| Aspartyl-tRNA synthetase | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||||
| Symbols | DARS; DKFZp781B11202; MGC111579 | ||||||||||||
| External IDs | OMIM: 603084 MGI: 2442544 HomoloGene: 1032 GeneCards: DARS Gene | ||||||||||||
| EC number | 6.1.1.12 | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 1615 | 226414 | |||||||||||
| Ensembl | ENSG00000115866 | ENSMUSG00000026356 | |||||||||||
| UniProt | P14868 | Q922B2 | |||||||||||
| RefSeq (mRNA) | NM_001349.2 | NM_145507.2 | |||||||||||
| RefSeq (protein) | NP_001340.2 | NP_663482.2 | |||||||||||
| Location (UCSC) | Chr 2: 136.66 – 136.74 Mb |
Chr 1: 130.26 – 130.31 Mb |
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| PubMed search | [1] | [2] | |||||||||||
Aspartyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the DARS gene.[1][2]
Aspartyl-tRNA synthetase (DARS) is part of a multienzyme complex of aminoacyl-tRNA synthetases. Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis.[2]
See also [link]
References [link]
- ^ Jacobo-Molina A, Peterson R, Yang DC (Oct 1989). "cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase". J Biol Chem 264 (28): 16608–12. PMID 2674137.
- ^ a b "Entrez Gene: DARS aspartyl-tRNA synthetase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1615.
Further reading [link]
- Norcum MT (1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents.". J. Biol. Chem. 266 (23): 15398–405. PMID 1651330.
- Reed VS, Wastney ME, Yang DC (1995). "Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha.". J. Biol. Chem. 269 (52): 32932–6. PMID 7806521.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. DOI:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Escalante C, Yang DC (1993). "Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix". J. Biol. Chem. 268 (8): 6014–23. PMID 8449960.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. DOI:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Quevillon S, Robinson JC, Berthonneau E, et al. (1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". J. Mol. Biol. 285 (1): 183–95. DOI:10.1006/jmbi.1998.2316. PMID 9878398.
- Rho SB, Kim MJ, Lee JS, et al. (1999). "Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (8): 4488–93. DOI:10.1073/pnas.96.8.4488. PMC 16359. PMID 10200289. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16359.
- Kang J, Kim T, Ko YG, et al. (2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". J. Biol. Chem. 275 (41): 31682–8. DOI:10.1074/jbc.M909965199. PMID 10913161.
- Sang Lee J, Gyu Park S, Park H, et al. (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. 291 (1): 158–64. DOI:10.1006/bbrc.2002.6398. PMID 11829477.
- 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Cheong HK, Park JY, Kim EH, et al. (2004). "Structure of the N-terminal extension of human aspartyl-tRNA synthetase: implications for its biological function". Int. J. Biochem. Cell Biol. 35 (11): 1548–57. DOI:10.1016/S1357-2725(03)00070-0. PMID 12824064.
- 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.
- 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Bonnefond L, Fender A, Rudinger-Thirion J, et al. (2005). "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS". Biochemistry 44 (12): 4805–16. DOI:10.1021/bi047527z. PMID 15779907.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. DOI:10.1038/nature04209. PMID 16189514.
- Tu LC, Yan X, Hood L, Lin B (2007). "Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells". Mol. Cell Proteomics 6 (4): 575–88. DOI:10.1074/mcp.M600249-MCP200. PMID 17220478.
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DARS
DARS may refer to:
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Gene
A gene is a locus (or region) of DNA that encodes a functional RNA or protein product, and is the molecular unit of heredity. The transmission of genes to an organism's offspring is the basis of the inheritance of phenotypic traits. Most biological traits are under the influence of polygenes (many different genes) as well as the gene–environment interactions. Some genetic traits are instantly visible, such as eye colour or number of limbs, and some are not, such as blood type, risk for specific diseases, or the thousands of basic biochemical processes that comprise life.
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