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Information on EC 2.1.1.319 - type I protein arginine methyltransferase
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EC Tree
2.1.1.319 type I protein arginine methyltransferaseIUBMB Comments
This eukaryotic enzyme catalyses the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues . PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells . cf. EC 2.1.1.320, type II protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
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Word Map
- 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
prmt1, carm1, prmt6, prmt3, protein arginine methyltransferase 1, prmt8, prmt2, prmt4, coactivator-associated arginine methyltransferase 1, prmt-1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CARM1
coactivator-associated arginine methyltransferase 1
EC 2.1.1.124
-
-
formerly, part transferred
-
EC 2.1.1.125
-
-
formerly, part transferred
-
EC 2.1.1.126
-
-
formerly, part transferred
-
EC 2.1.1.23
-
-
formerly, part transferred
-
PRMT1
PRMT2
PRMT3
PRMT4
PRMT6
PRMT8
protein arginine methyltransferase 1
protein arginine methyltransferase 2
protein arginine methyltransferase 4
RMT1
-
-
-
-
Tb927.1.4690
Tb927.5.3960
CARM1
-
-
-
-
PRMT1
-
-
-
-
PRMT1
-
PRMT2
-
-
-
-
PRMT3
-
-
-
-
PRMT4
-
-
-
-
PRMT6
-
-
-
-
PRMT8
-
-
-
-
protein arginine methyltransferase 1
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine
overall reaction
-
-
-
S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
(1a)
-
-
-
S-adenosyl-L-methionine + [protein]-Nomega-methyl-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine
(1b)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nomega,Nomega-dimethyl-L-arginine-forming)
This eukaryotic enzyme catalyses the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues [1]. PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells [2]. cf. EC 2.1.1.320, type II protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV 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
?
-
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
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
?
additional information
?
-
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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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
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
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 H3R26]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R26]-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 + [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
-
-
-
?
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
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14-benzoylacenaphtho[1',2':4,5]pyrido[2,1-b][1,3]benzothiazol-13-ium
cell membrane permeable inhibitor that effectively blocks proliferation of cancer cells including HELA, K562, and MCF7. Prediction of the binding mode of the inhibitors by molecular docking analysis indicates that the inhibitors competitively occupy the binding site of the substrate and destroy the protein-protein interactions between CARM1 and its substrates
2-[2-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]ethyl]guanidine
4-([6-[(2H-1,3-benzodioxol-5-yl)amino]-5-nitropyrimidin-4-yl]amino)benzene-1-carboximidamide
-
4-[(6-anilino-5-nitropyrimidin-4-yl)amino]benzene-1-carboximidamide
0.05 mM, 9% inhibition
4-[[5-nitro-6-(4-sulfamoylanilino)pyrimidin-4-yl]amino]benzene-1-carboximidamide
0.05 mM, 28% inhibition
4-[[6-(4-aminoanilino)-5-nitropyrimidin-4-yl]amino]benzene-1-carboximidamide
0.05 mM, 28% inhibition
4-[[6-(4-cyanoanilino)-5-nitropyrimidin-4-yl]amino]benzene-1-carboximidamide
-
4-[[6-(4-hydroxy-3,5-dimethoxyanilino)-5-nitropyrimidin-4-yl]amino]benzene-1-carboximidamide
0.05 mM, 44% inhibition
5'-([(3S)-3-amino-3-carboxypropyl]3-[[(pyridin-2-yl)amino]propyl]amino)-5'-deoxyadenosine
-
5'-([(3S)-3-amino-3-carboxypropyl]5-[[(iminiomethyl)amino]pentyl]amino)-5'-deoxyadenosine
-
5'-[(3-aminopropyl)[3-[(pyridin-2-yl)amino]propyl]amino]-5'-deoxyadenosine
-
5'-[(3-aminopropyl)[3-[(pyrimidin-2-yl)amino]propyl]amino]-5'-deoxyadenosine
-
5'-[(3-aminopropyl)[5-[(iminiomethyl)amino]pentyl]amino]-5'-deoxyadenosine
-
5'-[(3-[[amino(iminio)methyl]amino]propyl)(3-aminopropyl)amino]-5'-deoxyadenosine
-
5'-[(4-[[amino(iminio)methyl]amino]butyl)(3-aminopropyl)amino]-5'-deoxyadenosine
-
9-(ethoxycarbonyl)-1,4,8b,11,12,17a-hexahydrodibenzo[f,h]isoquinolino[2,1-b]isoquinolin-10-ium
cell membrane permeable inhibitor that effectively blocks proliferation of cancer cells including HELA, K562, and MCF7. Prediction of the binding mode of the inhibitors by molecular docking analysis indicates that the inhibitors competitively occupy the binding site of the substrate and destroy the protein-protein interactions between CARM1 and its substrates
Bay 11-7082
-
inhibits the protein arginine methyltransferase 1 (PRMT1) activity in vitro, and treatment of cells with the inhibitor causes the decline of the levels of protein asymmetric dimethylarginine catalyzed by PRMT1
Bay 11-7085
-
inhibits the protein arginine methyltransferase 1 (PRMT1) activity in vitro, and treatment of cells with the inhibitor causes the decline of the levels of protein asymmetric dimethylarginine catalyzed by PRMT1
Ca2+
weak inhibitor, 25% of the initial activity remains in the presence of 10 mM CaCl2
N,N'-dimethyl-N'-(1-(4-(2,2,2-trifluoroethoxy)phenyl)-1H-tetrazol-5-yl-methyl)ethylenediamine hydrochloride
-
N,N'-dimethyl-N'-(1-(4-isopropoxyphenyl)-1H-tetrazol-5-yl-methyl)ethylenediamine hydrochloride
non-competitive inhibition pattern with respect to either S-adenosyl-L-methionine or substrate arginine. Potent PRMT1 inhibitor, which can be used as lead compound for further drug discovery
N,N'-dimethyl-N'-(1-(4-trifluoromethoxyphenyl)-1H-tetrazol-5-yl-methyl)ethylenediamine hydrochloride
-
N-(1-(4-isopropoxyphenyl)-1H-tetrazol-5-yl-methyl)-N-methyl-ethylenediamine hydrochloride
-
N-(3-bromobenzyl)-1-(2-(methylamino)ethyl)piperidin-4-amine
potent and selective inhibitor of CARM1. It is around 20fold selective for CARM1 over PRMT6 and highly selective over PRMT1, PRMT3, PRMT8 as well as PRMT5 and PRMT7
N-aminoethyl-N'-(1-(4-isopropoxyphenyl)-1H-tetrazol-5-yl-methyl)-piperazinehydrochloride
-
N1-methyl-N1-([4-[3-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]methyl)ethane-1,2-diamine
-
N1-methyl-N1-([5-[3-(trifluoromethyl)phenyl]-2H-1,2,3-triazol-4-yl]methyl)ethane-1,2-diamine
the inhibitor is inactive against PRMT1, 3 and 4
-
N1-methyl-N1-[(4-[4-[(propan-2-yl)oxy]phenyl]-1H-pyrrol-3-yl)methyl]ethane-1,2-diamine
the inhibitor displays high potency for type I PRMTs including PRMT1, 3, 4, 6 and 8, but is completely inactive against type II and type III PRMTs, protein lysine methyltransferases and DNA methyltransferases. The inhibitor potently decreases cellular levels of histone arginine asymmetric dimethylation. MS094, a close analog of MS023, is developed which is inactive in biochemical and cellular assays, as a negative control for chemical biology studies. MS023 and MS094 are useful chemical tools for investigating the role of type I PRMTs in health and disease; the inhibitor displays high potency for type I PRMTs including PRMT1, 3, 4, 6 and 8, but is completely inactive against type II and type III PRMTs, protein lysine methyltransferases and DNA methyltransferases. The inhibitor potently decreases cellular levels of histone arginine asymmetric dimethylation. MS094, a close analog of MS023, is developed which is inactive in biochemical and cellular assays, as a negative control for chemical biology studies. MS023 and MS094 are useful chemical tools for investigating the role of type I PRMTs in health and disease; the inhibitor displays high potency for type I PRMTs including PRMT1, 3, 4, 6 and 8, but is completely inactive against type II and type III PRMTs, protein lysine methyltransferases and DNA methyltransferases. The inhibitor potently decreases cellular levels of histone arginine asymmetric dimethylation. MS094, a close analog of MS023, is developed which is inactive in biochemical and cellular assays, as a negative control for chemical biology studies. MS023 and MS094 are useful chemical tools for investigating the role of type I PRMTs in health and disease; the inhibitor displays high potency for type I PRMTs including PRMT1, 3, 4, 6 and 8, but is completely inactive against type II and type III PRMTs, protein lysine methyltransferases and DNA methyltransferases. The inhibitor potently decreases cellular levels of histone arginine asymmetric dimethylation. MS094, a close analog of MS023, is developed which is inactive in biochemical and cellular assays, as a negative control for chemical biology studies. MS023 and MS094 are useful chemical tools for investigating the role of type I PRMTs in health and disease
N2-[6-(4-carbamimidoylanilino)-5-nitropyrimidin-4-yl]glycinamide
0.05 mM, 49% inhibition
phenyl vinyl sulfonate
-
inhibits the protein arginine methyltransferase 1 (PRMT1) activity in vitro, and treatment of cells with the inhibitor causes the decline of the levels of protein asymmetric dimethylarginine catalyzed by PRMT1
phenyl vinyl sulfone
-
inhibits the protein arginine methyltransferase 1 (PRMT1) activity in vitro, and treatment of cells with the inhibitor causes the decline of the levels of protein asymmetric dimethylarginine catalyzed by PRMT1
tert-butyl (4-[[6-(4-carbamimidoylanilino)-5-nitropyrimidin-4-yl]amino]phenyl)carbamate
-
2-[2-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]ethyl]guanidine
-
2-[2-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]ethyl]guanidine
-
additional information
arginine methylation levels are increased when elt-2 is silenced, implying that erythroid-like transcription factor (ELT)-2 may have ability to inhibit methyltransferase activity of PRMT-1
-
additional information
-
arginine methylation levels are increased when elt-2 is silenced, implying that erythroid-like transcription factor (ELT)-2 may have ability to inhibit methyltransferase activity of PRMT-1
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
interleukin enhancer-binding factor ILF3
isoform PRMT1 and ILF3 coprecipitate in immunoprecipitation assays and can be isolated together in pull-down experiments. ILF3 is a robust substrate for methylation by PRMT1 and can modulate PRMT1 activity in in vitro methylation assays. 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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0222
FYSGFNS-dimethyl-R8-P-dimethyl-R10-GRVYATSWY
pH not specified in the publication, temperature not specified in the publication
0.0007
FYSGFNS-dimethyl-R8-PRG-dimethyl-R12-VYATSWY
pH not specified in the publication, temperature not specified in the publication
0.00061
FYSGFNS-dimethyl-R8-PRGRVYATSWY
pH not specified in the publication, temperature not specified in the publication
-
0.008
FYSGFNSRP-dimethyl-R10-G-dimethyl-R12-VYATSWY
pH not specified in the publication, temperature not specified in the publication
0.00069
FYSGFNSRP-methyl-R10-GRVYATSWY
pH not specified in the publication, temperature not specified in the publication
0.00037
[PABPN1 mutant DeltaC20]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.00007
[PABPN1 mutant DeltaC27]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.00003
[PABPN1 mutant DeltaC33]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.00323
[PABPN1 mutant DeltaC40]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.00018
[PABPN1 mutant DELTAC8]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0024
FYSGFNS-dimethyl-R8-P-dimethyl-R10-GRVYATSWY
pH not specified in the publication, temperature not specified in the publication
0.021
FYSGFNS-dimethyl-R8-PRG-dimethyl-R12-VYATSWY
pH not specified in the publication, temperature not specified in the publication
0.018
FYSGFNS-dimethyl-R8-PRGRVYATSWY
pH not specified in the publication, temperature not specified in the publication
-
0.0027
FYSGFNSRP-dimethyl-R10-G-dimethyl-R12-VYATSWY
pH not specified in the publication, temperature not specified in the publication
0.012
FYSGFNSRP-methyl-R10-GRVYATSWY
pH not specified in the publication, temperature not specified in the publication
0.0072
[PABPN1 mutant DeltaC20]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.0017
[PABPN1 mutant DeltaC27]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.00021
[PABPN1 mutant DeltaC33]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.00042
[PABPN1 mutant DeltaC40]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.023
[PABPN1 mutant DELTAC8]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
FYSGFNS-dimethyl-R8-P-dimethyl-R10-GRVYATSWY
pH not specified in the publication, temperature not specified in the publication
30.4
FYSGFNS-dimethyl-R8-PRG-dimethyl-R12-VYATSWY
pH not specified in the publication, temperature not specified in the publication
29.5
FYSGFNS-dimethyl-R8-PRGRVYATSWY
pH not specified in the publication, temperature not specified in the publication
-
0.3
FYSGFNSRP-dimethyl-R10-G-dimethyl-R12-VYATSWY
pH not specified in the publication, temperature not specified in the publication
17.9
FYSGFNSRP-methyl-R10-GRVYATSWY
pH not specified in the publication, temperature not specified in the publication
18.9
[PABPN1 mutant DeltaC20]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
26.5
[PABPN1 mutant DeltaC27]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
6.7
[PABPN1 mutant DeltaC33]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.1
[PABPN1 mutant DeltaC40]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
133.8
[PABPN1 mutant DELTAC8]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
4-[[6-(4-cyanoanilino)-5-nitropyrimidin-4-yl]amino]benzene-1-carboximidamide
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.036
14-benzoylacenaphtho[1',2':4,5]pyrido[2,1-b][1,3]benzothiazol-13-ium
Homo sapiens
pH 8.0, 23°C
0.0163
2-[2-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]ethyl]guanidine
Mus musculus
23°C, pH 8.0
0.025
4-([6-[(2H-1,3-benzodioxol-5-yl)amino]-5-nitropyrimidin-4-yl]amino)benzene-1-carboximidamide
Homo sapiens
pH and temperature not specified in the publication
0.038
4-[(6-amino-5-nitropyrimidin-4-yl)amino]benzene-1-carboximidamide
Homo sapiens
pH and temperature not specified in the publication
0.0093
4-[[6-(4-carbamimidoylanilino)-5-nitropyrimidin-4-yl]amino]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.002
4-[[6-(4-cyanoanilino)-5-nitropyrimidin-4-yl]amino]benzene-1-carboximidamide
Homo sapiens
pH and temperature not specified in the publication
0.0008
5'-([(3S)-3-amino-3-carboxypropyl]3-[[(pyridin-2-yl)amino]propyl]amino)-5'-deoxyadenosine
Homo sapiens
pH 7.3, 30°C
0.0241
5'-([(3S)-3-amino-3-carboxypropyl]5-[[(iminiomethyl)amino]pentyl]amino)-5'-deoxyadenosine
Homo sapiens
pH 7.3, 30°C
0.0003
5'-[(3-aminopropyl)[3-[(pyridin-2-yl)amino]propyl]amino]-5'-deoxyadenosine
Homo sapiens
pH 7.3, 30°C
0.0007
5'-[(3-aminopropyl)[3-[(pyrimidin-2-yl)amino]propyl]amino]-5'-deoxyadenosine
Homo sapiens
pH 7.3, 30°C
0.0177
5'-[(3-aminopropyl)[5-[(iminiomethyl)amino]pentyl]amino]-5'-deoxyadenosine
Homo sapiens
pH 7.3, 30°C
0.0023
5'-[(3-[[amino(iminio)methyl]amino]propyl)(3-aminopropyl)amino]-5'-deoxyadenosine
Homo sapiens
pH 7.3, 30°C
0.0087
5'-[(4-[[amino(iminio)methyl]amino]butyl)(3-aminopropyl)amino]-5'-deoxyadenosine
Homo sapiens
pH 7.3, 30°C
0.021
9-(ethoxycarbonyl)-1,4,8b,11,12,17a-hexahydrodibenzo[f,h]isoquinolino[2,1-b]isoquinolin-10-ium
Homo sapiens
pH 8.0, 23°C
0.0199
N,N'-dimethyl-N'-(1-(4-(2,2,2-trifluoroethoxy)phenyl)-1H-tetrazol-5-yl-methyl)ethylenediamine hydrochloride
Homo sapiens
pH and temperature not specified in the publication
0.0035
N,N'-dimethyl-N'-(1-(4-isopropoxyphenyl)-1H-tetrazol-5-yl-methyl)ethylenediamine hydrochloride
Homo sapiens
pH and temperature not specified in the publication
0.0238
N,N'-dimethyl-N'-(1-(4-trifluoromethoxyphenyl)-1H-tetrazol-5-yl-methyl)ethylenediamine hydrochloride
Homo sapiens
pH and temperature not specified in the publication
0.01
N-(1-(4-isopropoxyphenyl)-1H-tetrazol-5-yl-methyl)-N-methyl-ethylenediamine hydrochloride
Homo sapiens
pH and temperature not specified in the publication
0.000094
N-(3-bromobenzyl)-1-(2-(methylamino)ethyl)piperidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.029
N-aminoethyl-N'-(1-(4-isopropoxyphenyl)-1H-tetrazol-5-yl-methyl)-piperazinehydrochloride
Homo sapiens
pH and temperature not specified in the publication
0.000009 - 0.00111
N1-methyl-N1-([4-[3-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]methyl)ethane-1,2-diamine
0.00023
N1-methyl-N1-([5-[3-(trifluoromethyl)phenyl]-2H-1,2,3-triazol-4-yl]methyl)ethane-1,2-diamine
Homo sapiens
pH and temperature not specified in the publication
-
0.000004 - 0.000119
N1-methyl-N1-[(4-[4-[(propan-2-yl)oxy]phenyl]-1H-pyrrol-3-yl)methyl]ethane-1,2-diamine
0.013
tert-butyl (4-[[6-(4-carbamimidoylanilino)-5-nitropyrimidin-4-yl]amino]phenyl)carbamate
Homo sapiens
pH and temperature not specified in the publication
0.000009
N1-methyl-N1-([4-[3-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]methyl)ethane-1,2-diamine
Homo sapiens
pH and temperature not specified in the publication
0.00025
N1-methyl-N1-([4-[3-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]methyl)ethane-1,2-diamine
Homo sapiens
pH and temperature not specified in the publication
0.00111
N1-methyl-N1-([4-[3-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]methyl)ethane-1,2-diamine
Homo sapiens
pH and temperature not specified in the publication
0.000004
N1-methyl-N1-[(4-[4-[(propan-2-yl)oxy]phenyl]-1H-pyrrol-3-yl)methyl]ethane-1,2-diamine
Homo sapiens
pH and temperature not specified in the publication
0.00003
N1-methyl-N1-[(4-[4-[(propan-2-yl)oxy]phenyl]-1H-pyrrol-3-yl)methyl]ethane-1,2-diamine
Homo sapiens
pH and temperature not specified in the publication
0.000119
N1-methyl-N1-[(4-[4-[(propan-2-yl)oxy]phenyl]-1H-pyrrol-3-yl)methyl]ethane-1,2-diamine
Homo sapiens
pH and temperature not specified in the publication
0.00049
S-adenosyl-L-homocysteine
Homo sapiens
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Prmt1 is highly expressed in major metabolic organs and cell types, including thermogenic fat tissue and adipocytes
brenda
retinal pigment epithelial cell
brenda
additional information
isoform PRMT1 is the predominant protein arginine methyltransferase in RAT1 cells
brenda
PRMT1 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
brenda
PRMT4 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
brenda
additional information
isoform PRMT1 transcripts are detected from the zygote period to the early larva stage
brenda
additional information
-
isoform PRMT1 transcripts are detected from the zygote period to the early larva stage
brenda
additional information
enzyme is constitutively expressed during the Trypanosoma brucei life cycle
brenda
additional information
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
enzyme is constitutively expressed during the Trypanosoma brucei life cycle
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isoform PRMT8 is associated with the plasma membrane due to N-terminal myristoylation
brenda
PRMT1 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
brenda
PRMT4 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
brenda
PRMT1 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
brenda
PRMT4 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
brenda
isoform PRMT1 and interleukin enhancer-binding factor ILF3 colocalize in the nucleus
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
tamoxifen treatment induces a decrease in the enzyme (PRMT2) and an increase in ER-alpha36 as well as ER-alpha36-mediated non-genomic effect in MDA-MB-231 cells, which are relatively resistant to tamoxifen by contrast to MCF-7 cells. PRMT2 is able to interact with ER-alpha36 directly, suppress ER-alpha36 and downstream PI3K/Akt and MAPK/ERK signaling, reversing the tamoxifen resistance of breast cancer cells
physiological function
drug target
given the dual functions of PRMT1 (promotion of migration and invasion and inhibition of proliferation in gastric cancer cells), it is a potential drug target of gastric cancer with extreme caution
drug target
investigation of the role of the enzyme (PRMT2) in breast cancer progression and for developing a new endocrine therapeutic strategy for breast cancer patients with tamoxifen resistance
drug target
PRMT6 is overexpressed in several cancer types and is therefore considered as a potential anti-cancer drug target
drug target
protein arginine N-methyltransferase 1 expression is significantly upregulated in hepatocellular carcinoma cell lines and clinical tissues. Downregulation of protein arginine N-methyltransferase 1 in hepatocellular carcinoma cells by small interfering RNA could inhibit cell proliferation, migration, and invasion in vitro. The enzyme may contribute to hepatocellular carcinoma progression and serves as a promising target for the treatment of hepatocellular carcinoma patients
drug target
the enzme is associated with several human cancers including breast, colon, prostate and lung cancers and thus, is a potential oncological target
drug target
the enzyme (PRMT1) is a promising target for the treatment of cancer
malfunction
disruption of CARM1 enhances the nuclear retention of mRNAs containing inverted repeated Alu elements (IRAlus)
malfunction
knockdown of PRMT1 reverses epithelial-mesenchymal transition in HCC cell lines and inhibits the proliferation of HepG2 and Hep3B cells
malfunction
loss of Carm1 leads to a low sperm count and deformed sperm heads that can be attributed to defective elongation of round spermatids. RNA-seq analysis of Carm1-null spermatids reveals that the deregulated genes fell into similar categories as those impacted by p300-loss, thus providing a link between Carm1 and p300 (a major Carm1 substrate). CREMtau, a key testis-specific transcription factor, associates with p300 through its activator, ACT. This interaction is negatively regulates by the methylation of p300 by Carm1. Thus, high nuclear Carm1 levels negatively impact the p300/ACT/CREMtau axis during late stages of spermiogenesis
malfunction
Prmt1 ablation in adipocytes impairs thermogenic activation induced by cold exposure or beta3-adrenergic stimulation. Loss of enzyme (PRMT1) in mature adipocytes does not affect adipose tissue function at basal level. Loss of PRMT1 or overexpression of PRMT1 does not affect adipogenesis in fat cells
malfunction
PRMT6-deficient mice exhibit enhanced antiviral innate immunity. PRMT6 deficiency promotes the TBK1-IRF3 interaction and subsequently enhances IRF3 activation and type-I interferon production
malfunction
the null mutant of Caenorhabditis elegans prmt-1 is viable with no severe phenotype, despite loss of asymmetric arginine dimethylation
physiological function
arginine methyltransferases type II PRMT5 and type I PRMT4 mutants show similar alterations in flowering time, photomorphogenic responses and salt stress tolerance, while only prmt5 mutants exhibits alterations in circadian rhythms. PRMT5 and PRMT4s coregulate the expression and splicing of key regulatory genes associated with transcription, RNA processing, responses to light, flowering, and abiotic stress tolerance
physiological function
disruption of gene expression does not result in a significant growth defect in procyclic form Trypanosoma brucei. Isoform PRMT1 knock down leads to a dramatic decrease in the cellular level of asymmetric dimethylarginine
physiological function
knockdown of isoform PRMT1 results in delayed growth, shortened body-length, curled tails and cardiac edema. PRMT1 protein level, type I protein arginine methyltransferase activity, specific asymmetric protein arginine methylation and histone H4 R3 methylation all decreased in the knockdown mutants. The mutants show defective convergence and extension and the abnormalities are more severe at the posterior than the anterior parts. Cell migration defects are observed in the mutant embryos
physiological function
-
knockdown of isoform PRMT1 results in increased Smurf2 expression as well as inhibition of TGF-beta-mediated reporter activity
physiological function
knockdown of isoform PRMT6 in both procyclic form and bloodstream form Trypanosoma brucei leads to a modest but reproducible effect on parasite growth in culture. Upon PRMT6 depletion, both procyclic form and bloodstream form exhibit aberrant morphologies indicating defects in cell division, and these defects differ in the two life cycle stages. PRMT6-associated proteins are histones, components of the nuclear pore complex, and flagellar proteins
physiological function
PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity present in mammalian cells and tissues
physiological function
similar to H2O2 treatment, isoforms PRMT1 or PRMT4 overexpression increases retinal pigment epithelial cell damage. The H2O2-induced cell damage is attenuated by PRMT1 or PRMT4 knockdown and sirtuin SIRT1 overexpression
physiological function
similar to H2O2 treatment, isoforms PRMT1 or PRMT4 overexpression increases retinal pigment epithelial cell damage. The H2O2-induced cell damage is attenuated by PRMT1 or PRMT4 knockdown and sirtuin SIRT1 overexpression. SIRT1 expression is regulated by PRMT1
physiological function
a splicing isoform is characterized which does not affect the amino-terminus of the protein like the seven known isoforms, but rather lacks exons 8 and 9 which encode the dimerization arm of the enzyme that is essential for enzymatic activity. Consequently, the isoform does not form catalytically active oligomers with the other endogenous PRMT1 isoforms. This isoform is found in a variety of cell lines, but is increased in cell lines of cancer origin or after expression of the EMT-inducing transcriptional repressor Snail1. The novel isoform could act as a modulator of PRMT1 activity in cancer cells by acting as a competitive inhibitor that shields substrates from access to active PRMT1 oligomers
physiological function
dysregulation of PRMT1 is involved in a diverse range of diseases, including cancer
physiological function
enzyme (PRMT1) plays a regulatory role in thermogenic fat function
physiological function
important roles of the enzyme (PRMT1) in progression of gastric cancer. The enzyme is up-regulated and promotes migration, invasion and proliferation in wide range of cancers. PRMT1 promotes migration and invasion and inhibits proliferation in gastric cancer cells,whereas PRMT1 knockdown reverses the above abilities. PRMT1 reduces the expression of epithelial marker E-cadherin and increases the expression of mesenchymal markers including N-cadherin, Vimentin, snail and beta-catenin in gastric cancer cells. PRMT1 silencing promotes the phosphorylation of LATS1, and then induces YAP phosphorylation, while overexpression of PRMT1 down-regulates the phosphorylation of LATS1 and YAP, indicating that PRMT1 inhibits EMT probably via Hippo signaling
physiological function
overexpression or dysregulation of PRMT1 is associated with many diseases, particularly cancer
physiological function
PRMT1 expression, localization, and activity are altered following denervation-induced inactivity. Evidence from correlation, colocalization, and interaction analyses strongly support the existence of a novel, functional PRMT1-AMPKPGC-1alpha axis in skeletal muscle that is active during phenotypic remodeling elicited by denervation-evoked atrophy
physiological function
PRMT1 plays a regulatory role in thermogenic fat function
physiological function
PRMT2 is involved in a variety of cellular processes and has diverse roles in transcriptional regulation through different mechanisms depending on its binding partners
physiological function
PRMT2 is involved in a variety of cellular processes and has diverse roles in transcriptional regulation through different mechanisms depending on its binding partners
physiological function
PRMT4 expression, localization, and activity are altered following denervation-induced inactivity
physiological function
PRMT5 and PRMT1 are involved in the interaction between CFLARL (a CASP8 and FADD-like apoptosis regulator) and the E3 ligase ITCH. The PRMT5 silencing and PRMT1 overexpression enhance the interaction between CFLARL and ITCH, leading to an altered ubiquitination level and, eventually, the degradation of CFLARL
physiological function
protein arginine methyltransferase 4 (PRMT4) is an essential epigenetic regulator of fundamental and conserved processes during vertebrate development, such as pluripotency and differentiation
physiological function
the enzyme (CARM1) functions as a coactivator for various proteins that have been linked to cancer such as p53, NF-kappabeta, beta-catenin, E2F1 and steroid hormone receptor ERalpha. CARM1 is involved in transcriptional activation, cellular differentiation, cell cycle progression, RNA splicing and DNA damage response
physiological function
the enzyme (CARM1) is firmly implicated in transcriptional regulation
physiological function
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
physiological function
-
the enzyme (PRMT1) is important for cell division and growth. The enzyme (PRMT1) is a significant contributor to arginine monomethylation in Toxoplasma gondii
physiological function
-
the enzyme (PRMT1) methylate a number of key proteins and alters the transcription of a variety of genes involved in developmental processes. Appropriate levels of expression of type I PRMTs are necessary for the proper growth and development of Eucalyptus grandis roots. The enzyme (PRMT1) has a key role in root hair initiation and elongation and is involved in the methylation of beta-tubulin, a key protein in cytoskeleton formation
physiological function
the enzyme (PRMT1) represses MHC II transcription in macrophages by methylating Class II transactivator (CIITA)
physiological function
the enzyme (PRMT6) attenuates antiviral innate immunity by blocking TBK1-IRF3 signaling. Mechanistically, viral infection enhances the binding of PRMT6 to IRF3 and inhibited the interaction between IRF3 and TBK1. This mechanism is independent of PRMT6 methyltransferase activity
physiological function
the enzyme (PRMT6) is a protein arginine methyltransferase involved in transcriptional regulation, human immunodeficiency virus pathogenesis, DNA base excision repair, and cell cycle progression
physiological function
the enzyme catalyzes asymmetric arginine dimethylation of cellular proteins and thus modulates various biological processes, including gene regulation, RNA metabolism, cell signaling and DNA repair
physiological function
the enzyme is associated with various diseases including cancers
physiological function
the enzyme is involved in a variety of processes including transcription, DNA repair, and signal transduction
physiological function
the enzyme plays a critical role in the regulation of encystation
physiological function
the protein arginine methyltransferases 1 and 5 affect Myc properties in glioblastoma stem cells. Myc associates with both PRMT1 and PRMT5 being differentially dimethylated. Symmetric (S) by PRMT1 dimethylation protects Myc from degradation, while asymmetric (AS) dimethylation by PRMT5 allows Myc proper turnover. We hypothesize S-Myc as typical of aggressive glioblastoma stem cells, as S-Myc/AS-Myc ratio decreases in differentiating, less aggressive, cells
physiological function
via a mitochondrially mediated mechanism, the enzyme (PRMT1) is involved in driving the muscle differentiation program
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
disruption of gene expression does not result in a significant growth defect in procyclic form Trypanosoma brucei. Isoform PRMT1 knock down leads to a dramatic decrease in the cellular level of asymmetric dimethylarginine
-
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
knockdown of isoform PRMT6 in both procyclic form and bloodstream form Trypanosoma brucei leads to a modest but reproducible effect on parasite growth in culture. Upon PRMT6 depletion, both procyclic form and bloodstream form exhibit aberrant morphologies indicating defects in cell division, and these defects differ in the two life cycle stages. PRMT6-associated proteins are histones, components of the nuclear pore complex, and flagellar proteins
-
Show AA Sequence and Transmembrane Helices (1763 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the N-terminal end of isoform PRMT8 harbors a myristoylation motif. PRMT8 is modified by the attachment of a myristate to the glycine residue after the initiator methionine, resulting in its association with the plasma membrane
additional information
-
the N-terminal end of isoform PRMT8 harbors a myristoylation motif. PRMT8 is modified by the attachment of a myristate to the glycine residue after the initiator methionine, resulting in its association with the plasma membrane
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallisations of the enzyme (CARM1(135-479)) with inhibitors are carried out in 24-well plates using the sitting-drop vapour diffusion method
sitting-drop vapor-diffusion method at 20°C. Six crystal structures of PRMT6 are solved and refined at 1.34 A for the highest resolution structure.The crystal structures reveal that the folding of the helix aX is required to stabilize a productive active site before methylation of the bound peptide can occur. In the absence of cofactor, metal cations can be found in the catalytic pocket at the expected position of the guanidinium moiety of the target arginine substrate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H293S
mutant only produced the expected monomethyl arginine and dimethylarginine with reduced efficiency
M48F
mutation enables the enzyme to produce a limited amount of symmetric dimethylarginine product in addition to the expected monomethyl arginine and dimethylarginine products
M48F/H293S
the mutant enzyme generates a substantial amount of symmetric dimethylarginine product, with very little monomethyl arginine and dimethylarginine produced
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular cloning of alternative splice variants of PRMT1 with the use of 3' RACE coupled with next-generation sequencing technology. 58 PRMT1 transcripts are identified, 34 of which are mRNAs encoding protein isoforms, whereas the rest 24 transcripts are candidates for nonsense-mediated mRNA decay
prmt6 is cloned in the pnEA-vHis vector between the NdeI and XhoI restriction sites and used to transform Escherichia coli BL21 (DE3) pRARE2 cells. The resulting recombinant protein harbors an amino-terminal hexahistidine tag followed by a Tobacco etch virus (TEV) protease cleavage site. The protein also contains a F315L point mutation, reported for the entry as a natural variant
the enzyme (PRMT2) is expressed in insect cells using the baculovirus system
the enzyme (PRMT2) is expressed in insect cells using the baculovirus system
the enzyme (PRMT2) is expressed in insect cells using the baculovirus system
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression levels is highly increased after induction of encystation from 24-72 h
expression of PRMT1 mRNA and protein content are significantly induced in skeletal muscle cells during the phenotypic remodeling elicited by myogenesis
following 72 h and 168 h of denervation, PRMT1 protein content increases 3.6-5fold
H2O2 treatment increases isoforms PRMT1 and PRMT4 expression but decreases sirtuin SIRT1 expression. Similar to H2O2 treatment, PRMT1 or PRMT4 overexpression increases retinal pigment epithelial cell damage
PRMT1 mRNA content in the denervated soleus muscle decreases by 32% and 37% as compared with the control muscle after 6 and 12 h, respectively
PRMT4 mRNA content increases 2.3fold or 1.7fold in the denervated muscle compared with the control muscle after 72 and 168 h of denervation, respectively
protein arginine N-methyltransferase 1 expression is significantly upregulated in hepatocellular carcinoma cell lines and clinical tissues
relative to the control muscle, PRMT4 mRNA expression levels in the denervated soleus muscle is decreased by 31% after 12 h
the enzyme is up-regulated and promotes migration, invasion and proliferation in wide range of cancers
the GATA transcription factor elt-2 is a positive regulator of Pprmt-1:: gfp expression. elt-2 RNAi decreases endogenous PRMT-1 expression at mRNA and protein levels
two splice variants of PRMT1 (variants v.1 and v.2) are downregulated in breast cancer
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
oxidative stress induces apoptosis both via isoform PRMT1 in a SIRT1-dependent manner and via PRMT4 in a SIRT1-independent manner
medicine
modulating PRMT1 activity may represent new avenues to regulate thermogenic fat and mediate energy homeostasis and may ultimately lead to therapeutic strategies against human obesity and associated metabolic disorders
medicine
modulating PRMT1 activity may represent new avenues to regulate thermogenic fat and mediate energy homeostasis and may ultimately lead to therapeutic strategies against human obesity and associated metabolic disorders
medicine
PRMT1 and PRMT5 have opposing effects on chemotherapeutic agent-mediated apoptosis in lung cancer cells. The identification of PRMT5 and PRMT1 as CFLARL regulators involved in cellular apoptosis may help in developing new strategies to increase the sensitivity of cancer cells to chemotherapy, which may eventually benefit lung cancer treatments
medicine
splive variant PRMT1 v.2 promotes the survival and invasiveness of breast cancer cells, while it could serve as a biomarker of unfavorable prognosis in colon cancer patients
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hernando, C.E.; Sanchez, S.E.; Mancini, E.; Yanovsky, M.J.
Genome wide comparative analysis of the effects of PRMT5 and PRMT4/CARM1 arginine methyltransferases on the Arabidopsis thaliana transcriptome
BMC Genomics
16
192
2015
Arabidopsis thaliana (Q9MAT5)
brenda
Fisk, J.C.; Zurita-Lopez, C.; Sayegh, J.; Tomasello, D.L.; Clarke, S.G.; Read, L.K.
TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma brucei
Eukaryot. Cell
9
866-877
2010
Trypanosoma brucei brucei (Q57U70), Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927 (Q57U70)
brenda
Tsai, Y.J.; Pan, H.; Hung, C.M.; Hou, P.T.; Li, Y.C.; Lee, Y.J.; Shen, Y.T.; Wu, T.T.; Li, C.
The predominant protein arginine methyltransferase PRMT1 is critical for zebrafish convergence and extension during gastrulation
FEBS J.
278
905-917
2011
Danio rerio (Q803D9), Danio rerio
brenda
Tang, J.; Gary, J.D.; Clarke, S.; Herschman, H.R.
PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
J. Biol. Chem.
273
16935-16945
1998
Rattus norvegicus (O70467)
brenda
Tang, J.; Kao, P.N.; Herschman, H.R.
Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3
J. Biol. Chem.
275
19866-19876
2000
Homo sapiens (Q99873)
brenda
Tang, J.; Frankel, A.; Cook, R.J.; Kim, S.; Paik, W.K.; Williams, K.R.; Clarke, S.; Herschman, H.R.
PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells
J. Biol. Chem.
275
7723-7730
2000
Rattus norvegicus (Q63009)
brenda
Frankel, A.; Yadav, N.; Lee, J.; Branscombe, T.L.; Clarke, S.; Bedford, M.T.
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
J. Biol. Chem.
277
3537-3543
2002
Homo sapiens (Q96LA8), Homo sapiens
brenda
Lee, J.; Sayegh, J.; Daniel, J.; Clarke, S.; Bedford, M.T.
PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family
J. Biol. Chem.
280
32890-32896
2005
Homo sapiens (Q9NR22), Homo sapiens
brenda
Koelbel, K.; Ihling, C.; Bellmann-Sickert, K.; Neundorf, I.; Beck-Sickinger, A.G.; Sinz, A.; Kuehn, U.; Wahle, E.
Type I arginine methyltransferases PRMT1 and PRMT-3 act distributively
J. Biol. Chem.
284
8274-8282
2009
Homo sapiens (Q99873)
brenda
Gupta, N.; Madapura, M.P.; Bhat, U.A.; Rao, M.R.
Mapping of post-translational modifications of transition proteins, TP1 and TP2, and identification of protein arginine methyltransferase 4 and lysine methyltransferase 7 as methyltransferase for TP2
J. Biol. Chem.
290
12101-12122
2015
Rattus norvegicus (A0A068FP44)
brenda
Pelletier, M.; Pasternack, D.A.; Read, L.K.
In vitro and in vivo analysis of the major type I protein arginine methyltransferase from Trypanosoma brucei
Mol. Biochem. Parasitol.
144
206-217
2005
Trypanosoma brucei brucei (Q4GYA9), Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927 (Q4GYA9)
brenda
Cha, B.; Park, Y.; Hwang, B.N.; Kim, S.Y.; Jho, E.H.
Protein arginine methyltransferase 1 methylates Smurf2
Mol. Cells
38
723-728
2015
Mus musculus
brenda
Kim, D.I.; Park, M.J.; Choi, J.H.; Kim, I.S.; Han, H.J.; Yoon, K.C.; Park, S.W.; Lee, M.Y.; Oh, K.S.; Park, S.H.
PRMT1 and PRMT4 regulate oxidative stress-induced retinal pigment epithelial cell damage in SIRT1-dependent and SIRT1-independent manners
Oxid. Med. Cell. Longev.
2015
617919
2015
Homo sapiens (Q86X55), Homo sapiens (Q99873), Homo sapiens
brenda
Pahlich, S.; Bschir, K.; Chiavi, C.; Belyanskaya, L.; Gehring, H.
Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide
Proteins
61
164-175
2005
Homo sapiens (O60678), Homo sapiens (Q99873)
brenda
Eram, M.S.; Shen, Y.; Szewczyk, M.; Wu, H.; Senisterra, G.; Li, F.; Butler, K.V.; Kaniskan, H.U.e.; Speed, B.A.; Dela Sena, C.; Dong, A.; Zeng, H.; Schapira, M.; Brown, P.J.; Arrowsmith, C.H.; Barsyte-Lovejoy, D.; Liu, J.; Vedadi, M.; Jin, J.
A potent, selective, and cell-active inhibitor of human type I protein arginine methyltransferases
ACS Chem. Biol.
11
772-781
2016
Homo sapiens (O60678), Homo sapiens (Q86X55), Homo sapiens (Q96LA8), Homo sapiens (Q99873), Homo sapiens (Q9NR22), Homo sapiens
brenda
Stouth, D.W.; Manta, A.; Ljubicic, V.
Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity
Am. J. Physiol. Cell Physiol.
314
C177-C190
2018
Mus musculus (Q9JIF0), Mus musculus (Q9WVG6)
brenda
Gunnell, E.A.; Al-Noori, A.; Muhsen, U.; Davies, C.C.; Dowden, J.; Dreveny, I.
Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4)
Biochem. J.
477
787-800
2020
Homo sapiens (Q86X55), Homo sapiens (Q99873)
brenda
Ye, F.; Zhang, W.; Lu, W.; Xie, Y.; Jiang, H.; Jin, J.; Luo, C.
Identification of novel inhibitors against coactivator associated arginine methyltransferase 1 based on virtual screening and biological assays
BioMed Res. Int.
2016
7086390
2016
Homo sapiens (Q86X55)
brenda
Gathiaka, S.; Boykin, B.; Caceres, T.; Hevel, J.M.; Acevedo, O.
Understanding protein arginine methyltransferase 1 (PRMT1) product specificity from molecular dynamics
Bioorg. Med. Chem.
24
4949-4960
2016
Rattus norvegicus (Q63009)
brenda
Yu, X.R.; Tang, Y.; Wang, W.J.; Ji, S.; Ma, S.; Zhong, L.; Zhang, C.H.; Yang, J.; Wu, X.A.; Fu, Z.Y.; Li, L.L.; Yang, S.Y.
Discovery and structure-activity analysis of 4-((5-nitropyrimidin-4-yl)amino)benzimidamide derivatives as novel protein arginine methyltransferase 1 (PRMT1) inhibitors
Bioorg. Med. Chem. Lett.
25
5449-5453
2015
Homo sapiens (Q99873)
brenda
Shen, N.Y.; Ng, S.Y.; Toepp, S.L.; Ljubicic, V.
Protein arginine methyltransferase expression and activity during myogenesis
Biosci. Rep.
38
BSR20171533
2018
Mus musculus (Q9JIF0)
brenda
Yu, C.H.; Chou, C.C.; Lee, D.Y.; Khoo, K.H.; Chang, G.D.
Target identification reveals protein arginine methyltransferase 1 is a potential target of phenyl vinyl sulfone and its derivatives
Biosci. Rep.
38
BSR20171717
2018
Homo sapiens
brenda
Plett, K.; Raposo, A.; Bullivant, S.; Anderson, I.; Piller, S.; Plett, J.
Root morphogenic pathways in Eucalyptus grandis are modified by the activity of protein arginine methyltransferases
BMC Plant Biol.
17
62
2017
Eucalyptus grandis
brenda
Zhang, H.; Han, C.; Li, T.; Li, N.; Cao, X.
The methyltransferase PRMT6 attenuates antiviral innate immunity by blocking TBK1-IRF3 signaling
Cell. Mol. Immunol.
16
800-809
2019
Mus musculus (Q6NZB1)
brenda
Qiao, X.; Kim, D.I.; Jun, H.; Ma, Y.; Knights, A.J.; Park, M.J.; Zhu, K.; Lipinski, J.H.; Liao, J.; Li, Y.; Richard, S.; Weinman, S.A.; Wu, J.
Protein arginine methyltransferase 1 interacts with PGC1alpha and modulates thermogenic fat activation
Endocrinology
160
2773-2786
2019
Homo sapiens (Q99873), Homo sapiens, Mus musculus (Q9JIF0), Mus musculus
brenda
Zhang, Y.; Wang, D.; Zhang, M.; Wei, H.; Lu, Y.; Sun, Y.; Zhou, M.; Gu, S.; Feng, W.; Wang, H.; Zeng, J.; Gong, A.; Xu, M.
Protein arginine methyltransferase 1 coordinates the epithelial-mesenchymal transition/proliferation dichotomy in gastric cancer cells
Exp. Cell Res.
362
43-50
2018
Homo sapiens (Q99873)
brenda
Cura, V.; Marechal, N.; Troffer-Charlier, N.; Strub, J.M.; van Haren, M.J.; Martin, N.I.; Cianferani, S.; Bonnefond, L.; Cavarelli, J.
Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors
FEBS J.
284
77-96
2017
Danio rerio (A1L1Q4), Mus musculus (Q9R144)
brenda
Berberich, H.; Terwesten, F.; Rakow, S.; Sahu, P.; Bouchard, C.; Meixner, M.; Philipsen, S.; Kolb, P.; Bauer, U.M.
Identification and insilico structural analysis of Gallus gallus protein arginine methyltransferase 4 (PRMT4)
FEBS open bio
7
1909-1923
2017
Gallus gallus (A0A2D3I4C6)
brenda
Adamopoulos, P.G.; Mavrogiannis, A.V.; Kontos, C.K.; Scorilas, A.
Novel alternative splice variants of the human protein arginine methyltransferase 1 (PRMT1) gene, discovered using next-generation sequencing
Gene
699
135-144
2019
Homo sapiens (Q99873), Homo sapiens
brenda
Hu, S.B.; Xiang, J.F.; Li, X.; Xu, Y.; Xue, W.; Huang, M.; Wong, C.C.; Sagum, C.A.; Bedford, M.T.; Yang, L.; Cheng, D.; Chen, L.L.
Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus
Genes Dev.
29
630-645
2015
Mus musculus (Q9WVG6)
brenda
Sun, Y.; Wang, Z.; Yang, H.; Zhu, X.; Wu, H.; Ma, L.; Xu, F.; Hong, W.; Wang, H.
The Development of tetrazole derivatives as protein arginine methyltransferase I (PRMT I) inhibitors
Int. J. Mol. Sci.
20
3840
2019
Homo sapiens (Q99873)
brenda
Araoi, S.; Daitoku, H.; Yokoyama, A.; Kako, K.; Hirota, K.; Fukamizu, A.
The GATA transcription factor ELT-2 modulates both the expression and methyltransferase activity of PRMT-1 in Caenorhabditis elegans
J. Biochem.
163
433-440
2018
Caenorhabditis elegans (Q9U2X0), Caenorhabditis elegans
brenda
Patounas, O.; Papacharalampous, I.; Eckerich, C.; Markopoulos, G.S.; Kolettas, E.; Fackelmayer, F.O.
A novel splicing isoform of protein arginine methyltransferase 1 (PRMT1) that lacks the dimerization arm and correlates with cellular malignancy
J. Cell. Biochem.
119
2110-2123
2018
Homo sapiens (Q99873), Homo sapiens
brenda
Li, M.; An, W.; Xu, L.; Lin, Y.; Su, L.; Liu, X.
The arginine methyltransferase PRMT5 and PRMT1 distinctly regulate the degradation of anti-apoptotic protein CFLARL in human lung cancer cells
J. Exp. Clin. Cancer Res.
38
64
2019
Homo sapiens (Q99873), Homo sapiens
brenda
Bonnefond, L.; Stojko, J.; Mailliot, J.; Troffer-Charlier, N.; Cura, V.; Wurtz, J.M.; Cianferani, S.; Cavarelli, J.
Functional insights from high resolution structures of mouse protein arginine methyltransferase 6
J. Struct. Biol.
191
175-183
2015
Mus musculus (Q6NZB1), Mus musculus
brenda
Moon, E.K.; Kong, H.H.; Hong, Y.; Lee, H.A.; Quan, F.S.
Identification and Characterization of Protein Arginine Methyltransferase 1 in Acanthamoeba castellanii
Korean J. Parasitol.
55
109-114
2017
Acanthamoeba castellanii (A0A0U3T8U3), Acanthamoeba castellanii
brenda
Kaniskan, H.U.e.; Eram, M.S.; Liu, J.; Smil, D.; Martini, M.L.; Shen, Y.; Santhakumar, V.; Brown, P.J.; Arrowsmith, C.; Vedadi, M.; Jin, J.
Design and synthesis of selective, small molecule inhibitors of coactivator-associated arginine methyltransferase 1 (CARM1)
MedChemComm
7
1793-1796
2016
Homo sapiens (Q86X55), Homo sapiens
brenda
Yakubu, R.R.; Silmon de Monerri, N.C.; Nieves, E.; Kim, K.; Weiss, L.M.
Comparative monomethylarginine proteomics suggests that protein arginine methyltransferase 1 (PRMT1) is a significant contributor to arginine monomethylation in Toxoplasma gondii
Mol. Cell. Proteomics
16
567-580
2017
Toxoplasma gondii
brenda
Bao, J.; Rousseaux, S.; Shen, J.; Lin, K.; Lu, Y.; Bedford, M.T.
The arginine methyltransferase CARM1 represses p300/ACT/CREMtau activity and is required for spermiogenesis
Nucleic Acids Res.
46
4327-4343
2018
Mus musculus (Q9WVG6), Mus musculus
brenda
Shen, Y.; Zhong, J.; Liu, J.; Liu, K.; Zhao, J.; Xu, T.; Zeng, T.; Li, Z.; Chen, Y.; Ding, W.; Wen, G.; Zu, X.; Cao, R.
Protein arginine N-methyltransferase2 reverses tamoxifen resistance in breast cancer cells through suppression of ER-alpha36
Oncol. Rep.
39
2604-2612
2018
Homo sapiens (P55345), Homo sapiens
brenda
Fan, Z.; Li, J.; Li, P.; Ye, Q.; Xu, H.; Wu, X.; Xu, Y.
Protein arginine methyltransferase 1 (PRMT1) represses MHC II transcription in macrophages by methylating CIITA
Sci. Rep.
7
40531
2017
Mus musculus (Q9JIF0)
brenda
Favia, A.; Salvatori, L.; Nanni, S.; Iwamoto-Stohl, L.; Valente, S.; Mai, A.; Scagnoli, F.; Fontanella, R.; Totta, P.; Nasi, S.; Illi, B.
The protein arginine methyltransferases 1 and 5 affect Myc properties in glioblastoma stem cells
Sci. Rep.
9
15925
2019
Homo sapiens (Q99873)
brenda
Gou, Q.; He, S.; Zhou, Z.
Protein arginine N-methyltransferase 1 promotes the proliferation and metastasis of hepatocellular carcinoma cells
Tumour Biol.
39
1010428317691419
2017
Homo sapiens (Q99873)
brenda
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