EC 2.1.1.358 - [histone H3]-dimethyl-L-lysine36 N-methyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.1.358

Names

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

Reaction

Comments:

The enzyme, found in metazoa, methylates a dimethylated L-lysine36 residue of histone H3 (H3K36), which has been methylated previously by EC 2.1.1.357, [histone H3]-lysine36 N-dimethyltransferase. The homologous enzyme from yeast catalyses 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. Kizer, K. O., Phatnani, H. P., Shibata, Y., Hall, H., Greenleaf, A. L., 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: 3305-3316 (2005). [PMID: 15798214]
  2. Yuan, W., Xie, J., Long, C., Erdjument-Bromage, H., Ding, X., Zheng, Y., Tempst, P., Chen, S., Zhu, B., 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: 15701-15707 (2009). [PMID: 19332550]
  3. 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 2.1.1.358 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.354]