Information on EC 2.1.1.319 - type I protein arginine methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.319
-
RECOMMENDED NAME
GeneOntology No.
type I protein arginine methyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine
show the reaction diagram
overall reaction
-
-
-
S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
show the reaction diagram
(1a)
-
-
-
S-adenosyl-L-methionine + [protein]-Nomega-methyl-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine
show the reaction diagram
(1b)
-
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform PRMT4
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
overall reaction
-
?
2 S-adenosyl-L-methionine + [PABPN1 protein]-L-arginine
2 S-adenosyl-L-homocysteine + [PABPN1 protein]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
overall reaction
-
?
S-adenosyl-L-methionine + transition protein TP2
S-adenosyl-L-homocysteine + methylated transition protein TP2
show the reaction diagram
-
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
show the reaction diagram
S-adenosyl-L-methionine + [CGRGRGRGRGRGRGRG]-L-arginine
S-adenosyl-L-homocysteine + [CGRGRGRGRGRGRGRG]-Nomega-methyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [CGRGRGRGRGRGRGRG]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [CGRGRGRGRGRGRGRG]-Nomega,Nomega-dimethyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [Ewing sarkoma protein]-L-arginine
S-adenosyl-L-homocysteine + [Ewing sarkoma protein]-Nomega-methyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [Ewing sarkoma protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [Ewing sarkoma protein]-Nomega,Nomega-dimethyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [FYSGFNS-dimethyl-R8-P-dimethyl-R10-GRVYATSWY]-L-arginine
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [FYSGFNS-dimethyl-R8-PRGRVYATSWY]-L-arginine
S-adenosyl-L-homocysteine + [FYSGFNS-dimethyl-R8-P-methyl-R10-GRVYATSWY]-L-arginine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [FYSGFNSRP-dimethyl-R10-G-dimethyl-R12-VYATSWY]-L-arginine
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [FYSGFNSRP-methyl-R10-GRVYATSWY]-L-arginine
S-adenosyl-L-homocysteine + [FYSGFNSRP-dimethyl-R10-GRVYATSWY]-L-arginine
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
S-adenosyl-L-methionine + [GST-GAR protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR protein]-Nomega,Nomega-dimethyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [GST-PRMT6]-L-arginine
S-adenosyl-L-homocysteine + [GST-PRMT6]-Nomega-methyl-L-arginine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [histone H4]-L-arginine
S-adenosyl-L-homocysteine + [histone H4]-Nomega-methyl-L-arginine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [histone H4]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega-dimethyl-L-arginine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [interleukin enhancer-binding factor ILF3]-L-arginine
S-adenosyl-L-homocysteine + [interleukin enhancer-binding factor ILF3]-Nomega-methyl-L-arginine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
S-adenosyl-L-methionine + [RGG1 protein]-L-arginine
S-adenosyl-L-homocysteine + [RGG1 protein]-Nomega-methyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [RGG1 protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [RGG1 protein]-Nomega,Nomega-dimethyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [Smurf2]-L-arginine
S-adenosyl-L-homocysteine + [Smurf2]-Nomega-methyl-L-arginine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
S-adenosyl-L-methionine + [yeast Npl3 protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [yeast Npl3 protein]-Nomega,Nomega-dimethyl-L-arginine
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
;
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
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
-
0.00035 - 0.0008
[GRGGFGGRGGFRGGRGG]-L-arginine
-
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 hide
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
-
0.0065 - 0.036
[GRGGFGGRGGFRGGRGG]-L-arginine
-
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
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
8.1 - 100
[GRGGFGGRGGFRGGRGG]-L-arginine
206842
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 0.0027
S-adenosyl-L-homocysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000144
37C, pH 7.4
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
constitutive expression
Manually annotated by BRENDA team
retinal pigment epithelial cell; retinal pigment epithelial cell
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
predominant localization
Manually annotated by BRENDA team
-
isoform PRMT1 and interleukin enhancer-binding factor ILF3 colocalize in the nucleus
Manually annotated by BRENDA team
isoform PRMT8 is associated with the plasma membrane due to N-terminal myristoylation
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41900
x * 41900 calcualted
59400
1 * 59400, calculated, 1 * 60000, SDS-PAGE
60000
1 * 59400, calculated, 1 * 60000, SDS-PAGE
64000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 41900 calcualted
monomer
1 * 59400, calculated, 1 * 60000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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