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Not to be confused with RS-24 Yars.
Protein YARS PDB 1n3l.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases YARS, CMTDIC, TYRRS, YRS, YTS, tyrosyl-tRNA synthetase
External IDs MGI: 2147627 HomoloGene: 2730 GeneCards: YARS
RNA expression pattern
PBB GE YARS 212048 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 1: 32.78 – 32.82 Mb Chr 4: 129.19 – 129.22 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Tyrosyl-tRNA synthetase, cytoplasmic, also known as Tyrosine-tRNA ligase, is an enzyme that in humans is encoded by the YARS gene.[3][4][5]

Aminoacyl-tRNA synthetases catalyze the aminoacylation of transfer RNA (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. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.[5] Recently, tyrosyl-tRNA synthetase has been demonstrated as the biologically and functionally significant target for resveratrol[6]

For a comparison of cytoplasmic human tyrosyl-tRNA synthetase with its mitochondrial counterpart and with tyrosyl-tRNA synthetases of other biological kingdoms and organisms, see the Wikipedia page on Tyrosine-tRNA ligase and a general review on their structures and functions.[7]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P (Feb 1996). "Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria". Proc Natl Acad Sci U S A. 93 (1): 166–70. doi:10.1073/pnas.93.1.166. PMC 40199Freely accessible. PMID 8552597. 
  4. ^ Kleeman TA, Wei D, Simpson KL, First EA (Jun 1997). "Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine". J Biol Chem. 272 (22): 14420–5. doi:10.1074/jbc.272.22.14420. PMID 9162081. 
  5. ^ a b "Entrez Gene: YARS tyrosyl-tRNA synthetase". 
  6. ^ http://www.nature.com/nature/journal/vaop/ncurrent/full/nature14028.html
  7. ^ Bedouelle, Hugues. "Tyrosyl-tRNA Synthetases". In: Madame Curie Bioscience Database [NCBI NBK6553]. Austin (TX): Landes Bioscience. 

Further reading[edit]