IARS: Difference between revisions

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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
'''Isoleucyl-tRNA synthetase, cytoplasmic''' is an [[enzyme]] that in humans is encoded by the ''IARS'' [[gene]].<ref name="pmid8812440">{{cite journal |vauthors=Nichols RC, Blinder J, Pai SI, Ge Q, Targoff IN, Plotz PH, Liu P | title = Assignment of two human autoantigen genes-isoleucyl-tRNA synthetase locates to 9q21 and lysyl-tRNA synthetase locates to 16q23-q24 | journal = Genomics | volume = 36 | issue = 1 | pages = 210–3 |date=Feb 1997 | pmid = 8812440 | pmc =  | doi = 10.1006/geno.1996.0449 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: IARS isoleucyl-tRNA synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3376| accessdate = }}</ref>
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Isoleucyl-tRNA synthetase
| HGNCid = 5330
| Symbol = IARS
| AltSymbols =; FLJ20736; IARS1; ILRS; PRO0785
| OMIM = 600709
| ECnumber = 
| Homologene = 5325
| MGIid = 2145219
| GeneAtlas_image1 = PBB_GE_IARS_204744_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004812 |text = aminoacyl-tRNA ligase activity}} {{GNF_GO|id=GO:0004822 |text = isoleucine-tRNA ligase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006428 |text = isoleucyl-tRNA aminoacylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3376
    | Hs_Ensembl = ENSG00000196305
    | Hs_RefseqProtein = NP_002152
    | Hs_RefseqmRNA = NM_002161
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 94012310
    | Hs_GenLoc_end = 94095803
    | Hs_Uniprot = P41252
    | Mm_EntrezGene = 105148
    | Mm_Ensembl = ENSMUSG00000037851
    | Mm_RefseqmRNA = NM_172015
    | Mm_RefseqProtein = NP_742012
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 49694080
    | Mm_GenLoc_end = 49746196
    | Mm_Uniprot = Q3UWS7
  }}
}}
'''Isoleucyl-tRNA synthetase''', also known as '''IARS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IARS isoleucyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3376| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: IARS isoleucyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3376| accessdate = }}</ref>
| summary_text = [[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.<ref name="entrez" />
}}
}}
==Interactions==
IARS has been shown to [[Protein-protein interaction|interact]] with [[EPRS]].<ref name=pmid9556618>{{cite journal |doi=10.1074/jbc.273.18.11267 |last=Rho |first=S B |authorlink= |author2=Lee J S |author3=Jeong E J |author4=Kim K S |author5=Kim Y G |author6=Kim S  |date=May 1998 |title=A multifunctional repeated motif is present in human bifunctional tRNA synthetase |journal=J. Biol. Chem. |volume=273 |issue=18 |pages=11267–73 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9556618 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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  | author=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=  }}
*{{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 | author=Shiba K, Suzuki N, Shigesada K, ''et al.'' |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=  }}
*{{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  | author=Nichols RC, Blinder J, Pai SI, ''et al.'' |title=Assignment of two human autoantigen genes-isoleucyl-tRNA synthetase locates to 9q21 and lysyl-tRNA synthetase locates to 16q23-q24. |journal=Genomics |volume=36 |issue= 1 |pages= 210-3 |year= 1997 |pmid= 8812440 |doi= 10.1006/geno.1996.0449 }}
*{{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 | author=Rho SB, Lee KH, Kim JW, ''et al.'' |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=  }}
*{{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 | author=Degoul F, Brulé H, Cepanec C, ''et al.'' |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=  }}
*{{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 | author=Rho SB, Lee JS, Jeong EJ, ''et al.'' |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=  }}
*{{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 | author=Quevillon S, Robinson JC, Berthonneau E, ''et al.'' |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 | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{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 | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |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 | author=Humphray SJ, Oliver K, Hunt AR, ''et al.'' |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 }}
*{{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 | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |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 }}
*{{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 | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
}}
{{refend}}
{{refend}}


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Revision as of 23:25, 31 August 2017

For other uses, see IARS (disambiguation).

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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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



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