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Enzyme Nomenclature
Information on EC 2.1.1.319 - type I protein arginine methyltransferase
Word Map on EC 2.1.1.319
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.1.1.319
-
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RECOMMENDED NAME
GeneOntology No.
type I protein arginine methyltransferase
-
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
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
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
PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity present in mammalian cells and tissues
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 increased Smurf2 expression as well as inhibition of TGF-beta-mediated reporter activity
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; 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
-
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; 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
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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 + [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
-
?
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 + [FYSGFNS-dimethyl-R8-P-dimethyl-R10-GRVYATSWY]-L-arginine
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + [FYSGFNS-dimethyl-R8-PRG-dimethyl-R12-VYATSWY]-L-arginine
S-adenosyl-L-homocysteine + [FYSGFNS-dimethyl-R8-P-methyl-R10-G-dimethyl-R12-VYATSWY]-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [FYSGFNS-dimethyl-R8-PRGRVYATSWY]-L-arginine
S-adenosyl-L-homocysteine + [FYSGFNS-dimethyl-R8-P-methyl-R10-GRVYATSWY]-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [FYSGFNSRP-dimethyl-R10-G-dimethyl-R12-VYATSWY]-L-arginine
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + [FYSGFNSRP-methyl-R10-GRVYATSWY]-L-arginine
S-adenosyl-L-homocysteine + [FYSGFNSRP-dimethyl-R10-GRVYATSWY]-L-arginine
substrate is derived from bovine PABPN1. Methylation by isoform PRMT1 occurs exclusively at Arg10
-
-
?
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
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
-
-
-
?
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
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
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
-
-
-
?
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
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
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
?
-
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
?
-
-
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
?
-
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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.0007
[FYSGFNS-dimethyl-R8-PRG-dimethyl-R12-VYATSWY]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.00061
[FYSGFNS-dimethyl-R8-PRGRVYATSWY]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.008
[FYSGFNSRP-dimethyl-R10-G-dimethyl-R12-VYATSWY]-L-arginine
pH not specified in the publication, temperature not specified in the publication
-
0.00069
[FYSGFNSRP-methyl-R10-GRVYATSWY]-L-arginine
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]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
-
0.021
[FYSGFNS-dimethyl-R8-PRG-dimethyl-R12-VYATSWY]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
-
0.018
[FYSGFNS-dimethyl-R8-PRGRVYATSWY]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
-
0.0027
[FYSGFNSRP-dimethyl-R10-G-dimethyl-R12-VYATSWY]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
-
0.012
[FYSGFNSRP-methyl-R10-GRVYATSWY]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
-
0.0072
[PABPN1 mutant DeltaC20]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
-
0.0017
[PABPN1 mutant DeltaC27]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
-
0.00021
[PABPN1 mutant DeltaC33]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
-
0.00042
[PABPN1 mutant DeltaC40]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
-
0.023
[PABPN1 mutant DELTAC8]-L-arginine
Homo sapiens
Q99873
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]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206846
30.4
[FYSGFNS-dimethyl-R8-PRG-dimethyl-R12-VYATSWY]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206845
29.5
[FYSGFNS-dimethyl-R8-PRGRVYATSWY]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206844
0.3
[FYSGFNSRP-dimethyl-R10-G-dimethyl-R12-VYATSWY]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206847
17.9
[FYSGFNSRP-methyl-R10-GRVYATSWY]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206843
18.9
[PABPN1 mutant DeltaC20]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206849
26.5
[PABPN1 mutant DeltaC27]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206850
6.7
[PABPN1 mutant DeltaC33]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206851
0.1
[PABPN1 mutant DeltaC40]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206852
133.8
[PABPN1 mutant DELTAC8]-L-arginine
Homo sapiens
Q99873
pH not specified in the publication, temperature not specified in the publication
206848
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
retinal pigment epithelial cell; retinal pigment epithelial cell
additional information
isoform PRMT1 is the predominant protein arginine methyltransferase in RAT1 cells
additional information
isoform PRMT1 transcripts are detected from the zygote period to the early larva stage
additional information
enzyme is constitutively expressed during the Trypanosoma brucei life cycle
additional information
-
enzyme is constitutively expressed during the Trypanosoma brucei life cycle
-
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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
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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; 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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
oxidative stress induces apoptosis both via isoform PRMT1 in a SIRT1-dependent manner and via PRMT4 in a SIRT1-independent manner; oxidative stress induces apoptosis both via isoform PRMT1 in a SIRT1-dependent manner and via PRMT4 in a SIRT1-independent manner
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.319)
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