YARS

Tyrosyl-tRNA synthetase
PDB rendering based on 1n3l.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1N3L​, 1NTG​, 1Q11​, 4Q93​, 4QBT​
Identifiers
Symbols	YARS ; CMTDIC; TYRRS; YRS; YTS
External IDs	OMIM: 603623 MGI: 2147627 HomoloGene: 2730 ChEMBL: 3179 GeneCards: YARS Gene
EC number	6.1.1.1
Gene ontology Molecular function • tRNA binding • isoleucine-tRNA ligase activity • tyrosine-tRNA ligase activity • signal transducer activity • interleukin-8 receptor binding • ATP binding • poly(A) RNA binding Cellular component • extracellular space • nucleus • cytoplasm • cytosol Biological process • tRNA aminoacylation for protein translation • isoleucyl-tRNA aminoacylation • tyrosyl-tRNA aminoacylation • apoptotic process • signal transduction • gene expression Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8565	107271
Ensembl	ENSG00000134684	ENSMUSG00000028811
UniProt	P54577	Q91WQ3
RefSeq (mRNA)	NM_003680	NM_134151
RefSeq (protein)	NP_003671	NP_598912
Location (UCSC)	Chr 1: 32.78 – 32.82 Mb	Chr 4: 129.19 – 129.22 Mb
PubMed search

Tyrosyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the YARS gene.^[1][2][3]

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. 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.^[3]Recently, tyrosyl tRNA synthetase (TyrRS) has been demonstrated as the biologically and functionally significant target for resveratrol^[4]

References

1. 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 40199. PMID 8552597.
2. 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.
3. "Entrez Gene: YARS tyrosyl-tRNA synthetase".
4. http://www.nature.com/nature/journal/vaop/ncurrent/full/nature14028.html

Further reading

• Ewalt KL, Schimmel P (2002). "Activation of angiogenic signaling pathways by two human tRNA synthetases.". Biochemistry 41 (45): 13344–9. doi:10.1021/bi020537k. PMID 12416978.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Wakasugi K, Quinn CL, Tao N, Schimmel P (1998). "Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant". EMBO J. 17 (1): 297–305. doi:10.1093/emboj/17.1.297. PMC 1170380. PMID 9427763.
• Wakasugi K, Schimmel P (1999). "Two distinct cytokines released from a human aminoacyl-tRNA synthetase". Science 284 (5411): 147–51. doi:10.1126/science.284.5411.147. PMID 10102815.
• Wakasugi K, Schimmel P (1999). "Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase". J. Biol. Chem. 274 (33): 23155–9. doi:10.1074/jbc.274.33.23155. PMID 10438485.
• Austin J, First EA (2002). "Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase". J. Biol. Chem. 277 (17): 14812–20. doi:10.1074/jbc.M103396200. PMID 11856731.
• Austin J, First EA (2002). "Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase". J. Biol. Chem. 277 (23): 20243–8. doi:10.1074/jbc.M201923200. PMID 11927599.
• Wakasugi K, Slike BM, Hood J, et al. (2002). "Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase". J. Biol. Chem. 277 (23): 20124–6. doi:10.1074/jbc.C200126200. PMID 11956181.
• Austin J, First EA (2002). "Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases". J. Biol. Chem. 277 (32): 28394–9. doi:10.1074/jbc.M204404200. PMID 12016229.
• Yang XL, Skene RJ, McRee DE, Schimmel P (2003). "Crystal structure of a human aminoacyl-tRNA synthetase cytokine". Proc. Natl. Acad. Sci. U.S.A. 99 (24): 15369–74. doi:10.1073/pnas.242611799. PMC 137723. PMID 12427973.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Jia J, Li B, Jin Y, Wang D (2003). "Expression, purification, and characterization of human tyrosyl-tRNA synthetase". Protein Expr. Purif. 27 (1): 104–8. doi:10.1016/S1046-5928(02)00576-4. PMID 12509991.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Jordanova A, Thomas FP, Guergueltcheva V, et al. (2004). "Dominant intermediate Charcot-Marie-Tooth type C maps to chromosome 1p34-p35". Am. J. Hum. Genet. 73 (6): 1423–30. doi:10.1086/379792. PMC 1180404. PMID 14606043.
• Yang XL, Otero FJ, Skene RJ, et al. (2004). "Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains". Proc. Natl. Acad. Sci. U.S.A. 100 (26): 15376–80. doi:10.1073/pnas.2136794100. PMC 307575. PMID 14671330.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.