DNAJB1

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	MGI: 1931874 HomoloGene: 55957 GeneCards: DNAJB1
Gene ontology Molecular function • unfolded protein binding • ATPase binding • Hsp70 protein binding • chaperone binding • protein binding • ATPase activator activity • cadherin binding involved in cell-cell adhesion Cellular component • cytosol • nucleolus • extracellular exosome • nucleus • nucleoplasm • cell-cell adherens junction • cytoplasm Biological process • regulation of cellular response to heat • response to unfolded protein • chaperone cofactor-dependent protein refolding • positive regulation of ATPase activity • protein folding • chaperone mediated protein folding requiring cofactor • negative regulation of inclusion body assembly • cell-cell adhesion Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
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_001287843.1 NP_006136.1 NP_001300893.1	NP_061278.1
Location (UCSC)	Chr 19: 14.51 – 14.53 Mb	Chr 8: 83.61 – 83.61 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.^[3][4][5]

Interactions

DNAJB1 has been shown to interact with:

• HSPA4,^[6] and
• STUB1^[7]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Hata M, Okumura K, Seto M, Ohtsuka K (Mar 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.
4. 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.
5. "Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1".
6. Oh WK, Song J (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Mol. Cells. 16 (1): 84–91. PMID 14503850.
7. Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C (Jun 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. doi:10.1128/mcb.19.6.4535. PMC 104411. PMID 10330192.

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. doi:10.1247/csf.17.77. PMID 1586970.
• Raabe T, Manley JL (1992). "A human homologue of the Escherichia coli DnaJ heat-shock protein.". Nucleic Acids Res. 19 (23): 6645. doi:10.1093/nar/19.23.6645. PMC 329243. PMID 1754405.
• 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. PMC 450238. 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.
• Shi Y, Mosser DD, Morimoto RI (1998). "Molecular chaperones as HSF1-specific transcriptional repressors.". Genes Dev. 12 (5): 654–66. doi:10.1101/gad.12.5.654. PMC 316571. 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. doi:10.1016/S0167-4781(97)00208-X. 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. doi:10.1016/S0092-8674(00)81588-3. 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. doi:10.1074/jbc.274.6.3797. 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. doi:10.1128/mcb.19.6.4535. PMC 104411. 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. doi:10.1074/jbc.274.51.36757. 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. doi:10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2. PMC 312896. 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. PMC 125562. 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. PMC 139241. 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. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
• Honeyman, Joshua N; Simon E; Robine N; et al. (2014). "Detection of a Recurrent DNAJB1-PRKACA Chimeric Transcript in Fibrolamellar Hepatocellular Carcinoma.". Science. 343: 1010–1014. doi:10.1126/science.1249484. PMC 4286414. PMID 24578576.