RARS - Arginine--tRNA ligase, cytoplasmic - human protein (Function)
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RARS »  Arginine--tRNA ligase, cytoplasmic   [ EC ]
Protein also known as:  Arginyl-tRNA synthetase (ArgRS).
Gene name:  RARS
Entry whose protein(s) existence is based on evidence at protein level
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Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.  
  • CuratedUniProtKB
GO molecular function 
Arginine bindingdefinition[GO:0034618] silver  
  • IEAOrtholog Compara
ATP bindingdefinition[GO:0005524] silver  
  • IEAOrtholog Compara
Protein bindingdefinition[GO:0005515]  
  • IPIIntAct
tRNA bindingdefinition[GO:0000049] silver  
  • IEAOrtholog Compara
GO biological process 
Arginyl-tRNA aminoacylationdefinition[GO:0006420] silver  
  • IEAOrtholog Compara
Enzymatic activity 
This protein acts as an enzyme. It is known to catalyze the following reaction
EC ATP + L-arginine + tRNA(Arg) AMP + diphosphate + L-arginyl-tRNA(Arg).  
  • CuratedUniProtKB
According to KEGG, this protein belongs to the following pathway:
Aminoacyl-tRNA biosynthesis  hsa00970+5917  
According to Reactome, this protein belongs to the following pathway:
Cytosolic tRNA aminoacylation  REACT_15306  

Biophysicochemical properties

Kinetic parameters
KM 0.41 uM for calf liver tRNA-Arg (arginylation at 37 Celsius)
KM 3.9 uM for arginine (ATP-PPi exchange at 37 degrees Celsius)
KM 3.5 uM for arginine (arginylation at 37 degrees Celsius)
KM 1183 uM for ATP (ATP-PPi exchange at 37 Celsius)
KM 0.05 uM for calf liver tRNA-Arg (ATP-PPi exchange at 37 Celsius)
KM 910 uM for ATP (arginylation at 37 Celsius)


Biological process 
Protein biosynthesis  definition   [KW-0648]
Molecular function 
Aminoacyl-tRNA synthetase  definition   [KW-0030]
Ligase  definition   [KW-0436]
Technical term 
Reference proteome  definition   [KW-1185]

Further external links

GeneWiki: RARS_(gene)
GenomeRNAi: 5917
PRO: PR:P54136