EC 2.1.1.357 - [histone H3]-lysine36 N-dimethyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.1.357

Names

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

Reaction

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. The product can be further methylated to the trimethyl form by EC 2.1.1.358, [histone H3]-dimethyl-L-lysine36 N-methyltransferase. The yeast SET2 enzyme can catalyse all three methylations (see EC 2.1.1.359, [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

References

  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 2.1.1.357 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.357]