PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28069943-8	2017	Molecular dynamics simulations have shown that the in silico acetylation of K244 induces conformational changes in TyrRS near the NLS, which may promote the nuclear translocation of acetylated TyrRS.	k244	76-80	tyrosyl-tRNA synthetase 1	Homo sapiens	115-120	
28069943-8	2017	Molecular dynamics simulations have shown that the in silico acetylation of K244 induces conformational changes in TyrRS near the NLS, which may promote the nuclear translocation of acetylated TyrRS.	k244	76-80	tyrosyl-tRNA synthetase 1	Homo sapiens	193-198	
28069943-9	2017	Herein, we show that the acetylated K244 residue of TyrRS protects against DNA damage in mammalian cells and zebrafish by activating DNA repair genes downstream of transcription factor E2F1.	k244	36-40	tyrosyl-tRNA synthetase 1	Homo sapiens	52-57