Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xenopus laevis | Q6NUA1 | isoform PRMT5 | - |
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 | - |
oocyte | - |
Xenopus laevis | - |
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 | - |
Xenopus laevis | S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine | - |
? | |
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine | - |
Xenopus laevis | S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine | - |
? | |
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 | 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 |