Reaction: 2 S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4 (overall reaction)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine4
Other name(s): NSD3 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine4 N6-dimethyltransferase
Comments: This entry describes enzymes that successively methylate the L-lysine4 residue of histone H3 (H3K4) twice, ultimately generating a dimethylated form. These modifications influence the binding of chromatin-associated proteins.The human NSD3 protein also catalyses the activity of EC 2.1.1.371, [histone H3]-lysine27 N-dimethyltransferase. cf. EC 2.1.1.364, [histone H3]-lysine4 N-methyltransferase, and EC 2.1.1.354, [histone H3]-lysine4 N-trimethyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc PDB, CAS registry number:
References:
1. Kim, S.M., Kee, H.J., Eom, G.H., Choe, N.W., Kim, J.Y., Kim, Y.S., Kim, S.K., Kook, H., Kook, H. and Seo, S.B. Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity. Biochem. Biophys. Res. Commun. 345 (2006) 318-323. [PMID: 16682010]