EC 2.1.1.362 - [histone H4]-N-methyl-L-lysine20 N-methyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.1.362

Names

Accepted name:
[histone H4]-N-methyl-L-lysine20 N-methyltransferase
Systematic name:
S-adenosyl-L-methionine:[histone H4]-N6-methyl-L-lysine20 N6-methyltransferase

Reaction

Comments:

This entry describes a group of enzymes that catalyse a single methylation of monomethylated lysine20 of histone H4 (H4K20m1, generated by EC 2.1.1.361, [histone H4]-lysine20 N-methyltransferase), forming the dimethylated form. This modification is broadly distributed across the genome and is likely important for general chromatin-mediated processes. The double-methylated form of lysine20 in histone H4 is the most abundant methylation state of this residue and is found on ~80% of all histone H4 molecules. Full activity of the enzyme requires that the lysine at position 9 of histone H3 is trimethylated. Formerly EC 2.1.1.43.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Schotta, G., Lachner, M., Sarma, K., Ebert, A., Sengupta, R., Reuter, G., Reinberg, D., Jenuwein, T.
    A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin.
    Genes Dev. 18: 1251-1262 (2004). [PMID: 15145825]
  2. Jorgensen, S., Schotta, G., Sorensen, C. S.
    Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity.
    Nucleic Acids Res. 41: 2797-2806 (2013). [PMID: 23345616]
  3. Wu, H., Siarheyeva, A., Zeng, H., Lam, R., Dong, A., Wu, X. H., Li, Y., Schapira, M., Vedadi, M., Min, J.
    Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2.
    FEBS Lett. 587: 3859-3868 (2013). [PMID: 24396869]
  4. Southall, S. M., Cronin, N. B., Wilson, J. R.
    A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases.
    Nucleic Acids Res. 42: 661-671 (2014). [PMID: 24049080]
  5. Weirich, S., Kudithipudi, S., Jeltsch, A.
    Specificity of the SUV4-20H1 and SUV4-20H2 protein lysine methyltransferases and methylation of novel substrates.
    J. Mol. Biol. 428: 2344-2358 (2016). [PMID: 27105552]

[EC 2.1.1.362 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.362]