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
-
2.1.1.321
-
prmt7
-
histone
-
monomethylation
-
metastasis
-
monomethylarginine
-
dimethylarginine
-
nanog
-
adomet
-
medicine
- 2.1.1.321
- prmt7
- histone
-
monomethylation
- metastasis
-
monomethylarginine
- dimethylarginine
-
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
Advanced search results
Substrates Products
Substrates Products on EC 2.1.1.321 - type III protein arginine methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REACTION DIAGRAM
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega-dimethyl-L-arginine
3 S-adenosyl-L-methionine + SGRGKGGKGLGKGGAKRHRK-NH2
3 S-adenosyl-L-homocysteine + SG-(Nomega-Me)RGKGGKGLGKGGAK-(Nomega-Me)RH-(Nomega-Me)RK-NH2
-
-
-
?
5 S-adenosyl-L-methionine + AGRGRGKAAILKAQVAARGRGRGMGRGN-NH2
5 S-adenosyl-L-homocysteine + AG-(Nomega-Me)RG-(Nomega-Me)RGKAAILKAQVAA-(Nomega-Me)RG-(Nomega-Me)RGRGMG-(Nomega-Me)RGN-NH2
-
-
-
?
S-adenosyl-L-methionine + acetyl-GGRGG-NH2
S-adenosyl-L-homocysteine + acetyl-GG-(Nomega-methyl-)RGG-NH2
substrate is a synthetic peptide
-
-
?
S-adenosyl-L-methionine + GGFGGRGGFG-NH2
S-adenosyl-L-homocysteine + GGFGG-(Nomega-methyl-)RGGFG-NH2
substrate is a synthetic peptide
product is monomethylated at residue R6
-
?
S-adenosyl-L-methionine + GGPGGRGGPGG-NH2
S-adenosyl-L-homocysteine + GGPGG-Nomega-methyl-RGGPGG
substrate is a synthetic peptide
enzyme catalyzes monomethylation of Arg-residues
-
?
S-adenosyl-L-methionine + SG-(Nomega-methyl-)RGKGGKGLGKGGAKRHRK-NH2
S-adenosyl-L-homocysteine + SG-(Nomega-methyl-)RGKGGKGLGKGGAK-(Nomega-methyl-)RHRK-NH2
-
-
-
?
S-adenosyl-L-methionine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-L-arginine
S-adenosyl-L-homocysteine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [beta-catenin]-L-arginine
S-adenosyl-L-homocysteine + [beta-catenin]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [eukaryotic translation initiation factor 2alpha]-L-arginine
S-adenosyl-L-homocysteine + [eukaryotic translation initiation factor 2alpha]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [GLI2]-L-arginine
S-adenosyl-L-homocysteine + [GLI2]-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
-
-
?
S-adenosyl-L-methionine + [GST-GAR]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H2B peptide 23-37]-L-arginine
S-adenosyl-L-homocysteine + [histone H2B peptide 23-37]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H2B]-L-arginine
S-adenosyl-L-homocysteine + [histone H2B]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-arginine
S-adenosyl-L-homocysteine + [histone H3]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4 peptide 1-20]-L-arginine
S-adenosyl-L-homocysteine + [histone H4 peptide 1-20]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4 peptide 14-22]-L-arginine
S-adenosyl-L-homocysteine + [histone H4 peptide 14-22]-Nomega-methyl-L-arginine
-
-
-
?
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 + [human histone H2B peptide]-L-arginine
S-adenosyl-L-homocysteine + [human histone H2B peptide]-Nomega-methyl-L-arginine
Caenorhabditis elegans PRMT-7 is able to methylate synthetic human histone H2B peptides containing residues 23-37. The C. elegans enzyme recognizes the human peptide better than the Caenorhabditis elegans peptide. The histone H2B R29K peptide reduces methylation counts to a level about 40%, of that of the wild type peptide sequence. The R31K and R33K mutant peptides further decrease the activity to about 10% and 22% respectively, signifying the importance of arginine residues in a sequential R-X-R motif
-
-
?
S-adenosyl-L-methionine + [myelin basic protein]-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [protein]-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [Smb protein]-L-arginine
S-adenosyl-L-homocysteine + [Smb protein]-Nomega-methyl-L-arginine
-
-
-
?
2 S-adenosyl-L-homocysteine + [protein]-Nomega-dimethyl-L-arginine
the enzyme has a strong preference for RXR motifs surrounded by basic amino acids
-
-
?
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega-dimethyl-L-arginine
the enzyme has a strong preference for RXR motifs surrounded by basic amino acids
-
-
?
S-adenosyl-L-homocysteine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-Nomega-methyl-L-arginine
peptides based on the Arg-Gly-Gly (RGG)-containing RNA binding proteins are substrates in the naked form but are not substrates in the monomethylated form
-
-
?
S-adenosyl-L-methionine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-L-arginine
S-adenosyl-L-homocysteine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-Nomega-methyl-L-arginine
peptides based on the Arg-Gly-Gly (RGG)-containing RNA binding proteins are substrates in the naked form but are not substrates in the monomethylated form
-
-
?
S-adenosyl-L-homocysteine + [beta-catenin]-Nomega-methyl-L-arginine
-
-
-
?
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
-
-
?
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
-
-
?
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) within an RXR motif and regulates its role in stress granule formation
-
-
?
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
substrate preference for arginine residues in R-X-R motifs with additional flanking basic amino acid residues
-
-
?
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
-
-
?
S-adenosyl-L-methionine + [protein]-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
substrate preference for arginine residues in R-X-R motifs with additional flanking basic amino acid residues
-
-
?
?
-
enzyme is capable of forming only omega-NG-monomethylarginine, not asymmetric omega-NG,NG-dimethylarginine or symmetric omega-NG,NG-dimethylarginine. No substrates: SGAGKGGKGLGKGGAKAHAK-NH2, GRG-NH2
-
-
?
additional information
?
-
-
enzyme is capable of forming only omega-NG-monomethylarginine, not asymmetric omega-NG,NG-dimethylarginine or symmetric omega-NG,NG-dimethylarginine. No substrates: SGAGKGGKGLGKGGAKAHAK-NH2, GRG-NH2
-
-
?
additional information
?
-
no substrate: GST-fibrillarin fusion protein containing fibrillarin residues 1-148, substrate of isoforms PRMT1, PRMT3, PRMT4, PRMT5, EC 2.1.1.319. Isoform PRMT7 neither methylates myelin basic protein or histone H2A, in vitro substrates of PRMT5
-
-
?
additional information
?
-
argininosuccinate synthetase (ASS1) specifically interacts with PRMT7 and that mutations in ASS1 at the interaction interface of PRMT7-ASS1 are detrimental. The interaction of PRMT7 with ASS1 implies that ASS1 might be a plausible substrate of PRMT7
-
-
-