PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33929180-1	2021	Editing of the pre-mRNA of the DNA repair glycosylase NEIL1 results in substitution of a Lys with Arg in the lesion recognition loop of the enzyme.	Lysine	89-92	nei like DNA glycosylase 1	Homo sapiens	54-59	
23542007-6	2013	These observations are consistent with stabilization of the native NEIL1 structure via intramolecular, mostly electrostatic, interactions that were disrupted by mutating a positively charged (Lys-rich) cluster of residues (amino acids 355-360) near the C-terminus.	Lysine	192-195	nei like DNA glycosylase 1	Homo sapiens	67-72	
21068368-1	2010	Editing of the pre-mRNA for the DNA repair enzyme NEIL1 causes a lysine to arginine change in the lesion recognition loop of the protein.	Lysine	65-71	nei like DNA glycosylase 1	Homo sapiens	50-55	
18662981-7	2008	Fine structure mapping identified several Lys and Arg residues in this region that form salt bridges with Asp and Glu residues in NEIL1.	Lysine	42-45	nei like DNA glycosylase 1	Homo sapiens	130-135	
29698889-5	2018	NEIL1 mutant having the substitution of Lys 296-298 with neutral Ala loses nuclear localization, whereas Lys > Arg substitution (in 3KR mutant) at the same sites does not affect NEIL1"s nuclear localization or chromatin binding, presumably due to retention of the positive charge.	Lysine	40-43	nei like DNA glycosylase 1	Homo sapiens	0-5	
29698889-11	2018	We thus conclude that the major role of acetylable Lys residues in NEIL1 is to stabilize the formation of chromatin-bound repair complexes which protect cells from oxidative stress.	Lysine	51-54	nei like DNA glycosylase 1	Homo sapiens	67-72	
27924031-4	2017	We demonstrate that these enzymes are capable of polyubiquitylating NEIL1 in vitro, and that both catalyse ubiquitylation of NEIL1 within the same C-terminal lysine residues.	Lysine	158-164	nei like DNA glycosylase 1	Homo sapiens	68-73	
27924031-4	2017	We demonstrate that these enzymes are capable of polyubiquitylating NEIL1 in vitro, and that both catalyse ubiquitylation of NEIL1 within the same C-terminal lysine residues.	Lysine	158-164	nei like DNA glycosylase 1	Homo sapiens	125-130	
24382305-8	2014	Human NEIL1 is known to undergo editing whereby the lysine at position 242 is recoded into an arginine.	Lysine	52-58	nei like DNA glycosylase 1	Homo sapiens	6-11