Arginyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the RARS 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. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.[6]

Genetics

Mutations in RARS cause hypomyelination.[7]

Interactions

RARS (gene) has been shown to interact with QARS.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000113643Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018848Ensembl, 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. ^ Girjes AA, Hobson K, Chen P, Lavin MF (October 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.
  6. ^ a b "Entrez Gene: RARS arginyl-tRNA synthetase".
  7. ^ Wolf NI, Salomons GS, Rodenburg RJ, Pouwels PJ, Schieving JH, Derks TG, Fock JM, Rump P, van Beek DM, van der Knaap MS, Waisfisz Q (July 2014). "Mutations in RARS cause hypomyelination". Annals of Neurology. 76 (1): 134–9. doi:10.1002/ana.24167. PMID 24777941. S2CID 27717491.
  8. ^ Kim T, Park SG, Kim JE, Seol W, Ko YG, Kim S (July 2000). "Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex". The Journal of Biological Chemistry. 275 (28): 21768–72. doi:10.1074/jbc.M002404200. PMID 10801842.

Further reading

  • Overview of all the structural information available in the PDB for UniProt: P54136 (Human Arginine--tRNA ligase, cytoplasmic) at the PDBe-KB.
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