2.1.1.321: type III protein arginine methyltransferase
This is an abbreviated version!
For detailed information about type III protein arginine methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.321
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2.1.1.321
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prmt7
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histone
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monomethylation
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metastasis
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monomethylarginine
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dimethylarginine
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nanog
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adomet
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medicine
- 2.1.1.321
- prmt7
- histone
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monomethylation
- metastasis
-
monomethylarginine
- dimethylarginine
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nanog
- adomet
- medicine
Reaction
Synonyms
EC 2.1.1.124, EC 2.1.1.125, EC 2.1.1.126, EC 2.1.1.23, PRMT-7, PRMT7, protein arginine methyltransferase 7
ECTree
2.1.1.321 type III protein arginine methyltransferaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 2.1.1.321 - type III protein arginine methyltransferase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + [beta-catenin]-L-arginine
S-adenosyl-L-homocysteine + [beta-catenin]-Nomega-methyl-L-arginine
the enzyme (PRMT7) upregulates the expression of C-MYC via methylating beta-catenin and inhibiting the ubiquitin-mediated degradation of beta-catenin
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-
?
S-adenosyl-L-methionine + [eukaryotic translation initiation factor 2alpha]-L-arginine
S-adenosyl-L-homocysteine + [eukaryotic translation initiation factor 2alpha]-Nomega-methyl-L-arginine
PRMT7 methylates eukaryotic translation initiation factor 2alpha (eIF2alpha) and regulates its role in stress granule formation
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-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
S-adenosyl-L-methionine + [protein]-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
PRMT7 interacts with and methylates GLI2 on arginine residues 225 and 227 nearby a binding region of SUFU, a negative regulator of GLI2
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-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3
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-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
PRMT7-mediated monomethylation of histone H4 Arg17 regulates PRMT5 activity at Arg3 in the same protein
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-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3
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-
?
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
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-
-
?
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
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-
-
?
