The Enzyme Database

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EC 2.1.1.361     
Accepted name: [histone H4]-lysine20 N-methyltransferase
Reaction: S-adenosyl-L-methionine + a [histone H4]-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
Other name(s): KMT5A (gene name); SET8 (gene name); PR-SET7 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H4]-L-lysine20 N6-methyltransferase
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fang, J., Feng, Q., Ketel, C.S., Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H., Tempst, P., Simon, J.A. and Zhang, Y. Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase. Curr. Biol. 12 (2002) 1086–1099. [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. and 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 (2002) 1201–1213. [PMID: 12086618]
3.  Jorgensen, S., Elvers, I., Trelle, M.B., Menzel, T., Eskildsen, M., Jensen, O.N., Helleday, T., Helin, K. and Sorensen, C.S. The histone methyltransferase SET8 is required for S-phase progression. J. Cell Biol. 179 (2007) 1337–1345. [PMID: 18166648]
4.  Oda, H., Okamoto, I., Murphy, N., Chu, J., Price, S.M., Shen, M.M., Torres-Padilla, M.E., Heard, E. and 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 (2009) 2278–2295. [PMID: 19223465]
5.  Jorgensen, S., Schotta, G. and Sorensen, C.S. Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity. Nucleic Acids Res. 41 (2013) 2797–2806. [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]
 
 


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