DNAJA1

From Wikipedia, the free encyclopedia

DnaJ (Hsp40) homolog, subfamily A, member 1

Identifiers

DNAJA1; DJ-2; DjA1; HDJ2; HSDJ; HSJ2; HSPF4; hDJ-2

External IDs

OMIM: 602837 MGI: 1270129 HomoloGene: 55588

Gene ontology
Molecular Function:	• zinc ion binding • heat shock protein binding • metal ion binding • low-density lipoprotein receptor binding • unfolded protein binding
Biological Process:	• protein folding • response to unfolded protein

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001539 (mRNA)
NP_001530 (protein)

NM_008298 (mRNA)
NP_032324 (protein)

Location

Chr 9: 33.02 - 33.03 Mb

Chr 4: 40.91 - 40.92 Mb

Pubmed search

[1]

[2]

DnaJ (Hsp40) homolog, subfamily A, member 1, also known as DNAJA1, is a human gene.^[1]

[edit] References

^ Entrez Gene: DNAJA1 DnaJ (Hsp40) homolog, subfamily A, member 1.

[edit] Further reading

Chellaiah A, Davis A, Mohanakumar T (1993). "Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein.". Biochim. Biophys. Acta 1174 (1): 111–3. PMID 8334160.
Oh S, Iwahori A, Kato S (1993). "Human cDNA encoding DnaJ protein homologue.". Biochim. Biophys. Acta 1174 (1): 114–6. PMID 8334161.
Kanazawa M, Terada K, Kato S, Mori M (1997). "HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein import into mitochondria.". J. Biochem. 121 (5): 890–5. PMID 9192730.
Davis AR, Alevy YG, Chellaiah A, et al. (1998). "Characterization of HDJ-2, a human 40 kD heat shock protein.". Int. J. Biochem. Cell Biol. 30 (11): 1203–21. PMID 9839446.
Pei L (1999). "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells.". J. Biol. Chem. 274 (5): 3151–8. PMID 9915854.
Meacham GC, Lu Z, King S, et al. (1999). "The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis.". EMBO J. 18 (6): 1492–505. doi:10.1093/emboj/18.6.1492. PMID 10075921.
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.
Jana NR, Tanaka M, Wang G, Nukina N (2000). "Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity.". Hum. Mol. Genet. 9 (13): 2009–18. PMID 10942430.
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.
Bao YP, Cook LJ, O'Donovan D, et al. (2002). "Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy.". J. Biol. Chem. 277 (14): 12263–9. doi:10.1074/jbc.M109633200. PMID 11796717.
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.
Imai Y, Soda M, Hatakeyama S, et al. (2002). "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity.". Mol. Cell 10 (1): 55–67. PMID 12150907.
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.
Hanai R, Mashima K (2004). "Characterization of two isoforms of a human DnaJ homologue, HSJ2.". Mol. Biol. Rep. 30 (3): 149–53. PMID 12974469.
Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region.". Genomics 83 (1): 153–67. PMID 14667819.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway.". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
Marschang P, Brich J, Weeber EJ, et al. (2004). "Normal development and fertility of knockout mice lacking the tumor suppressor gene LRP1b suggest functional compensation by LRP1.". Mol. Cell. Biol. 24 (9): 3782–93. PMID 15082773.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
Hu Y, Zhou Z, Huang X, et al. (2005). "Expression of a novel DnaJA1 alternative splicing in human testis and sperm.". Int. J. Androl. 27 (6): 343–9. doi:10.1111/j.1365-2605.2004.00492.x. PMID 15595953.