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Literature summary for 2.1.1.320 extracted from

  • Wilczek, C.; Chitta, R.; Woo, E.; Shabanowitz, J.; Chait, B.T.; Hunt, D.F.; Shechter, D.
    Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs (2011), J. Biol. Chem., 286, 42221-42231.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.320

Organism

Organism UniProt Comment Textmining
Xenopus laevis Q6NUA1 isoform PRMT5
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Source Tissue

Source Tissue Comment Organism Textmining
egg histone H2A and nucleoplasmin methylation appears late in oogenesis and is most abundant in the laid egg Xenopus laevis
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oocyte
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 Xenopus laevis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information a complex of the protein arginine methyltransferase Prmt5 and the methylosome protein Mep50 isolated from Xenopus eggs specifically methylates predeposition histones H2A/H2A.X-F and H4 and the histone chaperone nucleoplasmin on a conserved motif GRGXK Xenopus laevis ?
-
 ?
S-adenosyl-L-methionine + [histone H2A]-L-arginine
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 Xenopus laevis S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
-
 ?
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
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 Xenopus laevis S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
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 ?
S-adenosyl-L-methionine + [histone H4]-L-arginine
-
 Xenopus laevis S-adenosyl-L-homocysteine + [histone H4]-Nomega-methyl-L-arginine
-
 ?
S-adenosyl-L-methionine + [histone H4]-Nomega-methyl-L-arginine
-
 Xenopus laevis S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
-
 ?
S-adenosyl-L-methionine + [nucleoplasmin]-L-arginine
-
 Xenopus laevis S-adenosyl-L-homocysteine + [nucleoplasmin]-Nomega-methyl-L-arginine nucleoplasmin is a potent substrate and is monomethylated and symmetrically dimethylated at Arg187 ?
S-adenosyl-L-methionine + [nucleoplasmin]-Nomega-methyl-L-arginine
-
 Xenopus laevis S-adenosyl-L-homocysteine + [nucleoplasmin]-Nomega,Nomega'-dimethyl-L-arginine nucleoplasmin is a potent substrate and is monomethylated and symmetrically dimethylated at Arg187 ?

General Information

General Information Comment Organism
physiological function isoform Prmt5 forms a complex with methylosome protein Mep50 that specifically methylates predeposition histones H2A/H2A.X-F and H4 and the histone chaperone nucleoplasmin on a conserved motif (GRGXK). Nucleoplasmin is a potent substrate for Prmt5-Mep50 and modulates Prmt5-Mep50 activity directed toward histones. Histone H2A and nucleoplasmin methylation appears late in oogenesis and is most abundant in the laid egg Xenopus laevis