DNAJB1

From Wikipedia, the free encyclopedia

DnaJ (Hsp40) homolog, subfamily B, member 1

PDB rendering based on 1hdj.

Available structures: 1hdj

Identifiers

Symbol(s)

DNAJB1; HSPF1; Hdj1; Hsp40

External IDs

OMIM: 604572 MGI: 1931874 HomoloGene: 55957

Gene ontology
Molecular Function:	• heat shock protein binding • unfolded protein binding
Cellular Component:	• nucleus
Biological Process:	• protein folding • response to unfolded protein • chaperone cofactor-dependent protein folding

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006145 (mRNA)
NP_006136 (protein)

NM_018808 (mRNA)
NP_061278 (protein)

Location

Chr 19: 14.49 - 14.49 Mb

Chr 8: 86.5 - 86.5 Mb

Pubmed search

[1]

[2]

DnaJ (Hsp40) homolog, subfamily B, member 1, also known as DNAJB1, is a human gene.^[1]

[edit] References

^ Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1.

[edit] 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. PMID 1586970.
Raabe T, Manley JL (1992). "A human homologue of the Escherichia coli DnaJ heat-shock protein.". Nucleic Acids Res. 19 (23): 6645. PMID 1754405.
Ohtsuka K (1994). "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ.". Biochem. Biophys. Res. Commun. 197 (1): 235-40. PMID 8250930.
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. 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.
Hata M, Okumura K, Seto M, Ohtsuka K (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.
Shi Y, Mosser DD, Morimoto RI (1998). "Molecular chaperones as HSF1-specific transcriptional repressors.". Genes Dev. 12 (5): 654-66. 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. 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. 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. 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. 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. 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. 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. 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. 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. PMID 14499622.