2.1.1.319: type I protein arginine methyltransferase
This is an abbreviated version!
For detailed information about type I protein arginine methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.319
-
2.1.1.319
-
histone
-
methyltransferases
-
prmts
-
chromatin
-
dimethylarginine
-
estrogen
-
monomethylated
-
co-activator
-
rna-binding
-
dimethylaminohydrolase
-
nucleosomal
-
protein-arginine
-
cbp
-
ribonucleoproteins
-
hnrnp
-
hypomethylated
-
ddahs
-
rps2
-
medicine
-
arginine-rich
-
monomethylarginine
-
tudor
-
coactivator-1
-
mre11
-
methylation-dependent
-
h3k4me3
-
adomet
-
fibrillarin
-
nanog
-
non-histone
-
corepressors
- 2.1.1.319
- histone
- methyltransferases
-
prmts
- chromatin
- dimethylarginine
- estrogen
-
monomethylated
-
co-activator
-
rna-binding
-
dimethylaminohydrolase
-
nucleosomal
- protein-arginine
- cbp
- ribonucleoproteins
- hnrnp
-
hypomethylated
-
ddahs
- rps2
- medicine
-
arginine-rich
-
monomethylarginine
-
tudor
- coactivator-1
- mre11
-
methylation-dependent
-
h3k4me3
- adomet
- fibrillarin
-
nanog
-
non-histone
-
corepressors
Reaction
2 S-adenosyl-L-methionine
+
Synonyms
arginine methyltransferase 1, CARM1, coactivator-associated arginine methyltransferase 1, coactivator-associated arginine methyltransferase 1 variant 5, EC 2.1.1.124, EC 2.1.1.125, EC 2.1.1.126, EC 2.1.1.23, Eucgr.C03665.1, PRMT I, PRMT-1, PRMT1, PRMT10, PRMT2, PRMT3, PRMT4, PRMT6, PRMT8, protein arginine methyltransferase 1, protein arginine methyltransferase 2, protein arginine methyltransferase 4, protein arginine methyltransferase 6, protein arginine methyltransferase I, protein arginine N-methyltransferase 2, protein arginine N-methyltransferase I, RMT1, Tb927.1.4690, Tb927.5.3960, type I protein arginine methyltransferase
ECTree
2.1.1.319 type I protein arginine methyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.1.1.319 - type I protein arginine methyltransferase
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SUBSTRATE 
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
2 S-adenosyl-L-methionine + [beta-tubulin]-L-arginine
2 S-adenosyl-L-homocysteine + [beta-tubulin]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
-
?
2 S-adenosyl-L-methionine + [CBP/p300]-L-arginine
2 S-adenosyl-L-homocysteine + [CBP/p300]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [coiled-coil domain of p54nrb]-L-arginine
2 S-adenosyl-L-homocysteine + [coiled-coil domain of p54nrb]-Nomega,Nomega-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [Gly-Gly-Arg-Gly-Gly]-L-arginine
2 S-adenosyl-L-homocysteine + [Gly-Gly-Arg-Gly-Gly]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R17]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R17]-Nomega,Nomega-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [histone H3R26]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R26]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H4 peptide]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4 peptide]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
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 + [NCOA2]-L-arginine
2 S-adenosyl-L-homocysteine + [NCOA2]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [PABP1]-L-arginine
2 S-adenosyl-L-homocysteine + [PABP1]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [PABPN1 mutant DeltaC20]-L-arginine
2 S-adenosyl-L-homocysteine + [PABPN1 mutant DeltaC0]-Nomega,Nomega'-dimethyl-L-arginine
-
overall reaction
-
?
2 S-adenosyl-L-methionine + [PABPN1 mutant DeltaC27]-L-arginine
2 S-adenosyl-L-homocysteine + [PABPN1 mutant DeltaC27]-Nomega,Nomega'-dimethyl-L-arginine
-
overall reaction
-
?
2 S-adenosyl-L-methionine + [PABPN1 mutant DeltaC33]-L-arginine
2 S-adenosyl-L-homocysteine + [PABPN1 mutant DeltaC33]-Nomega,Nomega'-dimethyl-L-arginine
-
overall reaction
-
?
2 S-adenosyl-L-methionine + [PABPN1 mutant DeltaC40]-L-arginine
2 S-adenosyl-L-homocysteine + [PABPN1 mutant DeltaC40]-Nomega,Nomega'-dimethyl-L-arginine
-
overall reaction
-
?
2 S-adenosyl-L-methionine + [PABPN1 mutant DELTAC8]-L-arginine
2 S-adenosyl-L-homocysteine + [PABPN1 mutant DELTAC8]-Nomega,Nomega'-dimethyl-L-arginine
-
overall reaction
-
?
2 S-adenosyl-L-methionine + [PABPN1 protein]-L-arginine
2 S-adenosyl-L-homocysteine + [PABPN1 protein]-Nomega,Nomega'-dimethyl-L-arginine
-
overall reaction
-
?
2 S-adenosyl-L-methionine + [peptide]-L-arginine
2 S-adenosyl-L-homocysteine + [peptide]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine
a site of in vitro automethylation of mouse PRMT6 is characterized at position 7
-
-
?
2 S-adenosyl-L-methionine + [repressor splicing factor 1]-L-arginine
2 S-adenosyl-L-homocysteine + [repressor splicing factor 1]-Nomega,Nomega-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [SAP49]-L-arginine
2 S-adenosyl-L-homocysteine + [SAP49]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [SRC-3]-L-arginine
2 S-adenosyl-L-homocysteine + [SRC-3]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + FYSGFNS-dimethyl-R8-P-dimethyl-R10-GRVYATSWY
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + FYSGFNS-dimethyl-R8-PRG-dimethyl-R12-VYATSWY
S-adenosyl-L-homocysteine + FYSGFNS-dimethyl-R8-P-methyl-R10-G-dimethyl-R12-VYATSWY
-
-
-
?
S-adenosyl-L-methionine + FYSGFNS-dimethyl-R8-PRGRVYATSWY
S-adenosyl-L-homocysteine + FYSGFNS-dimethyl-R8-P-methyl-R10-GRVYATSWY
-
-
-
?
S-adenosyl-L-methionine + FYSGFNSRP-dimethyl-R10-G-dimethyl-R12-VYATSWY
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + FYSGFNSRP-methyl-R10-GRVYATSWY
S-adenosyl-L-homocysteine + FYSGFNSRP-dimethyl-R10-GRVYATSWY
substrate is derived from bovine PABPN1. Methylation by isoform PRMT1 occurs exclusively at Arg10
-
-
?
S-adenosyl-L-methionine + transition protein TP2
S-adenosyl-L-homocysteine + methylated transition protein TP2
-
enzyme methylates TP2 at Arg71, Arg75, and Arg92 residues. TP2R92me1 modifications appear in elongating to condensing spermatids and predominantly associated with the chromatin-bound TP2
-
?
S-adenosyl-L-methionine + [bovine mixed histones]-L-arginine
S-adenosyl-L-homocysteine + [bovine mixed histones]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [CGRGRGRGRGRGRGRG]-L-arginine
S-adenosyl-L-homocysteine + [CGRGRGRGRGRGRGRG]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [CGRGRGRGRGRGRGRG]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [CGRGRGRGRGRGRGRG]-Nomega,Nomega-dimethyl-L-arginine
S-adenosyl-L-methionine + [Ewing sarkoma protein]-L-arginine
S-adenosyl-L-homocysteine + [Ewing sarkoma protein]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [Ewing sarkoma protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [Ewing sarkoma protein]-Nomega,Nomega-dimethyl-L-arginine
S-adenosyl-L-methionine + [GRGGFGGRGGFRGGRGG]-L-arginine
S-adenosyl-L-homocysteine + [GRGGFGGRGGFRGGRGG]-Nomega-methyl-L-arginine
GRGGFGGRGGFRGGRGG i.e. synthetic peptide corresponding to residues 676-692 of human nucleolin
-
-
?
S-adenosyl-L-methionine + [GRGGFGGRGGFRGGRGG]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GRGGFGGRGGFRGGRGG]-Nomega,Nomega-dimethyl-L-arginine
GRGGFGGRGGFRGGRGG i.e. synthetic peptide corresponding to residues 676-692 of human nucleolin
-
-
?
S-adenosyl-L-methionine + [GST-GAR protein]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [GST-GAR protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega,Nomega-dimethyl-L-arginine
S-adenosyl-L-methionine + [GST-PRMT6]-L-arginine
S-adenosyl-L-homocysteine + [GST-PRMT6]-Nomega-methyl-L-arginine
-
self-methylation of glutathione S-transferase-PRMT6 fusion protein in the PRMT6-moiety
-
?
S-adenosyl-L-methionine + [GST-PRMT6]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-PRMT6]-Nomega,Nomega-dimethyl-L-arginine
-
self-methylation of glutathione S-transferase-PRMT6 fusion protein in the PRMT6-moiety
-
?
S-adenosyl-L-methionine + [heterogeneous nuclear ribonucleoprotein A1]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [heterogeneous nuclear ribonucleoprotein A1]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4]-L-arginine
S-adenosyl-L-homocysteine + [histone H4]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [interleukin enhancer-binding factor ILF3]-L-arginine
S-adenosyl-L-homocysteine + [interleukin enhancer-binding factor ILF3]-Nomega-methyl-L-arginine
-
the COOH-terminal region of ILF3, rich in arginine, glycine, and serine, is responsible for the strong interaction between PRMT1 and ILF3 and is the site of ILF3 methylation by PRMT1
-
?
S-adenosyl-L-methionine + [interleukin enhancer-binding factor ILF3]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [interleukin enhancer-binding factor ILF3]-Nomega,Nomega-dimethyl-L-arginine
-
the COOH-terminal region of ILF3, rich in arginine, glycine, and serine, is responsible for the strong interaction between PRMT1 and ILF3 and is the site of ILF3 methylation by PRMT1
-
?
S-adenosyl-L-methionine + [protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine
S-adenosyl-L-methionine + [RGG1 protein]-L-arginine
S-adenosyl-L-homocysteine + [RGG1 protein]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [RGG1 protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [RGG1 protein]-Nomega,Nomega-dimethyl-L-arginine
S-adenosyl-L-methionine + [Smurf2]-L-arginine
S-adenosyl-L-homocysteine + [Smurf2]-Nomega-methyl-L-arginine
-
Smurf2, i.e. a member of the HECT domain E3 ligase family. Smurf2, not Smurf1, is methylated by PRMT1. Among the type I PRMT family, only PRMT1 shows activity for Smurf2. Methylation sites are located within amino acid region 224-298 of Smurf2
-
-
?
S-adenosyl-L-methionine + [Smurf2]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [Smurf2]-Nomega,Nomega-dimethyl-L-arginine
-
Smurf2, i.e. a member of the HECT domain E3 ligase family. Smurf2, not Smurf1, is methylated by PRMT1. Among the type I PRMT family, only PRMT1 shows activity for Smurf2. Methylation sites are located within amino acid region 224-298 of Smurf2
-
-
?
S-adenosyl-L-methionine + [yeast Npl3 protein]-L-arginine
S-adenosyl-L-homocysteine + [yeast Npl3protein]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [yeast Npl3 protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [yeast Npl3 protein]-Nomega,Nomega-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [coiled-coil domain of p54nrb]-L-arginine
2 S-adenosyl-L-homocysteine + [coiled-coil domain of p54nrb]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [coiled-coil domain of p54nrb]-L-arginine
2 S-adenosyl-L-homocysteine + [coiled-coil domain of p54nrb]-Nomega,Nomega-dimethyl-L-arginine
the enzyme (CARM1) regulates this nuclear retention pathway at two levels: CARM1 methylates the coiled-coil domain of p54nrb, resulting in reduced binding of p54nrb to mRNAs containing inverted repeated Alu elements (IRAlus), and also acts as a transcription regulator to suppress NEAT1 transcription, leading to reduced paraspeckle formation. These actions of CARM1 work together synergistically to regulate the export of transcripts containing IRAlus from paraspeckles under certain cellular stresses, such as poly(I:C) treatment
-
-
?
2 S-adenosyl-L-methionine + [histone H3R17]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R17]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R17]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R17]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
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 H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
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 H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [repressor splicing factor 1]-L-arginine
2 S-adenosyl-L-homocysteine + [repressor splicing factor 1]-Nomega,Nomega-dimethyl-L-arginine
a nonhistone protein substrate belonging to the serine-/arginine-rich protein family is identified which interacts with the enzyme (PRMT2)
-
-
?
2 S-adenosyl-L-methionine + [repressor splicing factor 1]-L-arginine
2 S-adenosyl-L-homocysteine + [repressor splicing factor 1]-Nomega,Nomega-dimethyl-L-arginine
a nonhistone protein substrate belonging to the serine-/arginine-rich protein family is identified which interacts with the enzyme (PRMT2)
-
-
?
S-adenosyl-L-methionine + [bovine mixed histones]-L-arginine
S-adenosyl-L-homocysteine + [bovine mixed histones]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [bovine mixed histones]-L-arginine
S-adenosyl-L-homocysteine + [bovine mixed histones]-Nomega-methyl-L-arginine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
S-adenosyl-L-methionine + [CGRGRGRGRGRGRGRG]-L-arginine
S-adenosyl-L-homocysteine + [CGRGRGRGRGRGRGRG]-Nomega-methyl-L-arginine
substrate is a synthetic peptide
-
-
?
S-adenosyl-L-methionine + [CGRGRGRGRGRGRGRG]-L-arginine
S-adenosyl-L-homocysteine + [CGRGRGRGRGRGRGRG]-Nomega-methyl-L-arginine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
substrate is a synthetic peptide
-
-
?
S-adenosyl-L-methionine + [CGRGRGRGRGRGRGRG]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [CGRGRGRGRGRGRGRG]-Nomega,Nomega-dimethyl-L-arginine
substrate i.e. Trypanosoma brucei mitochondrial RNA binding protein
-
-
?
S-adenosyl-L-methionine + [CGRGRGRGRGRGRGRG]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [CGRGRGRGRGRGRGRG]-Nomega,Nomega-dimethyl-L-arginine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
substrate i.e. Trypanosoma brucei mitochondrial RNA binding protein
-
-
?
S-adenosyl-L-methionine + [Ewing sarkoma protein]-L-arginine
S-adenosyl-L-homocysteine + [Ewing sarkoma protein]-Nomega-methyl-L-arginine
Ewing sarkoma protein i.e a RNA-binding protein, is asymmetrically dimethylated at nine arginine residues located mainly in the C-terminal region of Ewing sarkoma protein
-
-
?
S-adenosyl-L-methionine + [Ewing sarkoma protein]-L-arginine
S-adenosyl-L-homocysteine + [Ewing sarkoma protein]-Nomega-methyl-L-arginine
Ewing sarkoma protein i.e a RNA-binding protein, is extensively asymmetrically dimethylated at arginine residues within RGG consensus sequences. Isoform PRMT1 recognizes most if not all methylation sites of the protein. Endogenous Ewing Sarkoma protein binds efficiently to GST-PRMT1 fusion protein
-
-
?
S-adenosyl-L-methionine + [Ewing sarkoma protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [Ewing sarkoma protein]-Nomega,Nomega-dimethyl-L-arginine
Ewing sarkoma protein i.e a RNA-binding protein, is asymmetrically dimethylated at nine arginine residues located mainly in the C-terminal region of Ewing sarkoma protein
-
-
?
S-adenosyl-L-methionine + [Ewing sarkoma protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [Ewing sarkoma protein]-Nomega,Nomega-dimethyl-L-arginine
Ewing sarkoma protein i.e a RNA-binding protein, is extensively asymmetrically dimethylated at arginine residues within RGG consensus sequences. Isoform PRMT1 recognizes most if not all methylation sites of the protein. Endogenous Ewing Sarkoma protein binds efficiently to GST-PRMT1 fusion protein
-
-
?
S-adenosyl-L-methionine + [GST-GAR protein]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [GST-GAR protein]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [GST-GAR protein]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [GST-GAR protein]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega-methyl-L-arginine
substrate is a fusion protein of Schistosoma japonicum glutathione S-transferase protein to the first 148 amino acids of human fibrillarin, containing 14 arginine residues in a glycine-rich region
-
-
?
S-adenosyl-L-methionine + [GST-GAR protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [GST-GAR protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [GST-GAR protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
-
-
?
S-adenosyl-L-methionine + [RGG1 protein]-L-arginine
S-adenosyl-L-homocysteine + [RGG1 protein]-Nomega-methyl-L-arginine
substrate i.e. Trypanosoma brucei mitochondrial RNA binding protein
-
-
?
S-adenosyl-L-methionine + [RGG1 protein]-L-arginine
S-adenosyl-L-homocysteine + [RGG1 protein]-Nomega-methyl-L-arginine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
substrate i.e. Trypanosoma brucei mitochondrial RNA binding protein
-
-
?
S-adenosyl-L-methionine + [RGG1 protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [RGG1 protein]-Nomega,Nomega-dimethyl-L-arginine
substrate i.e. Trypanosoma brucei mitochondrial RNA binding protein
-
-
?
S-adenosyl-L-methionine + [RGG1 protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [RGG1 protein]-Nomega,Nomega-dimethyl-L-arginine
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
substrate i.e. Trypanosoma brucei mitochondrial RNA binding protein
-
-
?
S-adenosyl-L-methionine + [yeast Npl3 protein]-L-arginine
S-adenosyl-L-homocysteine + [yeast Npl3protein]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [yeast Npl3 protein]-L-arginine
S-adenosyl-L-homocysteine + [yeast Npl3protein]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [yeast Npl3 protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [yeast Npl3 protein]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [yeast Npl3 protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [yeast Npl3 protein]-Nomega,Nomega-dimethyl-L-arginine
-
-
-
?
additional information
?
-
the consecutive transfer of two methyl groups to a single arginine side chain by isoform PRMT1 occurs in a distributive manner, i.e. with intermittent release of the monomethylated intermediate. The reaction is distributive even with substrates containing multiple methyl-accepting arginines, including one with 13 such residues. PRMT1 also does not prefer substrates already containing one or more singly or doubly methylated arginine residues, but the efficiency of methylation of one particular protein strongly depends on the number of methyl-accepting arginine residues it contains
-
-
?
additional information
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isoform PRMT3 asymmetrically dimethylates arginine residues present both in the substrate GST-GAR and in substrate proteins present in hypomethylated extracts of a yeast rmt1 mutant that lacks type I arginine methyltransferase activity
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identification of TgPRMT1 substrates. A number of candidate PRMT1 substrates are identified in this study. A significant proportion of candidate TgPRMT1 substrates localize to the nucleus
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isoform PRMT6 is a type I PRMT, catalyzing the production of monomethylarginine and asymmetric dimethylarginine residues. Enzyme does not methylate several Trypanosoma brucei glycine/arginine-rich proteins tested
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additional information
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Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
isoform PRMT6 is a type I PRMT, catalyzing the production of monomethylarginine and asymmetric dimethylarginine residues. Enzyme does not methylate several Trypanosoma brucei glycine/arginine-rich proteins tested
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