Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy

S-adenosyl-L-methionine:[histone H3]-L-lysine9 N6-trimethyltransferase

3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 (overall reaction);
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9;
(1b) S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9;
(1c) S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9

(other) R03875 R04866 R04867
Reaction

S-adenosyl-L-methionine [CPD:C00019];
[histone H3]-L-lysine9;
[histone H3]-N6-methyl-L-lysine9;
[histone H3]-N6,N6-dimethyl-L-lysine9

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. cf. EC 2.1.1.367, [histone H3]-lysine9 N-methyltransferase, EC 2.1.1.368, [histone H3]-lysine9 N-dimethyltransferase, and EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase.

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, modified 2020

1  [PMID:11094092]

O'Carroll D, Scherthan H, Peters AH, Opravil S, Haynes AR, Laible G, Rea S, Schmid M, Lebersorger A, Jerratsch M, Sattler L, Mattei MG, Denny P, Brown SD, Schweizer D, Jenuwein T

Isolation and characterization of Suv39h2, a second histone H3 methyltransferase  gene that displays testis-specific expression.

Mol Cell Biol 20:9423-33 (2000)
DOI:10.1128/mcb.20.24.9423-9433.2000

[mmu:20937 64707]

2  [PMID:11867540]

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 21:1121-31 (2002)
DOI:10.1093/emboj/21.5.1121

[dme:Dmel_CG43664]

3  [PMID:12130538]

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 16:1779-91 (2002)
DOI:10.1101/gad.989402

[mmu:110147]

4  [PMID:11959841]

Schultz DC, Ayyanathan K, Negorev D, Maul GG, Rauscher FJ 3rd

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 16:919-32 (2002)
DOI:10.1101/gad.973302

[hsa:9869]

5  [PMID:14633678]

Kim KC, Geng L, Huang S

Inactivation of a histone methyltransferase by mutations in human cancers.

Cancer Res 63:7619-23 (2003)

[hsa:7799]

6  [PMID:20084102]

Wu H, Min J, Lunin VV, Antoshenko T, Dombrovski L, Zeng H, Allali-Hassani A, Campagna-Slater V, Vedadi M, Arrowsmith CH, Plotnikov AN, Schapira M

Structural biology of human H3K9 methyltransferases.

PLoS One 5:e8570 (2010)
DOI:10.1371/journal.pone.0008570

[hsa:79813 10919 79723 7799]