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{{Infobox_gene}}
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'''Arginyl-tRNA synthetase, cytoplasmic''' is an [[enzyme]] that in humans is encoded by the ''RARS'' [[gene]].<ref name="pmid7590355">{{cite journal |vauthors=Girjes AA, Hobson K, Chen P, Lavin MF | title = Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase | journal = Gene | volume = 164 | issue = 2 | pages = 347–50 |date=December 1995 | pmid = 7590355 | pmc =  | doi =10.1016/0378-1119(95)00502-W }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RARS arginyl-tRNA synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5917| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Arginyl-tRNA synthetase
| HGNCid = 9870
| Symbol = RARS
| AltSymbols =; ArgRS; DALRD1; MGC8641
| OMIM = 107820
| ECnumber =
| Homologene = 68281
| MGIid = 1914297
  | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004814 |text = arginine-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:0006420 |text = arginyl-tRNA aminoacylation}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5917
    | Hs_Ensembl = ENSG00000113643
    | Hs_RefseqProtein = NP_002878
    | Hs_RefseqmRNA = NM_002887
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 167846041
    | Hs_GenLoc_end = 167878885
    | Hs_Uniprot = P54136
    | Mm_EntrezGene = 104458
    | Mm_Ensembl = ENSMUSG00000018848
    | Mm_RefseqmRNA = NM_025936
    | Mm_RefseqProtein = NP_080212
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 35651806
    | Mm_GenLoc_end = 35677929
    | Mm_Uniprot = Q3THP2
  }}
}}
'''Arginyl-tRNA synthetase''', also known as '''RARS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RARS arginyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5917| accessdate = }}</ref>


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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. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.<ref name="entrez">{{cite web | title = Entrez Gene: RARS arginyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5917| 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. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.<ref name="entrez"/>
}}
}}
==Genetics==
Mutations in RARS cause {{SWL|type=mutation_results_in|target=hypomyelination|label=hypomyelination}}.<ref>{{Cite journal
| pmid = 24777941
| year = 2014
| author1 = Wolf
| first1 = N. I.
| title = Mutations in RARS cause hypomyelination
| journal = Annals of Neurology
| pages = 134–9
| last2 = Salomons
| first2 = G. S.
| last3 = Rodenburg
| first3 = R. J.
| last4 = Pouwels
| first4 = P. J.
| last5 = Schieving
| first5 = J. H.
| last6 = Derks
| first6 = T. G.
| last7 = Fock
| first7 = J. M.
| last8 = Rump
| first8 = P
| last9 = Van Beek
| first9 = D. M.
| last10 = Van Der Knaap
| first10 = M. S.
| last11 = Waisfisz
| first11 = Q
| doi = 10.1002/ana.24167
| volume=76
| issue=1
}}</ref>
==Interactions==
RARS (gene) has been shown to [[Protein-protein interaction|interact]] with [[QARS]].<ref name=pmid10801842>{{cite journal |last=Kim |first=T |authorlink= |author2=Park S G |author3=Kim J E |author4=Seol W |author5=Ko Y G |author6=Kim S  |date=July 2000  |title=Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex |journal=J. Biol. Chem. |volume=275 |issue=28 |pages=21768–72 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10801842 |doi = 10.1074/jbc.M002404200 | 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=McCune SA, Yu PL, Nance WE |title=A genetic study of erythrocyte arginine-tRNA synthetase activity in man. |journal=Acta geneticae medicae et gemellologiae |volume=26 |issue= 1 |pages= 21-7 |year= 1977 |pmid= 562050 |doi=  }}
*{{cite journal  |vauthors=McCune SA, Yu PL, Nance WE |title=A genetic study of erythrocyte arginine-tRNA synthetase activity in man. |journal=Acta geneticae medicae et gemellologiae |volume=26 |issue= 1 |pages= 21–7 |year= 1977 |pmid= 562050 |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=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=Wang HY, Pan F |title=Kinetic mechanism of arginyl-tRNA synthetase from human placenta. |journal=Int. J. Biochem. |volume=16 |issue= 12 |pages= 1379-85 |year= 1985 |pmid= 6530022 |doi=  }}
*{{cite journal  |vauthors=Wang HY, Pan F |title=Kinetic mechanism of arginyl-tRNA synthetase from human placenta. |journal=Int. J. Biochem. |volume=16 |issue= 12 |pages= 1379–85 |year= 1985 |pmid= 6530022 |doi=10.1016/0020-711X(84)90244-1 }}
*{{cite journal  | author=Girjes AA, Hobson K, Chen P, Lavin MF |title=Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase. |journal=Gene |volume=164 |issue= 2 |pages= 347-50 |year= 1995 |pmid= 7590355 |doi=  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |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=Park SG, Jung KH, Lee JS, etal |title=Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 16673–6 |year= 1999 |pmid= 10358004 |doi=10.1074/jbc.274.24.16673  }}
*{{cite journal | author=Park SG, Jung KH, Lee JS, ''et al.'' |title=Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 16673-6 |year= 1999 |pmid= 10358004 |doi= }}
*{{cite journal   |vauthors=Kim T, Park SG, Kim JE, etal |title=Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21768–72 |year= 2000 |pmid= 10801842 |doi= 10.1074/jbc.M002404200 }}
*{{cite journal | author=Kim T, Park SG, Kim JE, ''et al.'' |title=Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21768-72 |year= 2000 |pmid= 10801842 |doi= 10.1074/jbc.M002404200 }}
*{{cite journal   |vauthors=Kang J, Kim T, Ko YG, etal |title=Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31682–8 |year= 2000 |pmid= 10913161 |doi= 10.1074/jbc.M909965199 }}
*{{cite journal | author=Kang J, Kim T, Ko YG, ''et al.'' |title=Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31682-8 |year= 2000 |pmid= 10913161 |doi= 10.1074/jbc.M909965199 }}
*{{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=Gevaert K, Goethals M, Martens L, etal |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Ling C, Yao YN, Zheng YG, etal |title=The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex |journal=J. Biol. Chem. |volume=280 |issue= 41 |pages= 34755–63 |year= 2005 |pmid= 16055448 |doi= 10.1074/jbc.M413511200 }}
*{{cite journal | author=Ling C, Yao YN, Zheng YG, ''et al.'' |title=The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex. |journal=J. Biol. Chem. |volume=280 |issue= 41 |pages= 34755-63 |year= 2005 |pmid= 16055448 |doi= 10.1074/jbc.M413511200 }}
*{{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 }}
*{{cite journal   |vauthors=Bottoni A, Vignali C, Piccin D, etal |title=Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines |journal=J. Cell. Physiol. |volume=212 |issue= 2 |pages= 293–7 |year= 2007 |pmid= 17443684 |doi= 10.1002/jcp.21083 }}
*{{cite journal | author=Bottoni A, Vignali C, Piccin D, ''et al.'' |title=Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines. |journal=J. Cell. Physiol. |volume=212 |issue= 2 |pages= 293-7 |year= 2007 |pmid= 17443684 |doi= 10.1002/jcp.21083 }}
}}
}}
{{refend}}
{{refend}}


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Revision as of 08:55, 10 September 2017

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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
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View/Edit Human

Arginyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the RARS 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. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.[2]

Genetics

Mutations in RARS cause hypomyelination .[3]

Interactions

RARS (gene) has been shown to interact with QARS.[4]

References

  1. ↑ Girjes AA, Hobson K, Chen P, Lavin MF (December 1995). "Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase". Gene. 164 (2): 347–50. doi:10.1016/0378-1119(95)00502-W. PMID 7590355.
  2. ↑ 2.0 2.1 "Entrez Gene: RARS arginyl-tRNA synthetase".
  3. ↑ Wolf, N. I.; Salomons, G. S.; Rodenburg, R. J.; Pouwels, P. J.; Schieving, J. H.; Derks, T. G.; Fock, J. M.; Rump, P; Van Beek, D. M.; Van Der Knaap, M. S.; Waisfisz, Q (2014). "Mutations in RARS cause hypomyelination". Annals of Neurology. 76 (1): 134–9. doi:10.1002/ana.24167. PMID 24777941.
  4. ↑ Kim, T; Park S G; Kim J E; Seol W; Ko Y G; Kim S (July 2000). "Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex". J. Biol. Chem. UNITED STATES. 275 (28): 21768–72. doi:10.1074/jbc.M002404200. ISSN 0021-9258. PMID 10801842.

Further reading



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