PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30940768-7	2019	Through in vitro methylation assays, we validated a set of PRMT5 targets identified by mass spectrometry and provided previously unknown mechanistic insights into the preference of the enzyme to methylate arginine sandwiched between two neighboring glycines (a Gly-Arg-Gly, or "GRG," sequence).	Glycine	249-257	protein arginine methyltransferase 5	Homo sapiens	59-64	
23261437-1	2013	Epstein-Barr Virus Nuclear Antigen (EBNA) 2 features an Arginine-Glycine repeat (RG) domain at amino acid positions 335-360, which is a known target for protein arginine methyltransferaser 5 (PRMT5).	Glycine	65-72	protein arginine methyltransferase 5	Homo sapiens	192-197	
14583623-3	2004	Here, we demonstrate that the human FIB N-terminal glycine- and arginine-rich domain (residues 1-77) and its spacer region 1 (78-132) interact with splicing factor 2-associated p32 (SF2A-p32) and that the FIB methyltransferase-like domain (133-321) interacts with protein-arginine methyltransferase 5 (PRMT5, Janus kinase-binding protein 1).	Glycine	51-58	protein arginine methyltransferase 5	Homo sapiens	264-300	
14583623-3	2004	Here, we demonstrate that the human FIB N-terminal glycine- and arginine-rich domain (residues 1-77) and its spacer region 1 (78-132) interact with splicing factor 2-associated p32 (SF2A-p32) and that the FIB methyltransferase-like domain (133-321) interacts with protein-arginine methyltransferase 5 (PRMT5, Janus kinase-binding protein 1).	Glycine	51-58	protein arginine methyltransferase 5	Homo sapiens	302-307