The Enzyme Database

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Accepted name: [histone H3]-lysine36 N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36 (overall reaction)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine36
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine36 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine36
Other name(s): KMT3B (gene name); KMT3C (gene name); NSD2 (gene name); SETMAR (gene name); WHSC1 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine36 N6-dimethyltransferase
Comments: This entry describes a group of metazoan enzymes that catalyse two successive methylations of lysine36 of histone H3 (H3K36), forming mono- and dimethylated forms. These modifications influence the binding of chromatin-associated proteins. Some enzymes can catalyse three methylations, forming a trimethylated form; these enzymes are classified under EC, [histone H3]-lysine36 N-trimethyltransferase.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
1.  Fnu, S., Williamson, E.A., De Haro, L.P., Brenneman, M., Wray, J., Shaheen, M., Radhakrishnan, K., Lee, S.H., Nickoloff, J.A. and Hromas, R. Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. Proc. Natl. Acad. Sci. USA 108 (2011) 540–545. [PMID: 21187428]
2.  Kuo, A.J., Cheung, P., Chen, K., Zee, B.M., Kioi, M., Lauring, J., Xi, Y., Park, B.H., Shi, X., Garcia, B.A., Li, W. and Gozani, O. NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming. Mol. Cell 44 (2011) 609–620. [PMID: 22099308]
3.  Qiao, Q., Li, Y., Chen, Z., Wang, M., Reinberg, D. and Xu, R.M. The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation. J. Biol. Chem. 286 (2011) 8361–8368. [PMID: 21196496]
4.  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]

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