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Information on EC 2.1.1.319 - type I protein arginine methyltransferase and Organism(s) Homo sapiens and UniProt Accession P55345
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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 taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
prmt1, carm1, prmt6, prmt3, protein arginine methyltransferase 1, prmt8, prmt2, prmt4, coactivator-associated arginine methyltransferase 1, prmt-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CARM1
PRMT1
PRMT2
-
-
-
-
PRMT3
PRMT4
PRMT6
PRMT8
protein arginine methyltransferase 1
RMT1
-
-
-
-
CARM1
-
-
-
-
PRMT1
-
-
-
-
PRMT1
-
PRMT3
-
-
-
-
PRMT4
-
-
-
-
PRMT6
-
-
-
-
PRMT8
-
-
-
-
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.
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 + [CBP/p300]-L-arginine
2 S-adenosyl-L-homocysteine + [CBP/p300]-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 + [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 + [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 + [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 + [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
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
-
-
?
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
-
-
-
?
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]-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 + [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
-
-
-
?
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 + [CBP/p300]-L-arginine
2 S-adenosyl-L-homocysteine + [CBP/p300]-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 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 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
-
-
-
?
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
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
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
-
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
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
-
N1-methyl-N1-([5-[3-(trifluoromethyl)phenyl]-2H-1,2,3-triazol-4-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
-
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
-
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
-
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
-
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
-
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
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
0.025
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
0.00049
S-adenosyl-L-homocysteine
Homo sapiens
pH and temperature not specified in the publication
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isoform PRMT1 and interleukin enhancer-binding factor ILF3 colocalize in the nucleus
isoform PRMT8 is associated with the plasma membrane due to N-terminal myristoylation
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
drug target
malfunction
knockdown of PRMT1 reverses epithelial-mesenchymal transition in HCC cell lines and inhibits the proliferation of HepG2 and Hep3B 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
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
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
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 plays a regulatory role in thermogenic fat function
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
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 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 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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ANM2_HUMAN
433
0
49042
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
protein arginine N-methyltransferase 1 expression is significantly upregulated in hepatocellular carcinoma cell lines and clinical tissues
the enzyme is up-regulated and promotes migration, invasion and proliferation in wide range of cancers
two splice variants of PRMT1 (variants v.1 and v.2) are downregulated in breast cancer
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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
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
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)
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
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)
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
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)
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)
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)
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
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
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)
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
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)
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
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
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
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
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)
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