YARS

Tyrosyl-tRNA synthetase, also known as YARS, is a human gene.cite web | title = Entrez Gene: YARS tyrosyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8565| accessdate = ]

PBB_Summary
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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. 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.cite web | title = Entrez Gene: YARS tyrosyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8565| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Ewalt KL, Schimmel P |title=Activation of angiogenic signaling pathways by two human tRNA synthetases. |journal=Biochemistry |volume=41 |issue= 45 |pages= 13344–9 |year= 2002 |pmid= 12416978 |doi=
*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 | author=Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P |title=Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 166–70 |year= 1996 |pmid= 8552597 |doi=
*cite journal | author=Kleeman TA, Wei D, Simpson KL, First EA |title=Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. |journal=J. Biol. Chem. |volume=272 |issue= 22 |pages= 14420–5 |year= 1997 |pmid= 9162081 |doi=
*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 | author=Wakasugi K, Quinn CL, Tao N, Schimmel P |title=Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant. |journal=EMBO J. |volume=17 |issue= 1 |pages= 297–305 |year= 1998 |pmid= 9427763 |doi= 10.1093/emboj/17.1.297
*cite journal | author=Wakasugi K, Schimmel P |title=Two distinct cytokines released from a human aminoacyl-tRNA synthetase. |journal=Science |volume=284 |issue= 5411 |pages= 147–51 |year= 1999 |pmid= 10102815 |doi=
*cite journal | author=Wakasugi K, Schimmel P |title=Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23155–9 |year= 1999 |pmid= 10438485 |doi=
*cite journal | author=Austin J, First EA |title=Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase. |journal=J. Biol. Chem. |volume=277 |issue= 17 |pages= 14812–20 |year= 2002 |pmid= 11856731 |doi= 10.1074/jbc.M103396200
*cite journal | author=Austin J, First EA |title=Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase. |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20243–8 |year= 2002 |pmid= 11927599 |doi= 10.1074/jbc.M201923200
*cite journal | author=Wakasugi K, Slike BM, Hood J, "et al." |title=Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase. |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20124–6 |year= 2002 |pmid= 11956181 |doi= 10.1074/jbc.C200126200
*cite journal | author=Austin J, First EA |title=Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 28394–9 |year= 2002 |pmid= 12016229 |doi= 10.1074/jbc.M204404200
*cite journal | author=Yang XL, Skene RJ, McRee DE, Schimmel P |title=Crystal structure of a human aminoacyl-tRNA synthetase cytokine. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 24 |pages= 15369–74 |year= 2003 |pmid= 12427973 |doi= 10.1073/pnas.242611799
*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 | author=Jia J, Li B, Jin Y, Wang D |title=Expression, purification, and characterization of human tyrosyl-tRNA synthetase. |journal=Protein Expr. Purif. |volume=27 |issue= 1 |pages= 104–8 |year= 2003 |pmid= 12509991 |doi=
*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 | author=Jordanova A, Thomas FP, Guergueltcheva V, "et al." |title=Dominant intermediate Charcot-Marie-Tooth type C maps to chromosome 1p34-p35. |journal=Am. J. Hum. Genet. |volume=73 |issue= 6 |pages= 1423–30 |year= 2004 |pmid= 14606043 |doi=
*cite journal | author=Yang XL, Otero FJ, Skene RJ, "et al." |title=Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 26 |pages= 15376–80 |year= 2004 |pmid= 14671330 |doi= 10.1073/pnas.2136794100
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285

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