PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31680191-6	2020	Specifically, lysine 370/372/373 and 381/382/386 mutations decreased p53 stability, and lysine 305 mutation reduced p53 phosphorylation level at serine 15, while lysine 120 and 164 mutations decreased p53 acetylation level at lysine 382.	tyrosyl-lysine	14-20	tumor protein p53	Homo sapiens	69-72	
31680191-6	2020	Specifically, lysine 370/372/373 and 381/382/386 mutations decreased p53 stability, and lysine 305 mutation reduced p53 phosphorylation level at serine 15, while lysine 120 and 164 mutations decreased p53 acetylation level at lysine 382.	tyrosyl-lysine	88-94	tumor protein p53	Homo sapiens	116-119	
31680191-6	2020	Specifically, lysine 370/372/373 and 381/382/386 mutations decreased p53 stability, and lysine 305 mutation reduced p53 phosphorylation level at serine 15, while lysine 120 and 164 mutations decreased p53 acetylation level at lysine 382.	tyrosyl-lysine	88-94	tumor protein p53	Homo sapiens	116-119	
31680191-6	2020	Specifically, lysine 370/372/373 and 381/382/386 mutations decreased p53 stability, and lysine 305 mutation reduced p53 phosphorylation level at serine 15, while lysine 120 and 164 mutations decreased p53 acetylation level at lysine 382.	tyrosyl-lysine	88-94	tumor protein p53	Homo sapiens	116-119	
31680191-6	2020	Specifically, lysine 370/372/373 and 381/382/386 mutations decreased p53 stability, and lysine 305 mutation reduced p53 phosphorylation level at serine 15, while lysine 120 and 164 mutations decreased p53 acetylation level at lysine 382.	tyrosyl-lysine	88-94	tumor protein p53	Homo sapiens	116-119	
31680191-6	2020	Specifically, lysine 370/372/373 and 381/382/386 mutations decreased p53 stability, and lysine 305 mutation reduced p53 phosphorylation level at serine 15, while lysine 120 and 164 mutations decreased p53 acetylation level at lysine 382.	tyrosyl-lysine	88-94	tumor protein p53	Homo sapiens	116-119	
31680191-6	2020	Specifically, lysine 370/372/373 and 381/382/386 mutations decreased p53 stability, and lysine 305 mutation reduced p53 phosphorylation level at serine 15, while lysine 120 and 164 mutations decreased p53 acetylation level at lysine 382.	tyrosyl-lysine	88-94	tumor protein p53	Homo sapiens	116-119	
31682411-7	2019	Using thioacylated lysine residues in p53-derived peptides we optimized substrates for HDAC8 with catalytic efficiency over 250,000 M-1s-1, which are more than 100-fold more effective than most of the known substrates.	tyrosyl-lysine	6-25	tumor protein p53	Homo sapiens	38-41	
31594538-4	2019	RESULTS: Here, we present data suggesting that LSH regulates p53 in cis through two pathways: prevention proteasomal degradation through its deubiquitination, which is achieved by reducing the lysine 11-linked, lysine 48-linked polyubiquitin chains (K11 and K48) on p53; and revival of the transcriptional activity of p53 by forming a complex with PKM2 (pyruvate kinase 2).	tyrosyl-lysine	193-199	tumor protein p53	Homo sapiens	61-64	
31594538-4	2019	RESULTS: Here, we present data suggesting that LSH regulates p53 in cis through two pathways: prevention proteasomal degradation through its deubiquitination, which is achieved by reducing the lysine 11-linked, lysine 48-linked polyubiquitin chains (K11 and K48) on p53; and revival of the transcriptional activity of p53 by forming a complex with PKM2 (pyruvate kinase 2).	tyrosyl-lysine	211-217	tumor protein p53	Homo sapiens	61-64	
31863007-0	2019	PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth.	tyrosyl-lysine	20-26	tumor protein p53	Homo sapiens	16-19	
31863007-4	2019	Here, we identify PBRM1 as a reader for p53 acetylation on lysine 382 (K382Ac) through its bromodomain 4 (BD4).	tyrosyl-lysine	59-65	tumor protein p53	Homo sapiens	40-43