IUBMB Enzyme Nomenclature


Accepted name: [histone H3]-lysine4 N-methyltransferase

Reaction: S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4

Other name(s): KMT7 (gene name); SETD7 (gene name); SET7/9 (gene name); KIAA1717 (gene name)KMT7 (gene name); SETD7 (gene name); SET7/9 (gene name); KIAA1717 (gene name); KMT2A (gene name); KMT2B (gene name); KMT2C (gene name); KMT2D (gene name); KMT2F (gene name); KMT2G (gene name); MLL1 (gene name); MLL2 (gene name); MLL3 (gene name); MLL4 (gene name); SETD1A (gene name) Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine4 N6-methyltransferase

Comments: This entry describes enzymes that catalyse a single methylation of the L-lysine4 residue of histone H3 (H3K4), generating a monomethylated form. This modifications influence the binding of chromatin-associated proteins and result in gene activation or suppression. Some enzymes that catalyse this reaction continue to generate a dimethyated form, these enzymes are classified under EC, [histone H3]-lysine4 N-dimethyltransferase. Other enzymes continue to catalyse a third methylation, those are classified under EC, [histone H3]-lysine4 N-trimethyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:


1. Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H., Borchers, C., Tempst, P. and Zhang, Y. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell 8 (2001) 1207-1217. [PMID: 11779497]

2. Nishioka, K., Chuikov, S., Sarma, K., Erdjument-Bromage, H., Allis, C.D., Tempst, P. and Reinberg, D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16 (2002) 479-489. [PMID: 11850410]

3. Wilson, J.R., Jing, C., Walker, P.A., Martin, S.R., Howell, S.A., Blackburn, G.M., Gamblin, S.J. and Xiao, B. Crystal structure and functional analysis of the histone methyltransferase SET7/9. Cell 111 (2002) 105-115. [PMID: 12372304]

4. Xiao, B., Jing, C., Wilson, J.R., Walker, P.A., Vasisht, N., Kelly, G., Howell, S., Taylor, I.A., Blackburn, G.M. and Gamblin, S.J. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature 421 (2003) 652-656. [PMID: 12540855]

5. Hu, P. and Zhang, Y. Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial structures. J. Am. Chem. Soc. 128 (2006) 1272-1278. [PMID: 16433545]

[EC created 1976 as EC, modified 1982, modified 1983, part transferred 2020 to EC]

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