IARS

IARS
Identifiers
Aliases	IARS, IARS1, ILERS, ILRS, IRS, PRO0785, isoleucyl-tRNA synthetase
External IDs	MGI: 2145219 HomoloGene: 5325 GeneCards: IARS
Gene ontology Molecular function • aminoacyl-tRNA ligase activity • nucleotide binding • isoleucine-tRNA ligase activity • ligase activity • protein binding • GTPase binding • ATP binding • aminoacyl-tRNA editing activity • tRNA binding Cellular component • cytoplasm • membrane • nucleoplasm • extracellular exosome • cytosol Biological process • translation • tRNA aminoacylation for protein translation • osteoblast differentiation • regulation of translational fidelity • isoleucyl-tRNA aminoacylation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3376	105148
Ensembl	ENSG00000196305	ENSMUSG00000037851
UniProt	P41252 Q6P0M4	Q8BU30
RefSeq (mRNA)	NM_002161 NM_013417	NM_172015
RefSeq (protein)	NP_002152.2 NP_038203.2 NP_002152.2	NP_742012.2
Location (UCSC)	Chr 9: 92.21 – 92.29 Mb	Chr 13: 49.68 – 49.73 Mb
PubMed search	[1]	[2]
Wikidata

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Isoleucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the IARS gene.^[3][4]

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.^[4]

Interactions

IARS has been shown to interact with EPRS.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Nichols RC, Blinder J, Pai SI, Ge Q, Targoff IN, Plotz PH, Liu P (Feb 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.
4. "Entrez Gene: IARS isoleucyl-tRNA synthetase".
5. Rho, S B; Lee J S; Jeong E J; Kim K S; Kim Y G; Kim S (May 1998). "A multifunctional repeated motif is present in human bifunctional tRNA synthetase". J. Biol. Chem. UNITED STATES. 273 (18): 11267–73. doi:10.1074/jbc.273.18.11267. ISSN 0021-9258. PMID 9556618.

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. doi:10.1016/0378-1119(94)00634-5. 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. doi:10.1073/pnas.91.16.7435. PMC 44415. PMID 8052601.
• 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. doi:10.1073/pnas.93.19.10128. PMC 38348. 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. doi:10.1093/hmg/7.3.347. 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. 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.
• 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.
• 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. PMC 2734081. 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. 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.