EC 2.1.1.361 - [histone H4]-lysine20 N-methyltransferase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 2.1.1.361

Names

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

Reaction

Comments:

The enzyme catalyses the monomethylation of the L-lysine20 residue of histone H4 (H4K20). This event is usually followed by further methylation by EC 2.1.1.362, [histone H4]-N-methyl-L-lysine20 N-methyltransferase. This enzyme plays a pivotal role in DNA replication. Activity is high during the G2 and M phases, but declines significantly during G1 and S phases. Mutations in the enzyme have severe consequences, including DNA double-strand breaks, activation of DNA damage checkpoints, defective cell cycle progression, and reduced cell proliferation. 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. Fang, J., Feng, Q., Ketel, C. S., Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H., Tempst, P., Simon, J. A., Zhang, Y.
    Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase.
    Curr. Biol. 12: 1086-1099 (2002). [PMID: 12121615]
  2. Nishioka, K., Rice, J. C., Sarma, K., Erdjument-Bromage, H., Werner, J., Wang, Y., Chuikov, S., Valenzuela, P., Tempst, P., Steward, R., Lis, J. T., Allis, C. D., Reinberg, D.
    PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin.
    Mol. Cell 9: 1201-1213 (2002). [PMID: 12086618]
  3. Jorgensen, S., Elvers, I., Trelle, M. B., Menzel, T., Eskildsen, M., Jensen, O. N., Helleday, T., Helin, K., Sorensen, C. S.
    The histone methyltransferase SET8 is required for S-phase progression.
    J. Cell Biol. 179: 1337-1345 (2007). [PMID: 18166648]
  4. Oda, H., Okamoto, I., Murphy, N., Chu, J., Price, S. M., Shen, M. M., Torres-Padilla, M. E., Heard, E., Reinberg, D.
    Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development.
    Mol. Cell. Biol. 29: 2278-2295 (2009). [PMID: 19223465]
  5. 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]

[EC 2.1.1.361 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.361]