PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21273441-4	2011	Set9 methylated the nuclear and cytoplasmic AR utilizing the cofactor S-adenosyl-methionine.	S-Adenosylmethionine	72-91	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	0-4	
21273441-13	2011	Because the cellular metabolic state determines the level of S-adenosylmethionine and consequently the activity of Set9, the enhanced activity of methylated AR may have special significance in certain metabolic contexts.	S-Adenosylmethionine	61-81	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	115-119	
12514135-2	2003	Here, we report two crystal structures of SET7/9, a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet) determined at 1.7 and 2.3 A resolution.	S-Adenosylmethionine	155-178	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	42-48	
12514135-2	2003	Here, we report two crystal structures of SET7/9, a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet) determined at 1.7 and 2.3 A resolution.	S-Adenosylmethionine	180-186	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	42-48	
23519668-0	2013	Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives.	S-Adenosylmethionine	65-83	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	40-46	
23519668-2	2013	In previous work, novel inhibitors of SET7/9 that are amine analogues of the coenzyme S-(5"-adenosyl)-L-methionine (AdoMet) have been developed.	S-Adenosylmethionine	116-122	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	38-44	
21625555-6	2011	In addition, the results of molecular docking and MD simulations indicate that the new water channel continues to remain open when S-adenosyl-L-methionine (AdoMet) or S-adenosyl-L-homocysteine (AdoHcy) is bound to SET9.	S-Adenosylmethionine	131-154	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	214-218	
21625555-6	2011	In addition, the results of molecular docking and MD simulations indicate that the new water channel continues to remain open when S-adenosyl-L-methionine (AdoMet) or S-adenosyl-L-homocysteine (AdoHcy) is bound to SET9.	S-Adenosylmethionine	156-162	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	214-218	
18044969-2	2007	Proton dissociation (SET7/9.Lys4-NH3+.AdoMet --> SET7/9.Lys4-NH2.AdoMet + H+) must be prior to the methylation by S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	117-137	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	21-27	
18044969-2	2007	Proton dissociation (SET7/9.Lys4-NH3+.AdoMet --> SET7/9.Lys4-NH2.AdoMet + H+) must be prior to the methylation by S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	117-137	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	52-58	
18044969-2	2007	Proton dissociation (SET7/9.Lys4-NH3+.AdoMet --> SET7/9.Lys4-NH2.AdoMet + H+) must be prior to the methylation by S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	38-44	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	21-27	
18044969-2	2007	Proton dissociation (SET7/9.Lys4-NH3+.AdoMet --> SET7/9.Lys4-NH2.AdoMet + H+) must be prior to the methylation by S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	38-44	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	52-58