EC 2.1.1.355 - [histone H3]-lysine9 N-trimethyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.1.355

Names

Accepted name:
[histone H3]-lysine9 N-trimethyltransferase
Systematic name:
S-adenosyl-L-methionine:[histone H3]-L-lysine9 N6-methyltransferase

Reaction

Comments:

This entry describes several enzymes that successively methylate the L-lysine9 residue of histone H3 (H3K9), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. In general, the methylation of H3K9 leads to transcriptional repression of the affected target genes. 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. O'Carroll, D., Scherthan, H., Peters, A. H., Opravil, S., Haynes, A. R., Laible, G., Rea, S., Schmid, M., Lebersorger, A., Jerratsch, M., Sattler, L., Mattei, M. G., Denny, P., Brown, S. D., Schweizer, D., Jenuwein, T.
    Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression.
    Mol. Cell. Biol. 20: 9423-9433 (2000). [PMID: 11094092]
  2. Schotta, G., Ebert, A., Krauss, V., Fischer, A., Hoffmann, J., Rea, S., Jenuwein, T., Dorn, R., Reuter, G.
    Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing.
    EMBO J. 21: 1121-1131 (2002). [PMID: 11867540]
  3. Tachibana, M., Sugimoto, K., Nozaki, M., Ueda, J., Ohta, T., Ohki, M., Fukuda, M., Takeda, N., Niida, H., Kato, H., Shinkai, Y.
    G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis.
    Genes Dev. 16: 1779-1791 (2002). [PMID: 12130538]
  4. Schultz, D. C., Ayyanathan, K., Negorev, D., Maul, G. G., Rauscher, F. J.
    SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins.
    Genes Dev. 16: 919-932 (2002). [PMID: 11959841]
  5. Kim, K. C., Geng, L., Huang, S.
    Inactivation of a histone methyltransferase by mutations in human cancers.
    Cancer Res. 63: 7619-7623 (2003). [PMID: 14633678]
  6. Wu, H., Min, J., Lunin, V. V., Antoshenko, T., Dombrovski, L., Zeng, H., Allali-Hassani, A., Campagna-Slater, V., Vedadi, M., Arrowsmith, C. H., Plotnikov, A. N., Schapira, M.
    Structural biology of human H3K9 methyltransferases.
    PLoS ONE 5: e8570 (2010). [PMID: 20084102]

[EC 2.1.1.355 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.355]