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(+/-)-2',3'-dibenzyl-S-adenosyl-L-methionine + [histone H3]-L-lysine27
?
-
-
-
?
(+/-)-2'-benzyl-S-adenosyl-L-methionine + [histone H3]-L-lysine27
?
-
-
-
?
(+/-)-3'-benzyl-S-adenosyl-L-methionine + [histone H3]-L-lysine27
?
-
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-methionine + histone H3(K27)
?
S-adenosyl-L-methionine + histone H3(K27)
S-adenosyl-L-homocysteine + N-methylated histone H3(K27)
-
-
-
?
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine27
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27
additional information
?
-
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
Thermochaetoides thermophila
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
Thermochaetoides thermophila DSM1495
-
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
highest activity
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + histone H3(K27)
?
-
di- and trimethylation at histone H3(K27)
-
-
?
S-adenosyl-L-methionine + histone H3(K27)
?
-
Drosophila Polycomb Repressive Complex 2 is a lysine methyltransferase that trimethylates histone H3 (K27)
-
-
?
S-adenosyl-L-methionine + histone H3(K27)
?
-
RE-IIBP selectively transfers methyl groups to K27 of histone H3
-
-
?
S-adenosyl-L-methionine + histone H3(K27)
?
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
Thermochaetoides thermophila
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
Thermochaetoides thermophila DSM1495
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine27
Thermochaetoides thermophila
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine27
Thermochaetoides thermophila DSM1495
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27
Thermochaetoides thermophila
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27
Thermochaetoides thermophila DSM1495
-
-
-
-
?
additional information
?
-
the enzyme displays a preference for substrates with less methylation (unmethylated H3K27:monomethylated H3K27:dimethylated H3K27 kcat/Km ratio is 9:6:1)
-
-
?
additional information
?
-
-
the enzyme displays a preference for substrates with less methylation (unmethylated H3K27:monomethylated H3K27:dimethylated H3K27 kcat/Km ratio is 9:6:1)
-
-
?
additional information
?
-
the enzyme is able to add methyl groups to lysine 27 as well as 9 in histone H3
-
-
?
additional information
?
-
the enzyme shows a strong preference for histone H3 in oligonucleosome forms
-
-
?
additional information
?
-
enzyme shows versatility in substrate recognition. In a pan-methylation assay of histone H3, H3K4me3 and H3K27me3 species are preferably detected rather than me1 and me2 species, and H3K79-me1 and -me2 species are favored against me3 species. NSD3 shows significant di-/tri-methylation of histone H4K20
-
-
-
additional information
?
-
enzyme shows versatility in substrate recognition. In a pan-methylation assay of histone H3, H3K4me3 and H3K27me3 species are preferably detected rather than me1 and me2 species, and H3K79-me1 and -me2 species are favored against me3 species. NSD3 shows significant di-/tri-methylation of histone H4K20
-
-
-
additional information
?
-
enzyme shows versatility in substrate recognition. In a pan-methylation assay of histone H3, H3K4me3 and H3K27me3 species are preferably detected rather than me1 and me2 species, while H3K9-me1 and -me2 and H3K79-me1 and -me2 species are favored against me3 species. NSD2 shows di-/tri-methylation of histone H4K20
-
-
-
additional information
?
-
enzyme shows versatility in substrate recognition. In a pan-methylation assay of histone H3, H3K4me3 and H3K27me3 species are preferably detected rather than me1 and me2 species, while H3K9-me1 and -me2 and H3K79-me1 and -me2 species are favored against me3 species. NSD2 shows di-/tri-methylation of histone H4K20
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine27
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
Thermochaetoides thermophila
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
Thermochaetoides thermophila DSM1495
-
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
highest activity
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
Thermochaetoides thermophila
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
Thermochaetoides thermophila DSM1495
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine27
Thermochaetoides thermophila
-
-
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-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine27
Thermochaetoides thermophila DSM1495
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27
Thermochaetoides thermophila
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27
Thermochaetoides thermophila DSM1495
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-
-
-
?
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F681Y
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the mutation dramatically reduces PRC2 HMTase
A677G
the mutant cell line reveals aberrantly elevated trimethylated [histone H3]-L-lysine27 and decreased monomethylated and dimethylated [histone H3]-L-lysine27 as compared to the wild type. The mutant enzyme demonstrates nearly equal efficiency for all three substrates (unmethylated H3K27:monomethylated H3K27:dimethylated H3K27 kcat/Km ratio is 1.1:0.6:1)
C483A
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no activity, the SET domain cysteine 483 is a critical residue for the histone methyltransferase activity of RE-IIBP
R477A
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no activity, the SET domain 477 is a critical residue for the histone methyltransferase activity of RE-IIBP
F52Y
-
can only mono- and di- but not tri-methylate H38(K27)
L116A
the mutant shows strongly increased activity compared to the wild type enzyme
Y109G
the mutant shows strongly decreased activity compared to the wild type enzyme
Y50F
-
nearly abolishes di- and tri-methylation of H3(K27), but does not affect the mono-methylation
D329A
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
DELTAL350
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
H326A
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
P325S
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R839D
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D329A
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
DELTAL350
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
H326A
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
P325S
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
R839D
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
F679Y
-
the mutant is tolerated with about 2fold reduction compared with wild type
F679Y
-
the mutant retains the capacity to produce trimethylated histone H3(K27)
additional information
-
each SET domain mutation disrupts PRC2 histone methyltransferase, based on known SET domain structures, the mutations likely affect either the lysine-substrate binding pocket, the binding site for the adenosylmethionine methyl donor, or a critical tyrosine predicted to interact with the substrate lysine epsilon-amino group. The CXC mutant retains catalytic activity, Lys-27 specificity, and trimethylation capacity.
additional information
-
the E(z)Trm mutation increases the histone H3 (K27) trimethylation efficiency of catalytic subunit E(Z) of Polycomb Repressive Complex 2
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brenda
Joshi, P.; Carrington, E.A.; Wang, L.; Ketel, C.S.; Miller, E.L.; Jones, R.S.; Simon, J.A.
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Drosophila melanogaster
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2008
Homo sapiens
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Stepanik, V.A.; Harte, P.J.
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2012
Drosophila melanogaster
brenda
Gu, X.; Xu, T.; He, Y.
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7
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2014
Arabidopsis thaliana (P93831)
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Kisliouk, T.; Yosefi, S.; Meiri, N.
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brenda
Tachibana, M.; Sugimoto, K.; Fukushima, T.; Shinkai, Y.
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276
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Homo sapiens (Q96KQ7)
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Li, J.; Wei, H.; Zhou, M.M.
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54
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Paramecium bursaria Chlorella virus 1 (O41094)
brenda
Friedman, J.; Cho, W.K.; Chu, C.K.; Keedy, K.S.; Archin, N.M.; Margolis, D.M.; Karn, J.
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85
9078-9089
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Human immunodeficiency virus 1
brenda
Boros, J.; Arnoult, N.; Stroobant, V.; Collet, J.F.; Decottignies, A.
Polycomb repressive complex 2 and H3K27me3 cooperate with H3K9 methylation to maintain heterochromatin protein 1alpha at chromatin
Mol. Cell. Biol.
34
3662-3674
2014
Mus musculus (Q61188), Mus musculus
brenda
Connolly, L.R.; Smith, K.M.; Freitag, M.
The Fusarium graminearum histone H3 K27 methyltransferase KMT6 regulates development and expression of secondary metabolite gene clusters
PLoS Genet.
9
e1003916
2013
Fusarium graminearum
brenda
McCabe, M.T.; Graves, A.P.; Ganji, G.; Diaz, E.; Halsey, W.S.; Jiang, Y.; Smitheman, K.N.; Ott, H.M.; Pappalardi, M.B.; Allen, K.E.; Chen, S.B.; Della Pietra, A.; Dul, E.; Hughes, A.M.; Gilbert, S.A.; Thrall, S.H.; Tummino, P.J.; Kruger, R.G.; Brandt, M.; Schwartz, B.; Creasy, C.L.
Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27)
Proc. Natl. Acad. Sci. USA
109
2989-2994
2012
Homo sapiens (Q15910), Homo sapiens
brenda
Zhao, X.; Wang, Y.; Wang, Y.; Liu, Y.; Gao, S.
Histone methyltransferase TXR1 is required for both H3 and H3.3 lysine 27 methylation in the well-known ciliated protist Tetrahymena thermophila
Sci. China Life Sci.
60
264-270
2017
Tetrahymena thermophila (Q23QI3), Tetrahymena thermophila SB210 (Q23QI3)
brenda
Cao, R.; Wang, L.; Wang, H.; Xia, L.; Erdjument-Bromage, H.; Tempst, P.; Jones, R.; Zhang, Y.
Role of histone H3 lysine 27 methylation in polycomb-group silencing
Science
298
1039-1043
2002
Homo sapiens (Q15910)
brenda
Jiao, L.; Liu, X.
Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2
Science
350
aac4383
2015
Thermochaetoides thermophila, Thermochaetoides thermophila DSM1495
brenda
Morishita, M.; Mevius, D.; Di Luccio, E.
In vitro histone lysine methylation by NSD1, NSD2/MMSET/WHSC1 and NSD3/WHSC1L
BMC Struct. Biol.
14
25
2014
Homo sapiens (O96028), Homo sapiens (Q9BZ95)
brenda
Shen, Y.; Morishita, M.; di Luccio, E.
High yield recombinant expression and purification of oncogenic NSD1, NSD2, and NSD3 with human influenza hemagglutinin tag
Protein Expr. Purif.
166
105506
2020
Homo sapiens (O96028)
brenda
Liu, T.; Zhang, P.; Li, T.; Chen, X.; Zhu, Z.; Lyu, Y.; Li, X.; Tian, X.; Zeng, W.
SETDB1 plays an essential role in maintenance of gonocyte survival in pigs
Reproduction
154
23-34
2017
Sus scrofa (F1SS95)
brenda