IARS

Isoleucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the IARS1 gene.[5][6]

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
Orthologs
SpeciesHumanMouse
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_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

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

  1. GRCh38: Ensembl release 89: ENSG00000196305 - Ensembl, May 2017
  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.
  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. "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. UNITED STATES. 273 (18): 11267–73. doi:10.1074/jbc.273.18.11267. ISSN 0021-9258. PMID 9556618.

Further reading


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