EC Number |
Natural Substrates |
---|
2.1.1.320 | 2 S-adenosyl-L-methionine + [germ cell-specific protein Vasa]-L-arginine |
seven arginine residues in Vasa, including R101, R105, R177, R179, R183, R197 and R201, and two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Vasa mutant with seven arginines to lysines (Vasa-7M: R101K, R105K, R177K, R179K, R183K, R197K and R201K) can not be dimethylated by Prmt5 |
2.1.1.320 | 2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine |
two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Zili mutant with two arginines to lysines [Zili (1-133aa)-R68/221K] can not be dimethylated by Prmt5 |
2.1.1.320 | 2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine |
- |
2.1.1.320 | 2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine |
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code |
2.1.1.320 | 2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine |
- |
2.1.1.320 | 2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine |
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code |
2.1.1.320 | 2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine |
- |
2.1.1.320 | 2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine |
the enzyme (PRMT5) affects the levels of symmetric dimethylarginine at Arg3 on histone H4, leading to the repression of genes which are related to disease progression in lymphoma and leukemia. PRMT7-mediated monomethylation of histone H4 Arg17 regulates PRMT5 activity at Arg3 in the same protein |
2.1.1.320 | 2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine |
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code |
2.1.1.320 | 2 S-adenosyl-L-methionine + [KRAB-associated protein 1]-L-arginine |
methylation of KRAB-associated protein 1 (KAP1) arginine residues regulates the KAP1-ZNF224 interaction, thus suggesting that this KAP1 post-translational modification can actively contribute to the regulation of ZNF224-mediated repression |