IARS

Protein-coding gene in the species Homo sapiens

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
Gene location (Human)
Chromosome 9 (human)
Chr.Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for IARS1
Genomic location for IARS1
Band9q22.31Start92,210,207 bp[1]
End92,293,756 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for IARS1
Genomic location for IARS1
Band13|13 A5Start49,835,576 bp[2]
End49,887,743 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
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_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 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

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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196305 – Ensembl, May 2017
  2. ^ a b c 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. ^ 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

  • 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.


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