DNAJB1
From Wikipedia, the free encyclopedia
| DnaJ (Hsp40) homolog, subfamily B, member 1 | |||||||||||||
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 PDB rendering based on 1hdj. | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | DNAJB1; HSPF1; Hdj1; Hsp40; RSPH16B; Sis1 | ||||||||||||
| External IDs | OMIM: 604572 MGI: 1931874 HomoloGene: 55957 GeneCards: DNAJB1 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 3337 | 81489 | |||||||||||
| Ensembl | ENSG00000132002 | ENSMUSG00000005483 | |||||||||||
| UniProt | P25685 | Q9QYJ3 | |||||||||||
| RefSeq (mRNA) | NM_006145 | NM_018808 | |||||||||||
| RefSeq (protein) | NP_006136 | NP_061278 | |||||||||||
| Location (UCSC) | Chr 19: 14.63 – 14.64 Mb | Chr 8: 83.61 – 83.61 Mb | |||||||||||
| PubMed search | |||||||||||||
DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.[1][2][3]
Interactions
DNAJB1 has been shown to interact with STUB1[4] and HSPA4.[5]
References
- ↑ 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.
- ↑ 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.
- ↑ "Entrez Gene: DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1".
- ↑ Ballinger, C A; Connell P, Wu Y, Hu Z, Thompson L J, Yin L Y, 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. (UNITED STATES) 19 (6): 4535–45. ISSN 0270-7306. PMC 104411. PMID 10330192.
- ↑ Oh, Won-Kyung; Song Jaewhan (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Mol. Cells (Korea (South)) 16 (1): 84–91. ISSN 1016-8478. PMID 14503850.
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. 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. 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.
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