DNAJA1

DNAJA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2LO1, 2M6Y
Identifiers
Aliases	DNAJA1, DJ-2, DjA1, HDJ2, HSDJ, HSJ2, HSPF4, NEDD7, hDJ-2, HSJ-2, DnaJ heat shock protein family (Hsp40) member A1
External IDs	MGI: 1270129 HomoloGene: 55588 GeneCards: DNAJA1
Gene ontology Molecular function • chaperone binding • heat shock protein binding • unfolded protein binding • C3HC4-type RING finger domain binding • metal ion binding • low-density lipoprotein particle receptor binding • Hsp70 protein binding • protein binding • G-protein coupled receptor binding • ATP binding • ubiquitin protein ligase binding • Tat protein binding Cellular component • cytoplasm • cytosol • membrane • intracellular membrane-bounded organelle • ubiquitin ligase complex • mitochondrion • cytoplasmic side of endoplasmic reticulum membrane • endoplasmic reticulum • perinuclear region of cytoplasm • extracellular exosome • nucleus Biological process • flagellated sperm motility • androgen receptor signaling pathway • regulation of protein transport • negative regulation of apoptotic process • response to heat • toxin transport • negative regulation of protein ubiquitination • response to unfolded protein • protein folding • spermatogenesis • positive regulation of apoptotic process • protein localization to mitochondrion • negative regulation of JUN kinase activity • DNA damage response, detection of DNA damage • negative regulation of establishment of protein localization to mitochondrion 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_001314039	NM_001164671 NM_001164672 NM_008298
RefSeq (protein)	NP_001530.1	NP_001158143.1 NP_001158144.1 NP_032324.1
Location (UCSC)	Chr 9: 33.03 – 33.04 Mb	Chr 4: 40.72 – 40.74 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

DnaJ homolog subfamily A member 1 is a protein that in humans is encoded by the DNAJA1 gene.^[3][4][5]

Interactions

DNAJA1 has been shown to interact with PTTG1.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. 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.
5. "Entrez Gene: DNAJA1 DnaJ (Hsp40) homolog, subfamily A, member 1".
6. 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.