Information on EC 2.1.1.125 - histone-arginine N-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.125
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
RECOMMENDED NAME
GeneOntology No.
histone-arginine N-methyltransferase
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
250
cold shock protein-RXR
Rattus norvegicus
-
at pH 8.0 and 30°C
42148
0.61
eIF4A1
Homo sapiens
-
-
78505
0.17
eIF4A1-S
Homo sapiens
-
-
78507
0.08
eIF4A1-Y
Homo sapiens
-
-
78506
0.17
FYSGFNSKPRGRVYATSWY
Rattus norvegicus
-
at pH 8.0 and 30°C
42153
2.2
FYSGFNSRAKGRVYATSWY
Rattus norvegicus
-
at pH 8.0 and 30°C
42159
3.6
FYSGFNSRARGRVYATSWY
Rattus norvegicus
-
at pH 8.0 and 30°C
42158
12
FYSGFNSRGKGRVYATSWY
Rattus norvegicus
-
at pH 8.0 and 30°C
42157
19
FYSGFNSRGRGRVYATSWY
Rattus norvegicus
-
at pH 8.0 and 30°C
42156
0.15 - 7.4
FYSGFNSRPAGRVYATSWY
19659
0.14
FYSGFNSRPKGRVYATSWY
Rattus norvegicus
-
at pH 8.0 and 30°C
42152
0.54
FYSGFNSRPRGAVYATSVY
Rattus norvegicus
-
at pH 8.0 and 30°C
42154
12
FYSGFNSRPRGKVYATSVY
Rattus norvegicus
-
at pH 8.0 and 30°C
42155
20
FYSGFNSRPRGRVYATSWY
Rattus norvegicus
-
at pH 8.0 and 30°C
42151
21
GGRGGFGARGGFGGRGGFG
Rattus norvegicus
-
at pH 8.0 and 30°C
42150
4.3
GGRGGFGGRGGFGGRGGFG
Rattus norvegicus
-
at pH 8.0 and 30°C
10114
49
GGRGGFGPRGGFGGRGGFG
Rattus norvegicus
-
at pH 8.0 and 30°C
42149
0.934
histone H4 peptide PfH4-21-arginine
Plasmodium falciparum
-
pH 7.5, 37°C
40033
5
histone H4-arginine
Rattus norvegicus
-
at 30°C and pH 8.0
42160
0.013 - 4.5
N-acetyl-GGRGGFGGRGGFGGRGGFGG
8944
6.6
N-acetyl-SFRGKGGKGLGKGGAKRHRKV
Homo sapiens
-
isoform PRMT1, pH and temperature not specified in the publication
10362
2.17
N-acetyl-SGmeRGKGGKGLGKGGAKRHRKV
Homo sapiens
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
42144
14.3
N-acetyl-SGRGKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK
Rattus norvegicus
-
at 30°C and pH 8.0
42162
21.2
N-acetyl-SGRGKGGKGLGKGGAKRHRK
Rattus norvegicus
-
at 30°C and pH 8.0
42161
0.48 - 7.3
N-acetyl-SGRGKGGKGLGKGGAKRHRKV
7933
9.9
N-acetyl-SGRGRGGKGLGKGGAKRHRKV
Homo sapiens
-
isoform PRMT1, pH and temperature not specified in the publication
28720
26.7
N-acetyl-SGRme1GKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK
Rattus norvegicus
-
at 30°C and pH 8.0
42163
270
nuclear poly(A)-binding protein 1-arginine
Rattus norvegicus
-
at pH 8.0 and 30°C
42147
2.5 - 3.5
S-adenosyl-L-methionine
24
0.15
WGGYSmeRGGYGGW
Homo sapiens
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
42146
0.061
WGGYSRGGYGGW
Homo sapiens
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
42145
additional information
additional information
Homo sapiens
-
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; 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
2
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
-
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
-
overall PRMT2 expression is upregulated in breast cancer tissues; overall PRMT2 expression is upregulated in breast cancer tissues
-
PRMT1 expression is upregulated in the intestine during metamorphosis
-
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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