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*{{cite journal  | author=Norcum MT |title=Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15398–405 |year= 1991 |pmid= 1651330 |doi=  }}
*{{cite journal  | author=Norcum MT |title=Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15398–405 |year= 1991 |pmid= 1651330 |doi=  }}
*{{cite journal  |vauthors=Nichols RC, Raben N, Boerkoel CF, Plotz PH |title=Human isoleucyl-tRNA synthetase: sequence of the cDNA, alternative mRNA splicing, and the characteristics of an unusually long C-terminal extension. |journal=Gene |volume=155 |issue= 2 |pages= 299–304 |year= 1995 |pmid= 7721108 |doi=10.1016/0378-1119(94)00634-5  }}
*{{cite journal  |vauthors=Nichols RC, Raben N, Boerkoel CF, Plotz PH |title=Human isoleucyl-tRNA synthetase: sequence of the cDNA, alternative mRNA splicing, and the characteristics of an unusually long C-terminal extension. |journal=Gene |volume=155 |issue= 2 |pages= 299–304 |year= 1995 |pmid= 7721108 |doi=10.1016/0378-1119(94)00634-5  }}
*{{cite journal  |vauthors=Shiba K, Suzuki N, Shigesada K, etal |title=Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 16 |pages= 7435–9 |year= 1994 |pmid= 8052601 |doi=10.1073/pnas.91.16.7435  | pmc=44415  }}
*{{cite journal  |vauthors=Shiba K, Suzuki N, Shigesada K, etal |title=Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 16 |pages= 7435–9 |year= 1994 |pmid= 8052601 |doi=10.1073/pnas.91.16.7435  | pmc=44415  |bibcode=1994PNAS...91.7435S }}
*{{cite journal  |vauthors=Rho SB, Lee KH, Kim JW, etal |title=Interaction between human tRNA synthetases involves repeated sequence elements. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 19 |pages= 10128–33 |year= 1996 |pmid= 8816763 |doi=10.1073/pnas.93.19.10128  | pmc=38348  }}
*{{cite journal  |vauthors=Rho SB, Lee KH, Kim JW, etal |title=Interaction between human tRNA synthetases involves repeated sequence elements. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 19 |pages= 10128–33 |year= 1996 |pmid= 8816763 |doi=10.1073/pnas.93.19.10128  | pmc=38348  |bibcode=1996PNAS...9310128R }}
*{{cite journal  |vauthors=Degoul F, Brulé H, Cepanec C, etal |title=Isoleucylation properties of native human mitochondrial tRNAIle and tRNAIle transcripts. Implications for cardiomyopathy-related point mutations (4269, 4317) in the tRNAIle gene. |journal=Hum. Mol. Genet. |volume=7 |issue= 3 |pages= 347–54 |year= 1998 |pmid= 9466989 |doi=10.1093/hmg/7.3.347  }}
*{{cite journal  |vauthors=Degoul F, Brulé H, Cepanec C, etal |title=Isoleucylation properties of native human mitochondrial tRNAIle and tRNAIle transcripts. Implications for cardiomyopathy-related point mutations (4269, 4317) in the tRNAIle gene. |journal=Hum. Mol. Genet. |volume=7 |issue= 3 |pages= 347–54 |year= 1998 |pmid= 9466989 |doi=10.1093/hmg/7.3.347  }}
*{{cite journal  |vauthors=Rho SB, Lee JS, Jeong EJ, etal |title=A multifunctional repeated motif is present in human bifunctional tRNA synthetase. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11267–73 |year= 1998 |pmid= 9556618 |doi=10.1074/jbc.273.18.11267  }}
*{{cite journal  |vauthors=Rho SB, Lee JS, Jeong EJ, etal |title=A multifunctional repeated motif is present in human bifunctional tRNA synthetase. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11267–73 |year= 1998 |pmid= 9556618 |doi=10.1074/jbc.273.18.11267  }}
*{{cite journal  |vauthors=Quevillon S, Robinson JC, Berthonneau E, etal |title=Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. |journal=J. Mol. Biol. |volume=285 |issue= 1 |pages= 183–95 |year= 1999 |pmid= 9878398 |doi= 10.1006/jmbi.1998.2316 }}
*{{cite journal  |vauthors=Quevillon S, Robinson JC, Berthonneau E, etal |title=Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. |journal=J. Mol. Biol. |volume=285 |issue= 1 |pages= 183–95 |year= 1999 |pmid= 9878398 |doi= 10.1006/jmbi.1998.2316 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M }}
*{{cite journal  |vauthors=Bouwmeester T, Bauch A, Ruffner H, etal |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal  |vauthors=Bouwmeester T, Bauch A, Ruffner H, etal |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal  |vauthors=Humphray SJ, Oliver K, Hunt AR, etal |title=DNA sequence and analysis of human chromosome 9. |journal=Nature |volume=429 |issue= 6990 |pages= 369–74 |year= 2004 |pmid= 15164053 |doi= 10.1038/nature02465  | pmc=2734081 }}
*{{cite journal  |vauthors=Humphray SJ, Oliver K, Hunt AR, etal |title=DNA sequence and analysis of human chromosome 9. |journal=Nature |volume=429 |issue= 6990 |pages= 369–74 |year= 2004 |pmid= 15164053 |doi= 10.1038/nature02465  | pmc=2734081 |bibcode=2004Natur.429..369H }}
*{{cite journal  |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406  | pmc=1356129 }}
*{{cite journal  |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406  | pmc=1356129 }}
*{{cite journal  |vauthors=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134  | pmc=1847948 }}
*{{cite journal  |vauthors=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134  | pmc=1847948 }}

Revision as of 00:36, 24 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Isoleucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the IARS gene.[1][2]

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.[2]

Interactions

IARS has been shown to interact with EPRS.[3]

References

  1. Nichols RC, Blinder J, Pai SI, Ge Q, Targoff IN, Plotz PH, Liu P (Feb 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.
  2. 2.0 2.1 "Entrez Gene: IARS isoleucyl-tRNA synthetase".
  3. 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