Activating Compound | Comment | Organism | Structure |
---|---|---|---|
PRMT7 | PRMT7-mediated monomethylation of histone H4 Arg17 regulates PRMT5 activity at Arg3 in the same protein. Monomethylation at Arg-17 in histone H4 raises the general activity of PRMT5 with this substrate, but also ameliorates the low activity of PRMT5 at low substrate concentrations | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine | Homo sapiens | 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 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O14744 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine | - |
Homo sapiens | 2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine | - |
? | |
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 | Homo sapiens | 2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PRMT5 | - |
Homo sapiens |