Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O14744 | isoform PRMT5 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 S-adenosyl-L-methionine + [histone H3]-L-arginine | - |
Homo sapiens | 2 S-adenosyl-L-homocysteine + [histone H3]-Nomega,Nomega'-dimethyl-L-arginine | isoform PRMT5 bound to nuclear protein COPR5 methylates histone histone H3 at residue R8. Methylation of histone H4 is preferred over histone H3 | ? | |
2 S-adenosyl-L-methionine + [histone H4]-L-arginine | - |
Homo sapiens | 2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine | isoform PRMT5 bound to nuclear protein COPR5 methylates histone H4 at residue R3 preferentially when compared with histone H3 | ? |
General Information | Comment | Organism |
---|---|---|
physiological function | isoform PRMT5 binds to a nuclear protein, called cooperator of PRMT5, i.e. COPR5. COPR5 modulates the substrate specificity of nuclear PRMT5-containing complexes, at least towards histones. Rcombinant COPR5 binds to the amino terminus of histone H4 and is required to recruit PRMT5 to reconstituted nucleosomes in vitro. COPR5 depletion in cells strongly reduces PRMT5 recruitment on chromatin at the PRMT5 target gene cyclin E1 in vivo | Homo sapiens |