Tyrosyl tRNA Synthetase (YARS)

CMTDIC; TYRRS; YRS; YTS; Tyrosine tRNA Ligase 1,Cytoplasmic

SPN	T780
HGNC	12840
MGI	2147627
PubMed	15840835
RGD	1307616
UniProt	P54577
Wiki	YARS

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.

Reference

"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. 93:166-170(1996) [PubMed] [Europe PMC] [Abstract]

"Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine."
J. Biol. Chem. 272:14420-14425(1997) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]