DNAJA1

DnaJ (Hsp40) homolog, subfamily A, member 1
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2LO1​, 2M6Y​
Identifiers
Symbols	DNAJA1 ; DJ-2; DjA1; HDJ2; HSDJ; HSJ2; HSPF4; NEDD7; hDJ-2
External IDs	OMIM: 602837 MGI: 1270129 HomoloGene: 55588 GeneCards: DNAJA1 Gene
Gene ontology Molecular function • G-protein coupled receptor binding • protein binding • ATP binding • Hsp70 protein binding • ubiquitin protein ligase binding • metal ion binding • low-density lipoprotein particle receptor binding • unfolded protein binding • chaperone binding • C3HC4-type RING finger domain binding Cellular component • ubiquitin ligase complex • nucleus • mitochondrion • cytosol • membrane • perinuclear region of cytoplasm • extracellular exosome • cytoplasmic side of endoplasmic reticulum membrane Biological process • protein folding • response to unfolded protein • spermatogenesis • response to heat • sperm motility • androgen receptor signaling pathway • negative regulation of protein ubiquitination • protein refolding • DNA damage response, detection of DNA damage • positive regulation of apoptotic process • negative regulation of apoptotic process • negative regulation of JUN kinase activity • regulation of protein transport • protein localization to mitochondrion • toxin transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3301	15502
Ensembl	ENSG00000086061	ENSMUSG00000028410
UniProt	P31689	P63037
RefSeq (mRNA)	NM_001539	NM_001164671
RefSeq (protein)	NP_001530	NP_001158143
Location (UCSC)	Chr 9: 33.03 – 33.04 Mb	Chr 4: 40.72 – 40.74 Mb
PubMed search

DnaJ homolog subfamily A member 1 is a protein that in humans is encoded by the DNAJA1 gene.^[1][2][3]

Interactions

DNAJA1 has been shown to interact with PTTG1.^[4]

References

1. Chellaiah A, Davis A, Mohanakumar T (Aug 1993). "Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein". Biochim Biophys Acta 1174 (1): 111–3. doi:10.1016/0167-4781(93)90103-k. PMID 8334160.
2. Ohtsuka K, Hata M (Jan 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.
3. "Entrez Gene: DNAJA1 DnaJ (Hsp40) homolog, subfamily A, member 1".
4. Pei, L (Jan 1999). "Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells". J. Biol. Chem. (UNITED STATES) 274 (5): 3151–8. doi:10.1074/jbc.274.5.3151. ISSN 0021-9258. PMID 9915854.

Further reading

• Oh S, Iwahori A, Kato S (1993). "Human cDNA encoding DnaJ protein homologue.". Biochim. Biophys. Acta 1174 (1): 114–6. doi:10.1016/0167-4781(93)90104-l. 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. doi:10.1093/oxfordjournals.jbchem.a021670. 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. doi:10.1016/S1357-2725(98)00091-0. 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. doi:10.1074/jbc.274.5.3151. 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. PMC 1171238. 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. doi:10.1093/hmg/9.13.2009. PMID 10942430.
• 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. doi:10.1016/S1097-2765(02)00583-X. 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. PMC 139241. PMID 12477932.
• Hanai R, Mashima K (2004). "Characterization of two isoforms of a human DnaJ homologue, HSJ2.". Mol. Biol. Rep. 30 (3): 149–53. doi:10.1023/A:1024916223616. 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. doi:10.1016/S0888-7543(03)00235-0. 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. doi:10.1128/MCB.24.9.3782-3793.2004. PMC 387731. 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. PMC 528928. 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.