IARS

For other uses, see IARS (disambiguation).

IARS1
Identifiers
Aliases	IARS1, isoleucyl-tRNA synthetase 1, ILERS, isoleucyl-tRNA synthetase, PRO0785, GRIDHH, IRS, ILRS, IARS
External IDs	OMIM: 600709; MGI: 2145219; HomoloGene: 5325; GeneCards: IARS1; OMA:IARS1 - orthologs
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 6.1.1.5 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 9 (human) Band 9q22.31 Start 92,210,207 bp End 92,293,756 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A5 Start 49,835,576 bp End 49,887,743 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cartilage tissue corpus epididymis middle temporal gyrus tail of epididymis Skeletal muscle tissue of biceps brachii caput epididymis right ventricle oral cavity glutes trabecular bone Top expressed in primary oocyte motor neuron secondary oocyte primitive streak tail of embryo migratory enteric neural crest cell lacrimal gland seminal vesicula somite Gonadal ridge More reference expression data BioGPS More reference expression data
Gene ontology Molecular function aminoacyl-tRNA ligase activity nucleotide binding ligase activity protein binding GTPase binding ATP binding aminoacyl-tRNA editing activity tRNA binding isoleucine-tRNA ligase activity Cellular component membrane extracellular exosome cytoplasm aminoacyl-tRNA synthetase multienzyme complex cytosol Biological process protein biosynthesis tRNA aminoacylation for protein translation osteoblast differentiation regulation of translational fidelity isoleucyl-tRNA aminoacylation aminoacyl-tRNA metabolism involved in translational fidelity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3376 105148 Ensembl ENSG00000196305 ENSMUSG00000037851 UniProt P41252 Q6P0M4 Q8BU30 RefSeq (mRNA) NM_002161 NM_013417 NM_001374299 NM_001374300 NM_001374301 NM_172015 RefSeq (protein) NP_002152 NP_038203 NP_001361228 NP_001361229 NP_001361230 NP_001365498 NP_001365500 NP_001365501 NP_001365502 NP_001365503 NP_001365504 NP_001365505 NP_001365506 NP_001365507 NP_001365508 NP_001365509 NP_001365511 NP_001365512 NP_001365513 NP_001365514 NP_001365515 NP_002152.2 NP_742012 Location (UCSC) Chr 9: 92.21 – 92.29 Mb Chr 13: 49.84 – 49.89 Mb PubMed search
Wikidata
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Isoleucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the IARS1 gene.

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.

Interactions

IARS has been shown to interact with EPRS.

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. doi:10.1016/S0021-9258(18)98629-1. 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. Bibcode:1994PNAS...91.7435S. 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. Bibcode:1996PNAS...9310128R. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 11683986.
• Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. Bibcode:2004Natur.429..369H. 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.