IARS

Last updated

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
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002161
NM_013417
NM_001374299
NM_001374300
NM_001374301

Contents

NM_172015

RefSeq (protein)

NP_742012

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

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

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000196305 Ensembl, May 2017
  2. 1 2 3 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. 1 2 "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