The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: [histone H3]-dimethyl-L-lysine36 N-methyltransferase
Reaction: S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
Other name(s): KMT3A (gene name); SETD2 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-N6,N6-dimethyl-L-lysine36 N6-methyltransferase
Comments: The enzyme, found in metazoa, methylates a dimethylated L-lysine36 residue of histone H3 (H3K36), which has been methylated previously by EC, [histone H3]-lysine36 N-dimethyltransferase. The homologous enzyme from yeast catalyses all three methylations (see EC, [histone H3]-lysine36 N-trimethyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Kizer, K.O., Phatnani, H.P., Shibata, Y., Hall, H., Greenleaf, A.L. and Strahl, B.D. A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation. Mol. Cell Biol. 25 (2005) 3305–3316. [PMID: 15798214]
2.  Yuan, W., Xie, J., Long, C., Erdjument-Bromage, H., Ding, X., Zheng, Y., Tempst, P., Chen, S., Zhu, B. and Reinberg, D. Heterogeneous nuclear ribonucleoprotein L Is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo. J. Biol. Chem. 284 (2009) 15701–15707. [PMID: 19332550]
3.  Wagner, E.J. and Carpenter, P.B. Understanding the language of Lys36 methylation at histone H3. Nat. Rev. Mol. Cell. Biol. 13 (2012) 115–126. [PMID: 22266761]
[EC created 1976 as EC, modified 1982, modified 1983, part transferred 2019 to EC]

Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald