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IARS

From Wikipedia, the free encyclopedia

IARS1
Identifiers
AliasesIARS1, isoleucyl-tRNA synthetase 1, ILERS, isoleucyl-tRNA synthetase, PRO0785, GRIDHH, IRS, ILRS, IARS
External IDsOMIM: 600709; MGI: 2145219; HomoloGene: 5325; GeneCards: IARS1; OMA:IARS1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002161
NM_013417
NM_001374299
NM_001374300
NM_001374301

NM_172015

RefSeq (protein)

NP_742012

Location (UCSC)Chr 9: 92.21 – 92.29 MbChr 13: 49.84 – 49.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Isoleucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the IARS1 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

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

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196305Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037851Ensembl, 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.
  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.
  6. ^ a b "Entrez Gene: IARS1 isoleucyl-tRNA synthetase".
  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. 273 (18). UNITED STATES: 11267–73. doi:10.1074/jbc.273.18.11267. ISSN 0021-9258. PMID 9556618.

Further reading

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