Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
additional information
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hernando, C.E.; Sanchez, S.E.; Mancini, E.; Yanovsky, M.J.
Genome wide comparative analysis of the effects of PRMT5 and PRMT4/CARM1 arginine methyltransferases on the Arabidopsis thaliana transcriptome
BMC Genomics
16
192
2015
Arabidopsis thaliana (Q9MAT5)
brenda
Fisk, J.C.; Zurita-Lopez, C.; Sayegh, J.; Tomasello, D.L.; Clarke, S.G.; Read, L.K.
TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma brucei
Eukaryot. Cell
9
866-877
2010
Trypanosoma brucei (Q57U70), Trypanosoma brucei, Trypanosoma brucei 927/4 GUTat10.1 (Q57U70)
brenda
Tsai, Y.J.; Pan, H.; Hung, C.M.; Hou, P.T.; Li, Y.C.; Lee, Y.J.; Shen, Y.T.; Wu, T.T.; Li, C.
The predominant protein arginine methyltransferase PRMT1 is critical for zebrafish convergence and extension during gastrulation
FEBS J.
278
905-917
2011
Danio rerio, Danio rerio (Q803D9)
brenda
Tang, J.; Gary, J.D.; Clarke, S.; Herschman, H.R.
PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
J. Biol. Chem.
273
16935-16945
1998
Rattus norvegicus (O70467)
brenda
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)
brenda
Tang, J.; Frankel, A.; Cook, R.J.; Kim, S.; Paik, W.K.; Williams, K.R.; Clarke, S.; Herschman, H.R.
PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells
J. Biol. Chem.
275
7723-7730
2000
Rattus norvegicus (Q63009)
brenda
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, Homo sapiens (Q96LA8)
brenda
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, Homo sapiens (Q9NR22)
brenda
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)
brenda
Gupta, N.; Madapura, M.P.; Bhat, U.A.; Rao, M.R.
Mapping of post-translational modifications of transition proteins, TP1 and TP2, and identification of protein arginine methyltransferase 4 and lysine methyltransferase 7 as methyltransferase for TP2
J. Biol. Chem.
290
12101-12122
2015
Rattus norvegicus (A0A068FP44)
brenda
Pelletier, M.; Pasternack, D.A.; Read, L.K.
In vitro and in vivo analysis of the major type I protein arginine methyltransferase from Trypanosoma brucei
Mol. Biochem. Parasitol.
144
206-217
2005
Trypanosoma brucei (Q4GYA9), Trypanosoma brucei, Trypanosoma brucei 927/4 GUTat10.1 (Q4GYA9)
brenda
Cha, B.; Park, Y.; Hwang, B.N.; Kim, S.Y.; Jho, E.H.
Protein arginine methyltransferase 1 methylates Smurf2
Mol. Cells
38
723-728
2015
Mus musculus
brenda
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, Homo sapiens (Q86X55), Homo sapiens (Q99873)
brenda
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)
brenda