)13770-8. PMID 14503850.
- ↑ "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions". Molecular and Cellular Biology 19 (6): 4535–4545. June 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 Structure and Function 17 (1): 77–86. February 1992. doi:10.1247/csf.17.77. PMID 1586970.
- "A human homologue of the Escherichia coli DnaJ heat-shock protein". Nucleic Acids Research 19 (23): 6645. December 1991. 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". The EMBO Journal 15 (12): 2969–2979. June 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". Journal of Molecular Biology 260 (2): 224–235. July 1996. doi:10.1006/jmbi.1996.0394. PMID 8764402.
- "Molecular chaperones as HSF1-specific transcriptional repressors". Genes & Development 12 (5): 654–666. March 1998. doi:10.1101/gad.12.5.654. PMID 9499401.
- "Characterization of HSE sequences in human Hsp40 gene: structural and promoter analysis". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1397 (1): 43–55. April 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): 471–480. August 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". The Journal of Biological Chemistry 274 (6): 3797–3803. February 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". Molecular and Cellular Biology 19 (6): 4535–4545. June 1999. doi:10.1128/mcb.19.6.4535. PMID 10330192.
- "Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells". The Journal of Biological Chemistry 274 (51): 36757–36763. December 1999. doi:10.1074/jbc.274.51.36757. PMID 10593983.
- "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70". The Journal of Biological Chemistry 275 (32): 24728–24734. August 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. April 2000. doi:10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2. PMID 11147971.
- "Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages". American Journal of Physiology. Renal Physiology 281 (2): F326–F336. August 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". The EMBO Journal 20 (16): 4478–4489. August 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". The Journal of Biological Chemistry 277 (14): 11873–11881. April 2002. doi:10.1074/jbc.M111445200. PMID 11809754.
- "Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1". The Journal of Biological Chemistry 277 (16): 14060–14067. April 2002. doi:10.1074/jbc.M111576200. PMID 11821413.
- "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Experimental Cell Research 289 (2): 211–221. October 2003. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
- "Detection of a recurrent DNAJB1-PRKACA chimeric transcript in fibrolamellar hepatocellular carcinoma". Science 343 (6174): 1010–1014. February 2014. doi:10.1126/science.1249484. PMID 24578576. Bibcode: 2014Sci...343.1010H.
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