DNAJB1

DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.[5][6][7]

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
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19p13.12 Start 14,514,769 bp[1] End 14,529,770 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 C2 Start 83,608,193 bp[2] End 83,612,653 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • unfolded protein binding • ATPase binding • Hsp70 protein binding • chaperone binding • GO:0001948 protein binding • ATPase activator activity • GO:0001106 transcription corepressor activity • cadherin binding Cellular component • cytosol • nucleolus • extracellular exosome • cell nucleus • nucleoplasm • cytoplasm • GO:0097483, GO:0097481 postsynaptic density • neuronal cell body • dendritic spine • sperm head • postsynapse • glutamatergic synapse Biological process • regulation of cellular response to heat • response to unfolded protein • positive regulation of ATPase activity • protein folding • chaperone mediated protein folding requiring cofactor • negative regulation of inclusion body assembly • negative regulation of transcription from RNA polymerase II promoter in response to stress • negative regulation of transcription from RNA polymerase II promoter • 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 – 14.53 Mb	Chr 8: 83.61 – 83.61 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

DNAJB1 has been shown to interact with:

• HSPA4,[8] and
• STUB1[9]

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 (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.
6. 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.
7. "Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1".
8. 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.
9. 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.