IARS

IARS1
Identifiers
Aliases	IARS1, ILERS, ILRS, IRS, PRO0785, isoleucyl-tRNA synthetase, GRIDHH, IARS, isoleucyl-tRNA synthetase 1
External IDs	OMIM: 600709 MGI: 2145219 HomoloGene: 5325 GeneCards: IARS1
Gene location (Human)
Chr.	Chromosome 9 (human)[1]
End	92,293,756 bp[1]
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)[2]
End	49,734,267 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• aminoacyl-tRNA ligase activity; • nucleotide binding; • ligase activity; • GO:0001948 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
	3376
	105148
	ENSG00000196305
	ENSMUSG00000037851
	P41252; Q6P0M4
	Q8BU30
	NM_002161; NM_013417; NM_001374299; NM_001374300; NM_001374301
	NM_172015
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
	Wikidata
View/Edit Human	View/Edit Mouse

Isoleucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the IARS gene.[5][6]

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.[6]

Interactions

IARS has been shown to interact with EPRS.[7]

References

GRCh38: Ensembl release 89: ENSG00000196305 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000037851 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Nichols RC, Blinder J, Pai SI, Ge Q, Targoff IN, Plotz PH, Liu P (February 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.
"Entrez Gene: IARS isoleucyl-tRNA synthetase".
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.

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. 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000196305 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000037851 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8812440-5] Nichols RC, Blinder J, Pai SI, Ge Q, Targoff IN, Plotz PH, Liu P (February 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.

[entrez-6] "Entrez Gene: IARS isoleucyl-tRNA synthetase".

[pmid9556618-7] 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.

IARS

Interactions

References

Further reading