RARS (gene)
| Arginyl-tRNA synthetase | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | RARS ; ArgRS; DALRD1; HLD9 | ||||||||||||
| External IDs | OMIM: 107820 MGI: 1914297 HomoloGene: 68281 ChEMBL: 2824 GeneCards: RARS Gene | ||||||||||||
| EC number | 6.1.1.19 | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 5917 | 104458 | |||||||||||
| Ensembl | ENSG00000113643 | ENSMUSG00000018848 | |||||||||||
| UniProt | P54136 | Q9D0I9 | |||||||||||
| RefSeq (mRNA) | NM_002887 | NM_025936 | |||||||||||
| RefSeq (protein) | NP_002878 | NP_080212 | |||||||||||
| Location (UCSC) |
Chr 5: 168.49 – 168.52 Mb |
Chr 11: 35.81 – 35.83 Mb | |||||||||||
| PubMed search | |||||||||||||
Arginyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the RARS gene.[1][2]
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.[2]
Genetics
Mutations in RARS cause hypomyelination .[3]
Interactions
RARS (gene) has been shown to interact with QARS.[4]
References
- ↑ Girjes AA, Hobson K, Chen P, Lavin MF (December 1995). "Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase". Gene 164 (2): 347–50. doi:10.1016/0378-1119(95)00502-W. PMID 7590355.
- 1 2 "Entrez Gene: RARS arginyl-tRNA synthetase".
- ↑ Wolf, N. I.; Salomons, G. S.; Rodenburg, R. J.; Pouwels, P. J.; Schieving, J. H.; Derks, T. G.; Fock, J. M.; Rump, P; Van Beek, D. M.; Van Der Knaap, M. S.; Waisfisz, Q (2014). "Mutations in RARS cause hypomyelination". Annals of Neurology 76 (1): 134–9. doi:10.1002/ana.24167. PMID 24777941.
- ↑ Kim, T; Park S G; Kim J E; Seol W; Ko Y G; Kim S (July 2000). "Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex". J. Biol. Chem. (UNITED STATES) 275 (28): 21768–72. doi:10.1074/jbc.M002404200. ISSN 0021-9258. PMID 10801842.
Further reading
- McCune SA, Yu PL, Nance WE (1977). "A genetic study of erythrocyte arginine-tRNA synthetase activity in man.". Acta geneticae medicae et gemellologiae 26 (1): 21–7. PMID 562050.
- 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.
- Wang HY, Pan F (1985). "Kinetic mechanism of arginyl-tRNA synthetase from human placenta.". Int. J. Biochem. 16 (12): 1379–85. doi:10.1016/0020-711X(84)90244-1. PMID 6530022.
- 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.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- 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.
- Rho SB, Lee JS, Jeong EJ, et al. (1998). "A multifunctional repeated motif is present in human bifunctional tRNA synthetase". J. Biol. Chem. 273 (18): 11267–73. doi:10.1074/jbc.273.18.11267. PMID 9556618.
- 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.
- Park SG, Jung KH, Lee JS, et al. (1999). "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase". J. Biol. Chem. 274 (24): 16673–6. doi:10.1074/jbc.274.24.16673. PMID 10358004.
- Kim T, Park SG, Kim JE, et al. (2000). "Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex". J. Biol. Chem. 275 (28): 21768–72. doi:10.1074/jbc.M002404200. PMID 10801842.
- 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.
- 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.
- Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
- 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.
- Ling C, Yao YN, Zheng YG, et al. (2005). "The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex". J. Biol. Chem. 280 (41): 34755–63. doi:10.1074/jbc.M413511200. PMID 16055448.
- Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
- Bottoni A, Vignali C, Piccin D, et al. (2007). "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines". J. Cell. Physiol. 212 (2): 293–7. doi:10.1002/jcp.21083. PMID 17443684.
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