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DNAJB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1HDJ, 2QLD, 3AGX, 3AGY, 3AGZ, 4WB7
Identifiers
Aliases	DNAJB1, HSPF1, Hdj1, Hsp40, RSPH16B, Sis1, DnaJ heat shock protein family (Hsp40) member B1
External IDs	OMIM: 604572; MGI: 1931874; HomoloGene: 55957; GeneCards: DNAJB1; OMA:DNAJB1 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.12 Start 14,514,769 bp End 14,560,391 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 C2 Start 84,334,822 bp End 84,339,282 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gallbladder mucosa of pharynx left testis ventricular zone right testis trachea buccal mucosa cell epithelium of esophagus vagina cardia Top expressed in seminiferous tubule motor neuron utricle primitive streak ascending aorta aortic valve fossa Epithelium of choroid plexus conjunctival fornix spermatid More reference expression data BioGPS More reference expression data
Gene ontology Molecular function unfolded protein binding ATPase binding Hsp70 protein binding chaperone binding protein binding ATPase activator activity transcription corepressor activity cadherin binding Cellular component cytosol nucleolus extracellular exosome nucleus nucleoplasm cytoplasm postsynaptic density soma dendritic spine sperm head postsynapse glutamatergic synapse Biological process regulation of cellular response to heat response to unfolded protein positive regulation of ATP-dependent activity protein folding chaperone cofactor-dependent protein refolding negative regulation of inclusion body assembly negative regulation of transcription from RNA polymerase II promoter in response to stress negative regulation of transcription by RNA polymerase II forebrain development Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3337 81489 Ensembl ENSG00000132002 ENSMUSG00000005483 UniProt P25685 Q9QYJ3 RefSeq (mRNA) NM_001313964 NM_001300914 NM_006145 NM_018808 NM_001308227 RefSeq (protein) NP_001287843 NP_001300893 NP_006136 NP_001295156 NP_061278 Location (UCSC) Chr 19: 14.51 – 14.56 Mb Chr 8: 84.33 – 84.34 Mb PubMed search
Wikidata
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DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.

A fusion protein of DNAJB1 and PRKACA drives fibrolamellar hepatocellular carcinoma, a type of rare liver cancer.

Interactions

DNAJB1 has been shown to interact with:

• HSPA4, and
• STUB1

References

1. ^ GRCh38: Ensembl release 89: ENSG00000132002 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000005483 – 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. Hata M, Okumura K, Seto M, Ohtsuka K (December 1996). "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2". Genomics. 38 (3): 446–449. doi:10.1006/geno.1996.0653. PMID 8975727.
6. Ohtsuka K (November 1993). "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ". Biochemical and Biophysical Research Communications. 197 (1): 235–240. doi:10.1006/bbrc.1993.2466. PMID 8250930.
7. "Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1".
8. Neumayer C, Ng D, Jiang CS, Qureshi A, Lalazar G, Vaughan R, et al. (January 2023). "Oncogenic Addiction of Fibrolamellar Hepatocellular Carcinoma to the Fusion Kinase DNAJB1-PRKACA". Clinical Cancer Research. 29 (1): 271–278. doi:10.1158/1078-0432.CCR-22-1851. PMC 9811160. PMID 36302174.
9. Oh WK, Song J (August 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Molecules and Cells. 16 (1): 84–91. doi:10.1016/S1016-8478(23)13770-8. PMID 14503850.
10. Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, et al. (June 1999). "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. doi:10.1128/mcb.19.6.4535. PMC 104411. PMID 10330192.

Further reading

• Hattori H, Liu YC, Tohnai I, Ueda M, Kaneda T, Kobayashi T, et al. (February 1992). "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. doi:10.1247/csf.17.77. PMID 1586970. S2CID 21909960.
• Raabe T, Manley JL (December 1991). "A human homologue of the Escherichia coli DnaJ heat-shock protein". Nucleic Acids Research. 19 (23): 6645. doi:10.1093/nar/19.23.6645. PMC 329243. PMID 1754405.
• Freeman BC, Morimoto RI (June 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". The EMBO Journal. 15 (12): 2969–2979. doi:10.1002/j.1460-2075.1996.tb00660.x. PMC 450238. PMID 8670798.
• Qian YQ, Patel D, Hartl FU, McColl DJ (July 1996). "Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain". Journal of Molecular Biology. 260 (2): 224–235. doi:10.1006/jmbi.1996.0394. PMID 8764402.
• Shi Y, Mosser DD, Morimoto RI (March 1998). "Molecular chaperones as HSF1-specific transcriptional repressors". Genes & Development. 12 (5): 654–666. doi:10.1101/gad.12.5.654. PMC 316571. PMID 9499401.
• Hata M, Ohtsuka K (April 1998). "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. doi:10.1016/S0167-4781(97)00208-X. PMID 9545528.
• Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (August 1998). "Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1". Cell. 94 (4): 471–480. doi:10.1016/S0092-8674(00)81588-3. PMID 9727490. S2CID 9234420.
• Melville MW, Tan SL, Wambach M, Song J, Morimoto RI, Katze MG (February 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". The Journal of Biological Chemistry. 274 (6): 3797–3803. doi:10.1074/jbc.274.6.3797. PMID 9920933.
• Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, et al. (June 1999). "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. doi:10.1128/mcb.19.6.4535. PMC 104411. PMID 10330192.
• Michels AA, Kanon B, Bensaude O, Kampinga HH (December 1999). "Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells". The Journal of Biological Chemistry. 274 (51): 36757–36763. doi:10.1074/jbc.274.51.36757. PMID 10593983.
• Terada K, Mori M (August 2000). "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70". The Journal of Biological Chemistry. 275 (32): 24728–24734. doi:10.1074/jbc.M002021200. PMID 10816573.
• 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 2024-11-02). PMC 312896. PMID 11147971.{{cite journal}}: CS1 maint: DOI inactive as of November 2024 (link)
• Kuncewicz T, Balakrishnan P, Snuggs MB, Kone BC (August 2001). "Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages". American Journal of Physiology. Renal Physiology. 281 (2): F326 – F336. doi:10.1152/ajprenal.2001.281.2.F326. PMID 11457725. S2CID 15719851.
• Pang Q, Keeble W, Christianson TA, Faulkner GR, Bagby GC (August 2001). "FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity". The EMBO Journal. 20 (16): 4478–4489. doi:10.1093/emboj/20.16.4478. PMC 125562. PMID 11500375.
• Hernández MP, Chadli A, Toft DO (April 2002). "HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor". The Journal of Biological Chemistry. 277 (14): 11873–11881. doi:10.1074/jbc.M111445200. PMID 11809754.
• Anwar A, Siegel D, Kepa JK, Ross D (April 2002). "Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1". The Journal of Biological Chemistry. 277 (16): 14060–14067. doi:10.1074/jbc.M111576200. PMID 11821413.
• Reuter TY, Medhurst AL, Waisfisz Q, Zhi Y, Herterich S, Hoehn H, et al. (October 2003). "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. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
• Honeyman JN, Simon EP, Robine N, Chiaroni-Clarke R, Darcy DG, Lim II, et al. (February 2014). "Detection of a recurrent DNAJB1-PRKACA chimeric transcript in fibrolamellar hepatocellular carcinoma". Science. 343 (6174): 1010–1014. Bibcode:2014Sci...343.1010H. doi:10.1126/science.1249484. PMC 4286414. PMID 24578576.

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