2.1.1.320: type II protein arginine methyltransferase
This is an abbreviated version!
For detailed information about type II protein arginine methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.320
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2.1.1.320
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histone
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methyltransferases
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chromatin
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prmts
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dimethylarginine
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tumorigenesis
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h4r3me2s
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monomethylation
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spliceosomal
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mep50
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methylosome
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ribonucleoproteins
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non-histone
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pre-mrna
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snrnps
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picln
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monomethylarginine
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methylthioadenosine
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tudor
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menin
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protein-arginine
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medicine
- 2.1.1.320
- histone
- methyltransferases
- chromatin
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prmts
- dimethylarginine
- tumorigenesis
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h4r3me2s
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monomethylation
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spliceosomal
- mep50
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methylosome
- ribonucleoproteins
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non-histone
- pre-mrna
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snrnps
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picln
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monomethylarginine
- methylthioadenosine
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tudor
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menin
- protein-arginine
- medicine
Reaction
2 S-adenosyl-L-methionine + = 2 S-adenosyl-L-homocysteine +
Synonyms
At4g31120, EC 2.1.1.124, EC 2.1.1.125, EC 2.1.1.126, EC 2.1.1.23, Hsl7, Jak-binding protein 1, Janus kinase-binding protein 1, JBP1, PRMT-5, PRMT-9, PRMT15, PRMT5, PRMT7, PRMT9, protein arginine methyltransferase 5, Skb1
ECTree
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Substrates Products
Substrates Products on EC 2.1.1.320 - type II protein arginine methyltransferase
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REACTION DIAGRAM
2 S-adenosyl-L-methionine + [D2 dopamine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [D2 dopamine receptor]-Nomega,Nomega'-dimethyl-L-arginine
recombinant fragment of the third intracellular loop of D2, corresponding to amino acid residues 211 to 241 fused to glutathione S-transferase. Residues Arg217 and Arg219 are key methylation sites within this region
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2 S-adenosyl-L-methionine + [DOP-3 receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [DOP-3 receptor]-Nomega,Nomega'-dimethyl-L-arginine
recombinant fragment of the third intracellular loop of Caenorhabditis elegans DOP-3, amino acid residues 202 to 232 fused to GST. Residues Arg208 and Arg210 are key methylation sites within this region
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2 S-adenosyl-L-methionine + [germ cell-specific protein Vasa]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [golgin GM130]-L-arginine
2 S-adenosyl-L-homocysteine + [golgin GM130]-Nomega,Nomega'-dimethyl-L-arginine
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overall reaction
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?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [histone H3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3]-Nomega,Nomega'-dimethyl-L-arginine
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isoform PRMT5 bound to nuclear protein COPR5 methylates histone histone H3 at residue R8. Methylation of histone H4 is preferred over histone H3
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?
2 S-adenosyl-L-methionine + [histone H4 peptide]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4 peptide]-Nomega,Nomega'-dimethyl-L-arginine
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both PRMT5 alone and PRMT5 in complex with MEP50 are able to generate di-methylated H4 peptide product. The PRMT5:MEP50 complex consistently has a higher level of methyltransferase activity compared with PRMT5
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?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [histone H4]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [KRAB-associated protein 1]-L-arginine
2 S-adenosyl-L-homocysteine + [KRAB-associated protein 1]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [SER-2 tyramine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [SER-2 tyramine receptor]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [SmD3 protein]-L-arginine
2 S-adenosyl-L-homocysteine + [SmD3 protein]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [voltage-gated sodium channel NaV1.5]-L-arginine
2 S-adenosyl-L-homocysteine + [voltage-gated sodium channel NaV1.5]-Nomega,Nomega'-dimethyl-L-arginine
S-adenosyl-L-methionine + [GST-fibrillarin]-L-arginine
S-adenosyl-L-homocysteine + [GST-fibrillarin]-Nomega-methyl-L-arginine
substrate is amino terminus of fibrillarin fused to glutathione S-transferase
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?
S-adenosyl-L-methionine + [GST-fibrillarin]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-fibrillarin]-Nomega,Nomega'-dimethyl-L-arginine
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?
S-adenosyl-L-methionine + [GST-GAR]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR]-Nomega-methyl-L-arginine
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?
S-adenosyl-L-methionine + [GST-GAR]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR]-Nomega,Nomega'-dimethyl-L-arginine
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?
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
S-adenosyl-L-methionine + [histone H4]-L-arginine
S-adenosyl-L-homocysteine + [histone H4]-Nomega-methyl-L-arginine
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?
S-adenosyl-L-methionine + [histone H4]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
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?
S-adenosyl-L-methionine + [histone]-L-arginine
S-adenosyl-L-homocysteine + [histone]-Nomega-methyl-L-arginine
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?
S-adenosyl-L-methionine + [histone]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone]-Nomega,Nomega'-dimethyl-L-arginine
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?
S-adenosyl-L-methionine + [myelin basic protein]-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [myelin basic protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega,Nomega'-dimethyl-L-arginine
S-adenosyl-L-methionine + [nucleoplasmin]-L-arginine
S-adenosyl-L-homocysteine + [nucleoplasmin]-Nomega-methyl-L-arginine
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nucleoplasmin is a potent substrate and is monomethylated and symmetrically dimethylated at Arg187
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?
S-adenosyl-L-methionine + [nucleoplasmin]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [nucleoplasmin]-Nomega,Nomega'-dimethyl-L-arginine
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nucleoplasmin is a potent substrate and is monomethylated and symmetrically dimethylated at Arg187
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?
S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega-methyl-L-arginine
the enzyme methylates the R508 residue
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S-adenosyl-L-methionine + [splicing factor SF3B2]-Nomega-L-arginine
S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme methylates the R508 residue
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2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [germ cell-specific protein Vasa]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
seven arginine residues in Vasa, including R101, R105, R177, R179, R183, R197 and R201, and two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Vasa mutant with seven arginines to lysines (Vasa-7M: R101K, R105K, R177K, R179K, R183K, R197K and R201K) can not be dimethylated by Prmt5
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2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Zili mutant with two arginines to lysines [Zili (1-133aa)-R68/221K] can not be dimethylated by Prmt5
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2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code
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2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code
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2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-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
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2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code
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2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
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enzyme specifically methylates histone H4 Arg3 to form symmetric dimethylarginines. In addition, it is annotated for formation of omega-N monomethylarginine, reaction of EC 2.1.1.321
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2 S-adenosyl-L-methionine + [histone H4]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
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PRMT5 alone methylates both histone H4 and SmD3 proteins while PRMT5 complexed with p44 and pICln methylates SmD3 but not histone H4
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2 S-adenosyl-L-methionine + [histone H4]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
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isoform PRMT5 bound to nuclear protein COPR5 methylates histone H4 at residue R3 preferentially when compared with histone H3
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2 S-adenosyl-L-homocysteine + [KRAB-associated protein 1]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [KRAB-associated protein 1]-L-arginine
2 S-adenosyl-L-homocysteine + [KRAB-associated protein 1]-Nomega,Nomega'-dimethyl-L-arginine
methylation of KRAB-associated protein 1 (KAP1) arginine residues regulates the KAP1-ZNF224 interaction, thus suggesting that this KAP1 post-translational modification can actively contribute to the regulation of ZNF224-mediated repression
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2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-homocysteine + [SER-2 tyramine receptor]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [SER-2 tyramine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [SER-2 tyramine receptor]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT-5) regulates SER-2 tyramine receptor-mediated behaviors in Caenorhabditis elegans
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2 S-adenosyl-L-homocysteine + [SmD3 protein]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [SmD3 protein]-L-arginine
2 S-adenosyl-L-homocysteine + [SmD3 protein]-Nomega,Nomega'-dimethyl-L-arginine
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PRMT5 alone methylates both histone H4 and SmD3 proteins while PRMT5 complexed with p44 and pICln methylates SmD3 but not histone H4
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2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme methylates the R508 residue
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2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
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overall reaction, isoform PRMT9 symmetrically dimethylates arginine residues on splicing factor SF3B2. A peptide containing the methylatable Arg508 of SF3B2 is not recognized by PRMT9 in vitro. Amino acid substitutions of residues surrounding Arg508 have no great effect on PRMT9 recognition of SF3B2, but moving the arginine residue within this sequence abolishes methylation
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2 S-adenosyl-L-homocysteine + [voltage-gated sodium channel NaV1.5]-Nomega,Nomega'-dimethyl-L-arginine
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2 S-adenosyl-L-methionine + [voltage-gated sodium channel NaV1.5]-L-arginine
2 S-adenosyl-L-homocysteine + [voltage-gated sodium channel NaV1.5]-Nomega,Nomega'-dimethyl-L-arginine
PRMT5, along with PRMT3, binds to and methylate the voltage-gated sodium channel NaV1.5
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S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
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S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
histone H2A from calf thymus
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S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
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S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
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S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
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symmetric dimethylation is only observed when enzyme and the methyl-accepting substrate are incubated for extended times
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S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
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S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
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S-adenosyl-L-methionine + [myelin basic protein]-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
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S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega,Nomega'-dimethyl-L-arginine
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S-adenosyl-L-methionine + [myelin basic protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega,Nomega'-dimethyl-L-arginine
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methylation leads to omega-NG-monomethylarginine and and symmetric omega-NG,NG-dimethylarginine residues, no formation of asymmetric dimethylarginine residues
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myelin basic protein methylated by PRMT5 contains monomethylated and dimethylated arginine residues
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additional information
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myelin basic protein methylated by PRMT5 contains monomethylated and dimethylated arginine residues
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additional information
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isoform PRMT9 poorly methylates PRMT5 substrate GST-GAR
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additional information
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isoform PRMT9 poorly methylates PRMT5 substrate GST-GAR
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additional information
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PRMT5 alone methylates both histone H4 and SmD3 proteins while PRMT5 complexed with p44 and pICln methylates SmD3 but not histone H4
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additional information
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PRMT5 has a nonprocessive enzymatic mechanism for peptide substrates
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additional information
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PRMT5 has a nonprocessive enzymatic mechanism for peptide substrates
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additional information
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isoform Hsl7 has little or no activity on common substrate GST-GAR, and only minimal activity on myelin basic protein. Enzyme additionally shows type III protein arginine methyltransferase activity, EC 2.1.1.321
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additional information
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isoform Hsl7 has little or no activity on common substrate GST-GAR, and only minimal activity on myelin basic protein. Enzyme additionally shows type III protein arginine methyltransferase activity, EC 2.1.1.321
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additional information
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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
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additional information
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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
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additional information
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PRMT5-MEP50 activity is inhibited by substrate phosphorylation and enhanced by substrate acetylation
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additional information
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PRMT5-MEP50 activity is inhibited by substrate phosphorylation and enhanced by substrate acetylation
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