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IARS - Wikipedia, the free encyclopedia

IARS

From Wikipedia, the free encyclopedia


Isoleucyl-tRNA synthetase
Identifiers
Symbol(s) IARS; FLJ20736; IARS1; ILRS; PRO0785
External IDs OMIM: 600709 MGI2145219 HomoloGene5325
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 3376 105148
Ensembl ENSG00000196305 ENSMUSG00000037851
Uniprot P41252 Q3UWS7
Refseq NM_002161 (mRNA)
NP_002152 (protein)
NM_172015 (mRNA)
NP_742012 (protein)
Location Chr 9: 94.01 - 94.1 Mb Chr 13: 49.69 - 49.75 Mb
Pubmed search [1] [2]

Isoleucyl-tRNA synthetase, also known as IARS, is a human gene.[1]

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. Isoleucine-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family and has been identified as a target of autoantibodies in the autoimmune disease polymyositis/dermatomyositis. Two alternatively spliced variants have been isolated that represent alternate 5' UTRs.[1]

[edit] References

[edit] Further reading

  • 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. 
  • Nichols RC, Raben N, Boerkoel CF, Plotz PH (1995). "Human isoleucyl-tRNA synthetase: sequence of the cDNA, alternative mRNA splicing, and the characteristics of an unusually long C-terminal extension.". Gene 155 (2): 299–304. PMID 7721108. 
  • Shiba K, Suzuki N, Shigesada K, et al. (1994). "Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit.". Proc. Natl. Acad. Sci. U.S.A. 91 (16): 7435–9. PMID 8052601. 
  • Nichols RC, Blinder J, Pai SI, et al. (1997). "Assignment of two human autoantigen genes-isoleucyl-tRNA synthetase locates to 9q21 and lysyl-tRNA synthetase locates to 16q23-q24.". Genomics 36 (1): 210–3. doi:10.1006/geno.1996.0449. PMID 8812440. 
  • Rho SB, Lee KH, Kim JW, et al. (1996). "Interaction between human tRNA synthetases involves repeated sequence elements.". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10128–33. PMID 8816763. 
  • Degoul F, Brulé H, Cepanec C, et al. (1998). "Isoleucylation properties of native human mitochondrial tRNAIle and tRNAIle transcripts. Implications for cardiomyopathy-related point mutations (4269, 4317) in the tRNAIle gene.". Hum. Mol. Genet. 7 (3): 347–54. PMID 9466989. 
  • 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. 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. 
  • 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. 
  • 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. 
  • Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9.". Nature 429 (6990): 369–74. doi:10.1038/nature02465. PMID 15164053. 
  • 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. 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: 89. doi:10.1038/msb4100134. PMID 17353931. 


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