EC - [histone H3]-lysine36 N-dimethyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
[histone H3]-lysine36 N-dimethyltransferase
Systematic name:
S-adenosyl-L-methionine:[histone H3]-L-lysine36 N6-dimethyltransferase



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. The product can be further methylated to the trimethyl form by EC, [histone H3]-dimethyl-L-lysine36 N-methyltransferase. The yeast SET2 enzyme can catalyse all three methylations (see EC, [histone H3]-lysine36 N-trimethyltransferase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (24) [show] [UniProt]


  1. Fnu, S., Williamson, E. A., De Haro, L. P., Brenneman, M., Wray, J., Shaheen, M., Radhakrishnan, K., Lee, S. H., Nickoloff, J. A., Hromas, R.
    Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining.
    Proc. Natl. Acad. Sci. U.S.A. 108 : 540-545 (2011). [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., Gozani, O.
    NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming.
    Mol. Cell 44 : 609-620 (2011). [PMID: 22099308]
  3. Qiao, Q., Li, Y., Chen, Z., Wang, M., Reinberg, D., Xu, R. M.
    The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation.
    J. Biol. Chem. 286 : 8361-8368 (2011). [PMID: 21196496]
  4. Wagner, E. J., Carpenter, P. B.
    Understanding the language of Lys36 methylation at histone H3.
    Nat. Rev. Mol. Cell Biol. 13 : 115-126 (2012). [PMID: 22266761]

[EC created 1976 as EC, modified 1982, modified 1983, part transferred 2019 to EC]