PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31685992-3	2019	Here, we demonstrate that, in contrast with the well-established tumour-suppressive role of canonical PTEN, PTENalpha and PTENbeta promote tumourigenesis by directly interacting with the histone H3 lysine 4 (H3K4) presenter WDR5 to promote H3K4 trimethylation and maintain a tumour-promoting signature.	tyrosyl-lysine	198-206	WD repeat domain 5	Homo sapiens	224-228	
31544250-3	2020	In this study, we found that the WD repeat domain 5 protein (WDR5)-a core subunit of histone H3 lysine 4 methyltransferase complexes, which catalyze the generation of histone H3 lysine 4 trimethylation (H3K4me3) modification-is highly expressed in HBV-related HCC and promotes HCC development.	tyrosyl-lysine	96-102	WD repeat domain 5	Homo sapiens	33-51	
31544250-3	2020	In this study, we found that the WD repeat domain 5 protein (WDR5)-a core subunit of histone H3 lysine 4 methyltransferase complexes, which catalyze the generation of histone H3 lysine 4 trimethylation (H3K4me3) modification-is highly expressed in HBV-related HCC and promotes HCC development.	tyrosyl-lysine	96-102	WD repeat domain 5	Homo sapiens	61-65	
31544250-3	2020	In this study, we found that the WD repeat domain 5 protein (WDR5)-a core subunit of histone H3 lysine 4 methyltransferase complexes, which catalyze the generation of histone H3 lysine 4 trimethylation (H3K4me3) modification-is highly expressed in HBV-related HCC and promotes HCC development.	tyrosyl-lysine	178-184	WD repeat domain 5	Homo sapiens	33-51	
31544250-3	2020	In this study, we found that the WD repeat domain 5 protein (WDR5)-a core subunit of histone H3 lysine 4 methyltransferase complexes, which catalyze the generation of histone H3 lysine 4 trimethylation (H3K4me3) modification-is highly expressed in HBV-related HCC and promotes HCC development.	tyrosyl-lysine	178-184	WD repeat domain 5	Homo sapiens	61-65