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Literature summary for 2.1.1.320 extracted from

  • Lacroix, M.; Messaoudi, S.E.; Rodier, G.; Le Cam, A.; Sardet, C.; Fabbrizio, E.
    The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5 (2008), EMBO Rep., 9, 452-458.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens O14744 isoform PRMT5
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + [histone H3]-L-arginine
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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
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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

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