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Information on EC 2.1.1.125 - histone-arginine N-methyltransferase and Organism(s) Homo sapiens and UniProt Accession O14744

for references in articles please use BRENDA:EC2.1.1.125
deleted. Now covered by EC 2.1.1.319, type I protein arginine methyltransferase, 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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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.125 histone-arginine N-methyltransferase
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61
eIF4A1
-
-
-
0.17
eIF4A1-S
-
-
-
0.08
eIF4A1-Y
-
-
-
6.6
N-acetyl-SFRGKGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
2.17
N-acetyl-SGmeRGKGGKGLGKGGAKRHRKV
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
0.48 - 7.3
N-acetyl-SGRGKGGKGLGKGGAKRHRKV
9.9
N-acetyl-SGRGRGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
0.15
WGGYSmeRGGYGGW
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
0.061
WGGYSRGGYGGW
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
additional information
additional information
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Michaelis-Menten kinetics, kcat/Km for S-adenosyl-L-methionine is almost 2000fold higher for PRMT1 than for PRMT2, and the kcat/Km for histone H4 is nearly 600fold higher
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
construction of PRMT1 and CARM1 single and double knockouts in siRNA-treated HeLa cells, the mutations affect the expression of diverse other genes, expression analysis and phenotypes, overview
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in vivo PRMT5 overexpression is caused by the altered expression of the PRMT5-specific microRNAs 19a, 25, 32, 92, 92b, and 96 and results in the increased global symmetric methylation of H3R8 and H4R3
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overall PRMT2 expression is upregulated in breast cancer tissues
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through its interaction with the estrogen receptoralpha, peroxisome proliferator-activated receptor, progesterone receptor, and the retinoic acid receptor, PRMT2 shows a ligand-dependent increase in transcriptional activity
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