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Information on EC 2.1.1.320 - type II protein arginine methyltransferase
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EC Tree
2.1.1.320 type II protein arginine methyltransferaseIUBMB Comments
The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I 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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Word Map
- 2.1.1.320
- histone
- methyltransferases
- chromatin
-
prmts
- dimethylarginine
- tumorigenesis
-
h4r3me2s
-
monomethylation
-
spliceosomal
- mep50
-
methylosome
- ribonucleoproteins
-
non-histone
- pre-mrna
-
snrnps
-
picln
-
monomethylarginine
- methylthioadenosine
-
tudor
-
menin
- protein-arginine
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
prmt5, prmt7, protein arginine methyltransferase 5, prmt9, type ii protein arginine methyltransferase, prmt-5, prmt-9, jak-binding protein 1, janus kinase-binding protein 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.1.1.124
-
-
formerly, part transferred
-
EC 2.1.1.125
-
-
formerly, part transferred
-
EC 2.1.1.126
-
-
formerly, part transferred
-
EC 2.1.1.23
-
-
formerly, part transferred
-
PRMT5
PRMT9
protein arginine methyltransferase 5
PRMT5
-
-
-
-
PRMT5
-
PRMT9
-
-
-
-
protein arginine methyltransferase 5
-
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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)
The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I 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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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 + [D2 dopamine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [D2 dopamine receptor]-Nomega,Nomega'-dimethyl-L-arginine
recombinant fragment of the third intracellular loop of D2, corresponding to amino acid residues 211 to 241 fused to glutathione S-transferase. Residues Arg217 and Arg219 are key methylation sites within this region
-
-
?
2 S-adenosyl-L-methionine + [DOP-3 receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [DOP-3 receptor]-Nomega,Nomega'-dimethyl-L-arginine
recombinant fragment of the third intracellular loop of Caenorhabditis elegans DOP-3, amino acid residues 202 to 232 fused to GST. Residues Arg208 and Arg210 are key methylation sites within this region
-
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Vasa]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [golgin GM130]-L-arginine
2 S-adenosyl-L-homocysteine + [golgin GM130]-Nomega,Nomega'-dimethyl-L-arginine
-
overall reaction
-
?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [histone H3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3]-Nomega,Nomega'-dimethyl-L-arginine
-
isoform PRMT5 bound to nuclear protein COPR5 methylates histone histone H3 at residue R8. Methylation of histone H4 is preferred over histone H3
-
?
2 S-adenosyl-L-methionine + [histone H4 peptide]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4 peptide]-Nomega,Nomega'-dimethyl-L-arginine
-
both PRMT5 alone and PRMT5 in complex with MEP50 are able to generate di-methylated H4 peptide product. The PRMT5:MEP50 complex consistently has a higher level of methyltransferase activity compared with PRMT5
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [histone H4]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [KRAB-associated protein 1]-L-arginine
2 S-adenosyl-L-homocysteine + [KRAB-associated protein 1]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [SER-2 tyramine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [SER-2 tyramine receptor]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [SmD3 protein]-L-arginine
2 S-adenosyl-L-homocysteine + [SmD3 protein]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [voltage-gated sodium channel NaV1.5]-L-arginine
2 S-adenosyl-L-homocysteine + [voltage-gated sodium channel NaV1.5]-Nomega,Nomega'-dimethyl-L-arginine
S-adenosyl-L-methionine + [GST-fibrillarin]-L-arginine
S-adenosyl-L-homocysteine + [GST-fibrillarin]-Nomega-methyl-L-arginine
substrate is amino terminus of fibrillarin fused to glutathione S-transferase
-
-
?
S-adenosyl-L-methionine + [GST-fibrillarin]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-fibrillarin]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [GST-GAR]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR]-Nomega-methyl-L-arginine
-
-
-
-
?
S-adenosyl-L-methionine + [GST-GAR]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
-
?
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-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 + [histone]-L-arginine
S-adenosyl-L-homocysteine + [histone]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [myelin basic protein]-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [myelin basic protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega,Nomega'-dimethyl-L-arginine
S-adenosyl-L-methionine + [nucleoplasmin]-L-arginine
S-adenosyl-L-homocysteine + [nucleoplasmin]-Nomega-methyl-L-arginine
-
nucleoplasmin is a potent substrate and is monomethylated and symmetrically dimethylated at Arg187
-
?
S-adenosyl-L-methionine + [nucleoplasmin]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [nucleoplasmin]-Nomega,Nomega'-dimethyl-L-arginine
-
nucleoplasmin is a potent substrate and is monomethylated and symmetrically dimethylated at Arg187
-
?
S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega-methyl-L-arginine
the enzyme methylates the R508 residue
-
-
?
S-adenosyl-L-methionine + [splicing factor SF3B2]-Nomega-L-arginine
S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme methylates the R508 residue
-
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Vasa]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Vasa]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
seven arginine residues in Vasa, including R101, R105, R177, R179, R183, R197 and R201, and two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Vasa mutant with seven arginines to lysines (Vasa-7M: R101K, R105K, R177K, R179K, R183K, R197K and R201K) can not be dimethylated by Prmt5
-
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Zili mutant with two arginines to lysines [Zili (1-133aa)-R68/221K] can not be dimethylated by Prmt5
-
-
?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code
-
-
?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code
-
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) affects the levels of symmetric dimethylarginine at Arg3 on histone H4, leading to the repression of genes which are related to disease progression in lymphoma and leukemia. PRMT7-mediated monomethylation of histone H4 Arg17 regulates PRMT5 activity at Arg3 in the same protein
-
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code
-
-
?
2 S-adenosyl-L-methionine + [histone H4]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
-
enzyme specifically methylates histone H4 Arg3 to form symmetric dimethylarginines. In addition, it is annotated for formation of omega-N monomethylarginine, reaction of EC 2.1.1.321
-
?
2 S-adenosyl-L-methionine + [histone H4]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
-
PRMT5 alone methylates both histone H4 and SmD3 proteins while PRMT5 complexed with p44 and pICln methylates SmD3 but not histone H4
-
?
2 S-adenosyl-L-methionine + [histone H4]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
-
isoform PRMT5 bound to nuclear protein COPR5 methylates histone H4 at residue R3 preferentially when compared with histone H3
-
?
2 S-adenosyl-L-methionine + [KRAB-associated protein 1]-L-arginine
2 S-adenosyl-L-homocysteine + [KRAB-associated protein 1]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [KRAB-associated protein 1]-L-arginine
2 S-adenosyl-L-homocysteine + [KRAB-associated protein 1]-Nomega,Nomega'-dimethyl-L-arginine
methylation of KRAB-associated protein 1 (KAP1) arginine residues regulates the KAP1-ZNF224 interaction, thus suggesting that this KAP1 post-translational modification can actively contribute to the regulation of ZNF224-mediated repression
-
-
?
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [SER-2 tyramine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [SER-2 tyramine receptor]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [SER-2 tyramine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [SER-2 tyramine receptor]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT-5) regulates SER-2 tyramine receptor-mediated behaviors in Caenorhabditis elegans
-
-
?
2 S-adenosyl-L-methionine + [SmD3 protein]-L-arginine
2 S-adenosyl-L-homocysteine + [SmD3 protein]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [SmD3 protein]-L-arginine
2 S-adenosyl-L-homocysteine + [SmD3 protein]-Nomega,Nomega'-dimethyl-L-arginine
-
PRMT5 alone methylates both histone H4 and SmD3 proteins while PRMT5 complexed with p44 and pICln methylates SmD3 but not histone H4
-
?
2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme methylates the R508 residue
-
-
?
2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
-
overall reaction, isoform PRMT9 symmetrically dimethylates arginine residues on splicing factor SF3B2. A peptide containing the methylatable Arg508 of SF3B2 is not recognized by PRMT9 in vitro. Amino acid substitutions of residues surrounding Arg508 have no great effect on PRMT9 recognition of SF3B2, but moving the arginine residue within this sequence abolishes methylation
-
?
2 S-adenosyl-L-methionine + [voltage-gated sodium channel NaV1.5]-L-arginine
2 S-adenosyl-L-homocysteine + [voltage-gated sodium channel NaV1.5]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [voltage-gated sodium channel NaV1.5]-L-arginine
2 S-adenosyl-L-homocysteine + [voltage-gated sodium channel NaV1.5]-Nomega,Nomega'-dimethyl-L-arginine
PRMT5, along with PRMT3, binds to and methylate the voltage-gated sodium channel NaV1.5
-
-
?
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
-
-
-
-
?
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
histone H2A from calf thymus
-
-
?
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
-
?
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
-
symmetric dimethylation is only observed when enzyme and the methyl-accepting substrate are incubated for extended times
-
?
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [myelin basic protein]-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
-
-
-
-
?
S-adenosyl-L-methionine + [myelin basic protein]-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [myelin basic protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [myelin basic protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega,Nomega'-dimethyl-L-arginine
-
-
methylation leads to omega-NG-monomethylarginine and and symmetric omega-NG,NG-dimethylarginine residues, no formation of asymmetric dimethylarginine residues
-
?
additional information
?
-
myelin basic protein methylated by PRMT5 contains monomethylated and dimethylated arginine residues
-
-
?
additional information
?
-
-
myelin basic protein methylated by PRMT5 contains monomethylated and dimethylated arginine residues
-
-
?
additional information
?
-
isoform PRMT9 poorly methylates PRMT5 substrate GST-GAR
-
-
?
additional information
?
-
-
isoform PRMT9 poorly methylates PRMT5 substrate GST-GAR
-
-
?
additional information
?
-
PRMT5 alone methylates both histone H4 and SmD3 proteins while PRMT5 complexed with p44 and pICln methylates SmD3 but not histone H4
-
-
?
additional information
?
-
PRMT5 has a nonprocessive enzymatic mechanism for peptide substrates
-
-
?
additional information
?
-
-
PRMT5 has a nonprocessive enzymatic mechanism for peptide substrates
-
-
?
additional information
?
-
isoform Hsl7 has little or no activity on common substrate GST-GAR, and only minimal activity on myelin basic protein. Enzyme additionally shows type III protein arginine methyltransferase activity, EC 2.1.1.321
-
-
?
additional information
?
-
-
isoform Hsl7 has little or no activity on common substrate GST-GAR, and only minimal activity on myelin basic protein. Enzyme additionally shows type III protein arginine methyltransferase activity, EC 2.1.1.321
-
-
?
additional information
?
-
a complex of the protein arginine methyltransferase Prmt5 and the methylosome protein Mep50 isolated from Xenopus eggs specifically methylates predeposition histones H2A/H2A.X-F and H4 and the histone chaperone nucleoplasmin on a conserved motif GRGXK
-
-
?
additional information
?
-
-
a complex of the protein arginine methyltransferase Prmt5 and the methylosome protein Mep50 isolated from Xenopus eggs specifically methylates predeposition histones H2A/H2A.X-F and H4 and the histone chaperone nucleoplasmin on a conserved motif GRGXK
-
-
?
additional information
?
-
PRMT5-MEP50 activity is inhibited by substrate phosphorylation and enhanced by substrate acetylation
-
-
?
additional information
?
-
-
PRMT5-MEP50 activity is inhibited by substrate phosphorylation and enhanced by substrate acetylation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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 + [germ cell-specific protein Vasa]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Vasa]-Nomega,Nomega'-dimethyl-L-arginine
seven arginine residues in Vasa, including R101, R105, R177, R179, R183, R197 and R201, and two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Vasa mutant with seven arginines to lysines (Vasa-7M: R101K, R105K, R177K, R179K, R183K, R197K and R201K) can not be dimethylated by Prmt5
-
-
?
2 S-adenosyl-L-methionine + [germ cell-specific protein Zili]-L-arginine
2 S-adenosyl-L-homocysteine + [germ cell-specific protein Zili]-Nomega,Nomega'-dimethyl-L-arginine
two arginine residues in Zili, including R68 and R221, are dimethylated in vivo. Zili mutant with two arginines to lysines [Zili (1-133aa)-R68/221K] can not be dimethylated by Prmt5
-
-
?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
2 S-adenosyl-L-methionine + [KRAB-associated protein 1]-L-arginine
2 S-adenosyl-L-homocysteine + [KRAB-associated protein 1]-Nomega,Nomega'-dimethyl-L-arginine
methylation of KRAB-associated protein 1 (KAP1) arginine residues regulates the KAP1-ZNF224 interaction, thus suggesting that this KAP1 post-translational modification can actively contribute to the regulation of ZNF224-mediated repression
-
-
?
2 S-adenosyl-L-methionine + [SER-2 tyramine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [SER-2 tyramine receptor]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT-5) regulates SER-2 tyramine receptor-mediated behaviors in Caenorhabditis elegans
-
-
?
2 S-adenosyl-L-methionine + [SmD3 protein]-L-arginine
2 S-adenosyl-L-homocysteine + [SmD3 protein]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [voltage-gated sodium channel NaV1.5]-L-arginine
2 S-adenosyl-L-homocysteine + [voltage-gated sodium channel NaV1.5]-Nomega,Nomega'-dimethyl-L-arginine
PRMT5, along with PRMT3, binds to and methylate the voltage-gated sodium channel NaV1.5
-
-
?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code
-
-
?
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H3R8]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R8]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code
-
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) affects the levels of symmetric dimethylarginine at Arg3 on histone H4, leading to the repression of genes which are related to disease progression in lymphoma and leukemia. PRMT7-mediated monomethylation of histone H4 Arg17 regulates PRMT5 activity at Arg3 in the same protein
-
-
?
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega'-dimethyl-L-arginine
the enzyme (PRMT5) catalyse the formation of either activating H3R2me2s or repressive H3R8me2s and H4R3me2s marks as a part of epigenetic histone code
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2S,3R,5R)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(E)-2-(quinolin-7-yl)ethenyl]cyclopentane-1,2-diol
-
(1R,2S,3R,5R)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(S)-(3,4-difluorophenyl)(hydroxy)methyl]cyclopentane-1,2-diol
-
(1R,2S,3R,5R)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[[(quinolin-7-yl)oxy]methyl]cyclopentane-1,2-diol
-
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-(2-[2-[(cyclopropylmethyl)amino]quinolin-7-yl]ethyl)cyclopentane-1,2-diol
-
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(2,3-dimethylimidazo[1,2-a]pyridin-7-yl)ethyl]cyclopentane-1,2-diol
-
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(2-aminoquinolin-7-yl)ethyl]cyclopentane-1,2-diol
-
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(3-methylimidazo[1,2-a]pyridin-7-yl)ethyl]cyclopentane-1,2-diol
-
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(6-chloro-3-methylimidazo[1,2-a]pyridin-7-yl)ethyl]cyclopentane-1,2-diol
-
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(6-fluoro-3-methylimidazo[1,2-a]pyridin-7-yl)ethyl]cyclopentane-1,2-diol
-
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(quinolin-7-yl)ethyl]cyclopentane-1,2-diol
-
(1S,2R,3R,5R)-3-[(R)-hydroxy(1,2,3,4-tetrahydroisoquinolin-8-yl)methyl]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(1S,2R,3S,5R)-3-[2-(2-amino-3-bromoquinolin-7-yl)ethyl]-5-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(1S,2R,3S,5R)-3-[2-(6-aminopyridin-3-yl)ethyl]-5-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(1S,2R,3S,5R)-3-[4-(6-aminopyridin-2-yl)butyl]-5-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(1S,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(4-chloro-3-fluorophenyl)sulfanyl]cyclopentane-1,2-diol
-
(1S,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(quinolin-7-yl)methoxy]cyclopentane-1,2-diol
-
(1S,2S,3R,5S)-3-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(1,2,3,4-tetrahydroisoquinolin-8-yl)oxy]cyclopentane-1,2-diol
-
(1S,2S,3R,5S)-3-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[[6-(trifluoromethyl)-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]cyclopentane-1,2-diol
-
(1S,2S,3S,5R)-3-[(5-fluoro-6-methoxy-1,2,3,4-tetrahydroisoquinolin-8-yl)oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(1S,2S,3S,5R)-3-[(6-bromo-1,2,3,4-tetrahydroisoquinolin-8-yl)oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(1S,2S,3S,5R)-3-[[6-(difluoromethoxy)-5-fluoro-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(1S,2S,3S,5R)-3-[[6-(difluoromethyl)-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(1S,2S,3S,5R)-3-[[6-(difluoromethyl)-5-fluoro-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(1S,2S,3S,5R)-3-[[6-(difluoromethyl)-5-fluoro-4-methyl-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
-
(2R,3S,4R,5R)-2-[(S)-hydroxy(1,2,3,4-tetrahydroisoquinolin-8-yl)methyl]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)oxolane-3,4-diol
-
(4Z)-7-[(5R)-5-amino-5-(4-chlorophenyl)-5-deoxy-beta-D-ribofuranosyl]-4-hydrazinylidene-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine
-
1-(6-bromo-9-ethyl-9H-carbazol-3-yl)-N-[(2-methoxyphenyl)methyl]methanamine
-
1-[(5R)-5-C-(4-chlorophenyl)-beta-D-ribofuranosyl]-3-ethynyl-1H-pyrazolo[3,4-d]pyrimidin-4-amine
-
2-([[2-(benzyloxy)-1,4-dihydronaphthalen-1-yl]methyl]amino)-1-phenylethan-1-ol
-
3-(3,4-dihydroisoquinolin-2(1H)-yl)-N-[3-(trifluoromethoxy)phenyl]propanamide
-
3-(3,4-dihydroisoquinolin-2(1H)-yl)-N-[4-(trifluoromethyl)pyrimidin-2-yl]propanamide
-
7-[(5R)-5-amino-5-deoxy-5-(3,4-difluorophenyl)-beta-D-ribofuranosyl]-4-methyl-7H-pyrrolo[2,3-d]pyrimidine
-
7-[(5R)-5-C-(3,4-difluorophenyl)-beta-D-ribofuranosyl]-4-methyl-7H-pyrrolo[2,3-d]pyrimidine
-
7-[(5R)-5-C-(3,4-difluorophenyl)-beta-D-ribofuranosyl]-5-fluoro-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
7-[(5R)-5-C-(3,4-difluorophenyl)-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
7-[(5R)-5-C-(4-chloro-3-fluorophenyl)-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
7-[(5R)-5-C-(4-chlorophenyl)-beta-D-ribofuranosyl]-5-ethynyl-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
7-[(5R)-5-C-(4-chlorophenyl)-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
7-[(5R)-5-C-phenyl-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
7-[5-O-(quinolin-7-yl)-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
8-[[(1S,2S,3S,4R)-2,3-dihydroxy-4-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentyl]oxy]-1,2,3,4-tetrahydroisoquinoline-6-carbonitrile
-
GSK3326595
substrate competitive inhibitor, clinic trials for multiple cancer types
methyl 2-[2-[(6-methoxy-1H-benzimidazol-2-yl)sulfanyl]acetamido]benzoate
-
N-(3-bromo-2-cyanophenyl)-3-(3,4-dihydroisoquinolin-2(1H)-yl)propanamide
-
N-[(2S)-3-(3,4-dihydro-2(1H)-isoquinolinyl)-2-hydroxypropyl]-6-(3-oxetanylamino)-4-pyrimidinecarboxamide
i.e. EPZ015666
N-[(2S)-3-(3,4-dihydroisoquinolin-2(1H)-yl)-2-hydroxypropyl]-6-[(oxetan-3-yl)amino]pyrimidine-4-carboxamide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
PRMT7
PRMT7-mediated monomethylation of histone H4 Arg17 regulates PRMT5 activity at Arg3 in the same protein. Monomethylation at Arg-17 in histone H4 raises the general activity of PRMT5 with this substrate, but also ameliorates the low activity of PRMT5 at low substrate concentrations
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000022
S-adenosyl-L-methionine
isoform PRMT5, presence of 0.001 mM histone H4 peptide, 22°C, pH not specified in the publication
0.001
S-adenosyl-L-methionine
isoform PRMT5 in complex with MEP50, presence of 0.001 mM histone H4 peptide, 22°C, pH not specified in the publication
0.0042
[histone H4 peptide]-L-arginine
isoform PRMT5, presence of 0.01 mM S-adenosyl-L-methionine, 22°C, pH not specified in the publication
-
0.0102
[histone H4 peptide]-L-arginine
isoform PRMT5 in complex with MEP50,presence of 0.01 mM S-adenosyl-L-methionine, 22°C, pH not specified in the publication
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000079
(1R,2S,3R,5R)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(E)-2-(quinolin-7-yl)ethenyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000002
(1R,2S,3R,5R)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(S)-(3,4-difluorophenyl)(hydroxy)methyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000026
(1R,2S,3R,5R)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[[(quinolin-7-yl)oxy]methyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.00000079
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-(2-[2-[(cyclopropylmethyl)amino]quinolin-7-yl]ethyl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.0000002
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(2,3-dimethylimidazo[1,2-a]pyridin-7-yl)ethyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.00000025
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(2-aminoquinolin-7-yl)ethyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000008
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(3-methylimidazo[1,2-a]pyridin-7-yl)ethyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.0000016
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(6-chloro-3-methylimidazo[1,2-a]pyridin-7-yl)ethyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.00000032
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(6-fluoro-3-methylimidazo[1,2-a]pyridin-7-yl)ethyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.0000063
(1R,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[2-(quinolin-7-yl)ethyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000002
(1S,2R,3R,5R)-3-[(R)-hydroxy(1,2,3,4-tetrahydroisoquinolin-8-yl)methyl]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.00000013
(1S,2R,3S,5R)-3-[2-(2-amino-3-bromoquinolin-7-yl)ethyl]-5-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000000501
(1S,2R,3S,5R)-3-[2-(6-aminopyridin-3-yl)ethyl]-5-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.0000004
(1S,2R,3S,5R)-3-[4-(6-aminopyridin-2-yl)butyl]-5-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000026
(1S,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(4-chloro-3-fluorophenyl)sulfanyl]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000126
(1S,2S,3R,5S)-3-(4-amino-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(quinolin-7-yl)methoxy]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000001
(1S,2S,3R,5S)-3-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[(1,2,3,4-tetrahydroisoquinolin-8-yl)oxy]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000002
(1S,2S,3R,5S)-3-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-5-[[6-(trifluoromethyl)-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000001
(1S,2S,3S,5R)-3-[(5-fluoro-6-methoxy-1,2,3,4-tetrahydroisoquinolin-8-yl)oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000001
(1S,2S,3S,5R)-3-[(6-bromo-1,2,3,4-tetrahydroisoquinolin-8-yl)oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000001
(1S,2S,3S,5R)-3-[[6-(difluoromethoxy)-5-fluoro-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000001
(1S,2S,3S,5R)-3-[[6-(difluoromethyl)-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000001
(1S,2S,3S,5R)-3-[[6-(difluoromethyl)-5-fluoro-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000001
(1S,2S,3S,5R)-3-[[6-(difluoromethyl)-5-fluoro-4-methyl-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000001
(2R,3S,4R,5R)-2-[(S)-hydroxy(1,2,3,4-tetrahydroisoquinolin-8-yl)methyl]-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)oxolane-3,4-diol
Homo sapiens
pH and temperature not specified in the publication
0.0000006
(4Z)-7-[(5R)-5-amino-5-(4-chlorophenyl)-5-deoxy-beta-D-ribofuranosyl]-4-hydrazinylidene-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine
Homo sapiens
pH and temperature not specified in the publication
0.000003
(5R)-5'-C-(3,4-difluorophenyl)adenosine
Homo sapiens
pH and temperature not specified in the publication
0.000517
1-(6-bromo-9-ethyl-9H-carbazol-3-yl)-N-[(2-methoxyphenyl)methyl]methanamine
Homo sapiens
pH and temperature not specified in the publication
0.000116
1-[(5R)-5-C-(4-chlorophenyl)-beta-D-ribofuranosyl]-3-ethynyl-1H-pyrazolo[3,4-d]pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.0028
2-([[2-(benzyloxy)-1,4-dihydronaphthalen-1-yl]methyl]amino)-1-phenylethan-1-ol
Homo sapiens
pH and temperature not specified in the publication
0.04587
3-(3,4-dihydroisoquinolin-2(1H)-yl)-N-(3-fluorophenyl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.06295
3-(3,4-dihydroisoquinolin-2(1H)-yl)-N-[3-(trifluoromethoxy)phenyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.06987
3-(3,4-dihydroisoquinolin-2(1H)-yl)-N-[4-(trifluoromethyl)pyrimidin-2-yl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.000009
7-[(5R)-5-amino-5-deoxy-5-(3,4-difluorophenyl)-beta-D-ribofuranosyl]-4-methyl-7H-pyrrolo[2,3-d]pyrimidine
Homo sapiens
pH and temperature not specified in the publication
0.000003
7-[(5R)-5-C-(3,4-difluorophenyl)-beta-D-ribofuranosyl]-4-methyl-7H-pyrrolo[2,3-d]pyrimidine
Homo sapiens
pH and temperature not specified in the publication
0.000002
7-[(5R)-5-C-(3,4-difluorophenyl)-beta-D-ribofuranosyl]-5-fluoro-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.000001
7-[(5R)-5-C-(3,4-difluorophenyl)-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.00000002
7-[(5R)-5-C-(4-chloro-3-fluorophenyl)-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.000017
7-[(5R)-5-C-(4-chlorophenyl)-beta-D-ribofuranosyl]-5-ethynyl-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.0000043
7-[(5R)-5-C-(4-chlorophenyl)-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.0000095 - 0.000026
7-[(5R)-5-C-phenyl-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
0.0000158
7-[5-O-(quinolin-7-yl)-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
0.000001
8-[[(1S,2S,3S,4R)-2,3-dihydroxy-4-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentyl]oxy]-1,2,3,4-tetrahydroisoquinoline-6-carbonitrile
Homo sapiens
pH and temperature not specified in the publication
0.000035
dehydrosinefungin
Homo sapiens
pH and temperature not specified in the publication
0.06
methyl 2-[2-(3,4-dihydroisoquinolin-2(1H)-yl)acetamido]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.00033
methyl 2-[2-[(6-methoxy-1H-benzimidazol-2-yl)sulfanyl]acetamido]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.03162
methyl 2-[3-(3,4-dihydroisoquinolin-2(1H)-yl)propanamido]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.08789
methyl 2-[4-(3,4-dihydroisoquinolin-2(1H)-yl)butanamido]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.07254
N'-[3-(3,4-dihydroisoquinolin-2(1H)-yl)propanoyl]benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.02555
N-(2-cyanophenyl)-3-(3,4-dihydroisoquinolin-2(1H)-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.05195
N-(3-acetylphenyl)-3-(3,4-dihydroisoquinolin-2(1H)-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.00271
N-(3-bromo-2-cyanophenyl)-3-(3,4-dihydroisoquinolin-2(1H)-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.01812
N-(3-bromophenyl)-3-(3,4-dihydroisoquinolin-2(1H)-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.04213
N-(3-chlorophenyl)-3-(3,4-dihydroisoquinolin-2(1H)-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.000047
N-[(2S)-3-(3,4-dihydro-2(1H)-isoquinolinyl)-2-hydroxypropyl]-6-(3-oxetanylamino)-4-pyrimidinecarboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000022
N-[(2S)-3-(3,4-dihydroisoquinolin-2(1H)-yl)-2-hydroxypropyl]-6-[(oxetan-3-yl)amino]pyrimidine-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00056
S-adenosyl-L-homocysteine
Homo sapiens
pH and temperature not specified in the publication
0.0000095
7-[(5R)-5-C-phenyl-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Homo sapiens
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PRMT5 expression gradually increases throughout postnatal brain development, coinciding with the period of active myelination
brenda
histone H2A and nucleoplasmin methylation appears late in oogenesis and is most abundant in the laid egg
brenda
-
isoform PRMT5 is abundantly expressed in the germ cells of both male and female gonads
brenda
PRMT5 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
brenda
additional information
Prmt7 transcripts and protein are maternally deposited and ubiquitously expressed through gastrulation
brenda
the enzyme (PRMT5) is localized in the cytoplasm in the tachyzoite stage. It shifts largely to the nuclear compartment in the bradyzoite stage
brenda
-
the enzyme (PRMT5) is localized in the cytoplasm in the tachyzoite stage. It shifts largely to the nuclear compartment in the bradyzoite stage
-
brenda
the enzyme (PRMT5) is localized in the cytoplasm in the tachyzoite stage. It shifts largely to the nuclear compartment in the bradyzoite stage
brenda
-
the enzyme (PRMT5) is localized in the cytoplasm in the tachyzoite stage. It shifts largely to the nuclear compartment in the bradyzoite stage
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PRMT5 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
brenda
coexpression of candidate tumor suppressor gene RASSF1A and PRMT5 leads to a redistribution of PRMT5 from the cytosol to stabilized microtubules
brenda
additional information
high levels of cytoplasmic PRMT5 are detected in 20.5% of non-small cell lung carcinomas and in 16.5% of pulmonary neuroendocrine tumors
brenda
isoform PRMT5 and p44/MED50/WD45/WDR77 colocalize in the cytoplasm, and both are required for the growth of prostate cancer cells in an PRMT5 methyltransferase activity-dependent manner
brenda
PRMT5 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
brenda
isoform PRMT5 localizes to the Golgi apparatus and forms complexes with several components involved in Golgi apparatus ribbon formation and vesicle tethering. PRMT5 interacts with the golgin GM130
brenda
original isoform PRMT5L mainly colocalizes with Giantin, a Golgi marker
brenda
high levels of nuclear PRMT5 are detected in 38.0% of non-small cell lung carcinomas and 24.0% of pulmonary neuroendocrine tumors
brenda
isoform PRMT5 in the nucleus inhibits cell growth in a methyltransferase activity-independent manner
brenda
additional information
evolutionarily emerged splice variant PRMT5S is distributed all over the cell. The isoforms are differentially expressed during neuronal or dendritic cell differentiation, and their ectopic expression shows an opposite effect on dendritic cell differentiation
-
brenda
additional information
-
evolutionarily emerged splice variant PRMT5S is distributed all over the cell. The isoforms are differentially expressed during neuronal or dendritic cell differentiation, and their ectopic expression shows an opposite effect on dendritic cell differentiation
-
brenda
additional information
presence of three nuclear exclusion signals in the PRMT5 protein
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
prmt5 loss in zebrafish leads to the expression of an infertile male phenotype due to a reduction in germ cell number, an increase in germ cell apoptosis and the failure of gonads to differentiate into normal testes or ovaries. Arginine methylation of the germ cell-specific proteins Zili and Vasa, as well as histones H3 (H3R8me2s) and H4 (H4R3me2s), is reduced in the gonads of prmt5-null zebrafish
physiological function
drug target
targeting PRMT5 offers a great opportunity to combat cancer in an efficient and selective way
drug target
the enzyme is a promising therapeutic target for human cancer
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 exhibited 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
at 10 hours post-fertilization, Prmt7 morphants display an epibolic delay defects phenotype compared with control embryos that have completed epiboly and entirely enclosed the yolk sphere. Both shape and orientation of enveloping layer cells in Prmt7 morphants are altered. In control embryos, enveloping layer cells are elongated and regularly aligned. Enveloping layer cells in Prmt7 morphants are mostly round, small, and irregularly aligned more disorganized and fail to align their cell bodies along the direction of epibolic movement
physiological function
both PRMT5 alone and PRMT5 in complex with MEP50 are able to generate di-methylated H4 peptide product. The PRMT5:MEP50 complex consistently has a higher level of methyltransferase activity compared with PRMT5
physiological function
Caenorhabditis elegans lacking PRMT-5 are hypersensitive to dilute octanol. PRMT-5 contributes to the regulation of locomotion by both exogenous and endogenous dopamine
physiological function
-
deletion of Prmt5 results in germ cell depletion in adult mice. Germ cell loss is first observed between embryonic days 12.5 and 13.5, and very few of these cells remain at birth. Oct4, Sox2, and Nanog are abundantly expressed in Prmt5-deficient germ cells, whereas their expression is dramatically decreased in control germ cells. The expression of meiosis-associated genes is virtually absent in Prmt5-deficient female germ cells at embryonic day 13.5 , whereas the expression of other germ cell-specific genes is not changed. Methylation of histine H4R3 is completely absent after Prmt5 inactivation, whereas the level of histone H3R2 is not changed
physiological function
inactivation of isoform Prmt5 in skeletal muscle stem cells of adult mice prevents expansion of skeletal muscle stem cells, abolishes long-term skeletal muscle stem cells maintenance and abrogates skeletal muscle regeneration. Prmt5 is dispensable for proliferation and differentiation of Pax7+ myogenic progenitor cells during mouse embryonic development. Prmt5 controls proliferation of adult skeletal muscle stem cells by direct epigenetic silencing of the cell cycle inhibitor p21
physiological function
isoform PRMT5 binds to a nuclear protein, called cooperator of PRMT5, i.e. COPR5. COPR5 modulates the substrate specificity of nuclear PRMT5-containing complexes, at least towards histones. Rcombinant COPR5 binds to the amino terminus of histone H4 and is required to recruit PRMT5 to reconstituted nucleosomes in vitro. COPR5 depletion in cells strongly reduces PRMT5 recruitment on chromatin at the PRMT5 target gene cyclin E1 in vivo
physiological function
isoform Prmt5 forms a complex with methylosome protein Mep50 that specifically methylates predeposition histones H2A/H2A.X-F and H4 and the histone chaperone nucleoplasmin on a conserved motif (GRGXK). Nucleoplasmin is a potent substrate for Prmt5-Mep50 and modulates Prmt5-Mep50 activity directed toward histones. Histone H2A and nucleoplasmin methylation appears late in oogenesis and is most abundant in the laid egg
physiological function
isoform PRMT5 interacts with candidate tumor suppressor gene RASSF1A. Coexpression of RASSF1A and PRMT5 leads to a redistribution of PRMT5 from the cytosol to stabilized microtubules, where RASSF1A and PRMT5 become colocalized. PRMT5 translocates to bundled microtubules on stabilization by RASSF1A expression
physiological function
isoform PRMT5 interacts with the golgin GM130, and depletion of PRMT5 causes defects in Golgi ribbon formation. PRMT5 methylates N-terminal arginine residues in GM130, and such arginine methylation appears critical for Golgi apparatus ribbon formation
physiological function
isoform PRMT5 is down-regulated by amyloid-beta in primary neurons and SH-SY5Y cells, and this is associated with the up-regulation of the PRMT5 target protein E2F-1. Knockdown of PRMT5 in SH-SY5Y cells over-expressing the Swedish mutant form of human amyloid-beta precursor protein causes activation of E2F-1/p53/Bax, NF-kappaB, and GSK-3beta pathways, which coincides with increased apoptosis. Co-depletion of E2F-1 reduces the activation of p53/Bax, NF-kappaB, and GSK-3beta, and limits cell apoptosis
physiological function
isoform PRMT5 knockdown leads to an enlarged Giantin pattern, which is prevented by the expression of either original isoform PRMT5L or evolutionary emerged splice variant PRMT5S. Rescuing PRMT5S also increases the percentage of cells with an interphase Giantin pattern compacted at one end of the nucleus, consistent with its cell cycle-arresting effect, while rescuing PRMT5L increases that of the mitotic Giantin patterns of dynamically fragmented structures. Both isoforms also similarly regulate over a thousand genes particularly those involved in apoptosis and differentiation
physiological function
knockdown of isoform PRMT5 results in a reduction in symmetric dimethyl arginine modifcation of the SM protein set of small nuclear ribonucleoproteins. A similar effect is observed when cells are treated with siRNAs targeting methylosome protein MEP50. Isoform PRMT7, EC 2.1.1.321, knockdown also causes a reduction in Sm protein symmetric dimethylarginine modification. Double depletion of both PRMT5 and PRMT7 does not disrupt the modification to a greater extent than either single depletion alone. PRMT7 is not able to restore symmetric dimethylarginine modification of the Sm proteins in cells that are depleted of PRMT5. Cytoplasmic small nuclear ribonucleoprotein assembly requires the activities of both PRMT5 and PRMT7, and Sm protein symmetric dimethylarginine modification is primarily required for cytoplasmic small nuclear ribonucleoprotein assembly
physiological function
knockdown of isoform PRMT5 results in more paralysis in a Caenorhabditis elegans model of Alzheimer's disease
physiological function
Loss of PRMT5 in conditional KO mice triggers an initial but transient expansion of hematopoietic stem cells. Prmt5 deletion results in a concurrent loss of hematopoietic progenitor cells, leading to fatal bone marrow aplasia. PRMT5-specific effects on hematopoiesis are cell intrinsic and depend on PRMT5 methyltransferase activity. PRMT5-deficient hematopoietic stem and progenitor cells exhibit severely impaired cytokine signaling as well as upregulation of p53 and expression of its downstream targets
physiological function
prmt5 mutants are impaired in light inhibition of hypocotyl elongation. Loss of PRMT5 function affects both the period and strength of expression of multiple clock genes
physiological function
-
siRNA-mediated depletion of PRMT5 primary oligodendrocyte progenitor cells abrogates oligodendrocyte differentiation. PRMT5-depleted oligodendrocyte progenitor and C6 glioma cells express high levels of the inhibitors of differentiation/DNA binding, Id2 and Id4, known repressors of glial cell differentiation. CpG-rich islands within the Id2 and Id4 genes are bound by PRMT5 and are hypomethylated in PRMT5-deficient cells
physiological function
epigenetic regulation by the type II protein arginine methyltransferase, PRMT5, plays an essential role in the control of cancer cell proliferation and tumorigenesis. PRMT5 governs expression of prosurvival genes by promoting WNT/beta-CATENIN and AKT/GSK3x02 proliferative signaling
physiological function
in stem cells, PRMT5 is only required for proliferation, and not pluripotency, through methylation of the cell cycle-regulated p57. In keratinocyte differentiation involucrin gene expression is partially controlled by PKC-delta suppression of PRMT5. In the human osteosarcoma cell line U2OS, PRMT5, Strap and p53 form a complex in response to DNA damage
physiological function
methylation of KRAB-associated protein 1 (KAP1) arginine residues regulates the KAP1-ZNF224 interaction, thus suggesting that this KAP1 post-translational modification can actively contribute to the regulation of ZNF224-mediated repression
physiological function
PRMT5 and PRMT1 are involved in the interaction between CFLARL (a CASP8 and FADD-like apoptosis regulator) and the E3 ligase ITCH. The PRMT5 silencing and PRMT1 overexpression enhance the interaction between CFLARL and ITCH, leading to an altered ubiquitination level and, eventually, the degradation of CFLARL
physiological function
PRMT5 expression, localization, and activity are altered following denervation-induced inactivity
physiological function
PRMT5 inhibition induces mouse primary lymphoma cell death through inactivation of AKT/GSK3x02 and WNT/beta-CATENIN proliferative signaling
physiological function
protein arginine methyltransferase 5 (Prmt5) symmetrically dimethylates arginine in nuclear and cytoplasmic proteins. Prmt5 is involved in a variety of cellular processes, including ribosome biogenesis, cellular differentiation, germ cell development and tumorigenesis
physiological function
the enzyme (PRMT-5) regulates SER-2 tyramine receptor-mediated behaviors in Caenorhabditis elegans
physiological function
the enzyme (PRMT-9) may play a regulatory role in nematode alternative RNA splicing
physiological function
the enzyme (PRMT5) is a major enzyme responsible for symmetric dimethylation of arginine residues on both histone and non-histone proteins, regulating many biological pathways in mammalian cells
physiological function
the enzyme (PRMT5) is essential for IFN-gamma induced, CIITA-dependent MHC II transactivation by promoting histone H3R2 methylation in macrophages. Over-expression of PRMT5 potentiates IFN-gamma induced activation of MHC II transcription in an enzyme activity-dependent manner. Pathophysiologically relevant role for PRMT5 in MHC II transactivation in macrophages
physiological function
the enzyme (PRMT5) is essential for IFN-gamma induced, CIITA-dependent MHC II transactivation by promoting histone H3R2 methylation in macrophages. Over-expression of PRMT5 potentiates IFN-gamma induced activation of MHC II transcription in an enzyme activity-dependent manner. Pathophysiologically relevant role for PRMT5 in MHC II transactivation in macrophages
physiological function
the enzyme (PRMT5) is involved in tumour initiation, progression, invasion, metastasis as well as poor prognosis in cancer. Increased expression of PRMT5-MEP50 is correlated with the growth of cancer cells
physiological function
the enzyme (PRMT5) may be involved in tachyzoite-bradyzoite transformation
physiological function
the protein arginine methyltransferases 1 and 5 affect Myc properties in glioblastoma stem cells. Myc associates with both PRMT1 and PRMT5 being differentially dimethylated. Symmetric (S) by PRMT1 dimethylation protects Myc from degradation, while asymmetric (AS) dimethylation by PRMT5 allows Myc proper turnover. We hypothesize S-Myc as typical of aggressive glioblastoma stem cells, as S-Myc/AS-Myc ratio decreases in differentiating, less aggressive, cells
physiological function
WD repeat domain 77 (WDR77), also known as p44 forms a stoichiometric complex with PRMT5. The PRMT5/p44 complex is required for cellular proliferation of lung and prostate epithelial cells during earlier stages of development and is re-activated during prostate and lung tumorigenesis. PRMT5 and p44 regulate expression of a specific set of genes encoding growth and anti-growth factors, including receptor tyrosine kinases and antiproliferative proteins. Genes whose expression is suppressed by PRMT5 and p44 encode anti-growth factors and inhibit cell growth when ectopically expressed. Genes whose expression is enhanced by PRMT5 and p44 encode growth factors and increased cell growth when expressed. Altered expression of target genes is associated with reactivation of PRMT5 and p44 during lung tumorigenesis
physiological function
-
the enzyme (PRMT5) may be involved in tachyzoite-bradyzoite transformation
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
72000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
PRMT5 forms distinct homooligomeric complexes, including a dimer and tetramer. The PRMT5 homo-oligomers are dissociated into a monomer in the presence of a reducing agent, whereas a monomer, dimer, and multimer are detected in the absence or at low concentrations of a reducing agent
additional information
-
PRMT5 forms distinct homooligomeric complexes, including a dimer and tetramer. The PRMT5 homo-oligomers are dissociated into a monomer in the presence of a reducing agent, whereas a monomer, dimer, and multimer are detected in the absence or at low concentrations of a reducing agent
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of isoform PRMT5 in complex with methylosome protein MEP50, bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4
in a structural model, the carboxylate group of the position 4 Asp258 points away from the substrate arginine, possibly to coordinate the binding of one or both of the two lysine residues adjacent to the methylated arginine in the FKRKY sequence of substrate SF3B2
complex of isoform PRMT5, methylosome protein MEP50 and S-adenosylhomocysteine. PRMT5-MEP50 forms an unusual tetramer of heterodimers with substantial surface negative charge. MEP50 is required for PRMT5-catalyzed histone H2A and H4 methyltransferase activity and binds substrates independently. MEP50 binds to the substrate distal of the target arginine and orients the unstructured substrate tail towards the catalytic site of the PRMT5 molecule that is not directly coupled to the substrate-bound MEP50
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA365-369
-
deletion of the sequence GAGRG, residues 365-369 in the -adenosyl-L-methionine-binding motif I, leads to dramatic reduction in catalytic activity
additional information
additional information
construction of deletion mutant, in which the TPR motif or the N terminus is missing, and two C-terminal mutants. No activity is observed with any of the mutants
additional information
-
construction of deletion mutant, in which the TPR motif or the N terminus is missing, and two C-terminal mutants. No activity is observed with any of the mutants
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
curcumin downregulates the PRMT5 expression. Curcumin-mediated signalling events are responsible for its anti-oncogene action against PRMT5
isoform PRMT5 expression is regulated by the circadian clock and responds to both light and temperature cues
PRMT5 expression is down-regulated in senescent and H2O2-treated macrophages rendering ineffectual induction of MHC II transcription by IFN-gamma
PRMT5 protein expression is elevated by 1.8-2.9fold in the denervated tibialis anterior muscle, as compared with the control tibialis anterior muscle
relative to the control muscle PRMT5 mRNA expression levels in the denervated soleus muscle is decreased by 26% after 12 h
PRMT5 expression is down-regulated in senescent and H2O2-treated macrophages rendering ineffectual induction of MHC II transcription by IFN-gamma
PRMT5 expression is down-regulated in senescent and H2O2-treated macrophages rendering ineffectual induction of MHC II transcription by IFN-gamma
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
abundant expression of isoform PRMT5 and its symmetric methylation mark H4R3 in lung carcinoma but not in non-neoplastic human pulmonary alveolar and bronchial epithelial cell lines. More than two thirds of lung tumors express PRMT5. High levels of cytoplasmic PRMT5 are detected in 20.5% of non-small cell lung carcinomas and in 16.5% of pulmonary neuroendocrine tumors. High levels of nuclear PRMT5 are detected in 38.0% of non-small cell lung carcinomas and 24.0% of pulmonary neuroendocrine tumors. Cytoplasmic PRMT5 is associated with high grade in both non-small cell lung carcinomas and pulmonary pulmonary neuroendocrine tumors, while nuclear PRMT5 is more frequent in carcinoid tumors
medicine
knockdown of isoform PRMT5 results in more paralysis in a Caenorhabditis elegans model of Alzheimer's disease
medicine
PRMT5 localizes in the nucleus in benign prostate epithelium, whereas it localizes in the cytoplasm in prostate premalignant and cancer tissues
medicine
PRMT1 and PRMT5 have opposing effects on chemotherapeutic agent-mediated apoptosis in lung cancer cells. The identification of PRMT5 and PRMT1 as CFLARL regulators involved in cellular apoptosis may help in developing new strategies to increase the sensitivity of cancer cells to chemotherapy, which may eventually benefit lung cancer treatments
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rho, J.; Choi, S.; Seong, Y.R.; Cho, W.K.; Kim, S.H.; Im, D.S.
PRMT5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family
J. Biol. Chem.
276
11393-11401
2001
Homo sapiens (O14744), Homo sapiens
brenda
Branscombe, T.L.; Frankel, A.; Lee, J.H.; Cook, J.R.; Yang, Z.; Pestka, S.; Clarke, S.
PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
J. Biol. Chem.
276
32971-32976
2001
Homo sapiens
brenda
Sayegh, J.; Clarke, S.G.
Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast
Biochem. Biophys. Res. Commun.
372
811-815
2008
Saccharomyces cerevisiae (P38274), Saccharomyces cerevisiae
brenda
Lacroix, M.; Messaoudi, S.E.; Rodier, G.; Le Cam, A.; Sardet, C.; Fabbrizio, E.
The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5
EMBO Rep.
9
452-458
2008
Homo sapiens (O14744)
brenda
Wilczek, C.; Chitta, R.; Woo, E.; Shabanowitz, J.; Chait, B.T.; Hunt, D.F.; Shechter, D.
Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs
J. Biol. Chem.
286
42221-42231
2011
Xenopus laevis (Q6NUA1), Xenopus laevis
brenda
Sakai, N.; Saito, Y.; Fujiwara, Y.; Shiraki, T.; Imanishi, Y.; Koshimizu, T.A.; Shibata, K.
Identification of protein arginine N-methyltransferase 5 (PRMT5) as a novel interacting protein with the tumor suppressor protein RASSF1A
Biochem. Biophys. Res. Commun.
467
778-784
2015
Homo sapiens (O14744)
brenda
Sohail, M.; Zhang, M.; Litchfield, D.; Wang, L.; Kung, S.; Xie, J.
Differential expression, distinct localization and opposite effect on Golgi structure and cell differentiation by a novel splice variant of human PRMT5
Biochim. Biophys. Acta
1853
2444-2452
2015
Homo sapiens (O14744), Homo sapiens
brenda
Wang, Y.; Li, Q.; Liu, C.; Han, F.; Chen, M.; Zhang, L.; Cui, X.; Qin, Y.; Bao, S.; Gao, F.
Protein arginine methyltransferase 5 (Prmt5) is required for germ cell survival during mouse embryonic development
Biol. Reprod.
92
104
2015
Mus musculus
brenda
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 (Q8GWT4), Arabidopsis thaliana
brenda
Zhou, Z.; Sun, X.; Zou, Z.; Sun, L.; Zhang, T.; Guo, S.; Wen, Y.; Liu, L.; Wang, Y.; Qin, J.; Li, L.; Gong, W.; Bao, S.
PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130
Cell Res.
20
1023-1033
2010
Homo sapiens (O14744)
brenda
Shilo, K.; Wu, X.; Sharma, S.; Welliver, M.; Duan, W.; Villalona-Calero, M.; Fukuoka, J.; Sif, S.; Baiocchi, R.; Hitchcock, C.L.; Zhao, W.; Otterson, G.A.
Cellular localization of protein arginine methyltransferase-5 correlates with grade of lung tumors
Diagn. Pathol.
8
201
2013
Homo sapiens (O14744)
brenda
Huang, J.; Vogel, G.; Yu, Z.; Almazan, G.; Richard, S.
Type II arginine methyltransferase PRMT5 regulates gene expression of inhibitors of differentiation/DNA binding Id2 and Id4 during glial cell differentiation
J. Biol. Chem.
286
44424-44432
2011
Mus musculus, Rattus norvegicus (D4A0E8)
brenda
Hadjikyriacou, A.; Yang, Y.; Espejo, A.; Bedford, M.T.; Clarke, S.G.
Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing Factor SF3B2
J. Biol. Chem.
290
16723-16743
2015
Homo sapiens (Q6P2P2), Homo sapiens
brenda
Gonsalvez, G.B.; Tian, L.; Ospina, J.K.; Boisvert, F.M.; Lamond, A.I.; Matera, A.G.
Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins
J. Cell Biol.
178
733-740
2007
Homo sapiens (O14744), Homo sapiens
brenda
Liu, F.; Cheng, G.; Hamard, P.J.; Greenblatt, S.; Wang, L.; Man, N.; Perna, F.; Xu, H.; Tadi, M.; Luciani, L.; Nimer, S.D.
Arginine methyltransferase PRMT5 is essential for sustaining normal adult hematopoiesis
J. Clin. Invest.
125
3532-3544
2015
Mus musculus (Q8CIG8)
brenda
Zhang, W.; Zhang, Y.; Zhao, X.; Hua, Y.; Wu, Z.; Yan, Y.; Li, Y.
Prmt7 regulates epiboly by facilitating 2-OST and modulating actin cytoskeleton
J. Mol. Cell Biol.
7
489-491
2015
Danio rerio (A2AV36)
brenda
Quan, X.; Yue, W.; Luo, Y.; Cao, J.; Wang, H.; Wang, Y.; Lu, Z.
The protein arginine methyltransferase PRMT5 regulates Abeta-induced toxicity in human cells and Caenorhabditis elegans models of Alzheimers disease
J. Neurochem.
134
969-977
2015
Caenorhabditis elegans (P46580), Caenorhabditis elegans, Homo sapiens (O14744), Homo sapiens
brenda
Zhang, T.; Guenther, S.; Looso, M.; Kuenne, C.; Krueger, M.; Kim, J.; Zhou, Y.; Braun, T.
Prmt5 is a regulator of muscle stem cell expansion in adult mice
Nat. Commun.
6
7140
2015
Mus musculus (Q8CIG8), Mus musculus
brenda
Gu, Z.; Li, Y.; Lee, P.; Liu, T.; Wan, C.; Wang, Z.
Protein arginine methyltransferase 5 functions in opposite ways in the cytoplasm and nucleus of prostate cancer cells
PLoS ONE
7
e44033
2012
Homo sapiens (O14744)
brenda
Ho, M.C.; Wilczek, C.; Bonanno, J.B.; Xing, L.; Seznec, J.; Matsui, T.; Carter, L.G.; Onikubo, T.; Kumar, P.R.; Chan, M.K.; Brenowitz, M.; Cheng, R.H.; Reimer, U.; Almo, S.C.; Shechter, D.
Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity
PLoS ONE
8
e57008
2013
Xenopus laevis (Q6NUA1), Xenopus laevis
brenda
Hong, S.; Song, H.R.; Lutz, K.; Kerstetter, R.A.; Michael, T.P.; McClung, C.R.
Type II protein arginine methyltransferase 5 (PRMT5) is required for circadian period determination in Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
107
21211-21216
2010
Arabidopsis thaliana (Q8GWT4), Arabidopsis thaliana
brenda
Antonysamy, S.; Bonday, Z.; Campbell, R.M.; Doyle, B.; Druzina, Z.; Gheyi, T.; Han, B.; Jungheim, L.N.; Qian, Y.; Rauch, C.; Russell, M.; Sauder, J.M.; Wasserman, S.R.; Weichert, K.; Willard, F.S.; Zhang, A.; Emtage, S.
Crystal structure of the human PRMT5:MEP50 complex
Proc. Natl. Acad. Sci. USA
109
17960-17965
2012
Homo sapiens (O14744), Homo sapiens
brenda
Likhite, N.; Jackson, C.A.; Liang, M.S.; Krzyzanowski, M.C.; Lei, P.; Wood, J.F.; Birkaya, B.; Michaels, K.L.; Andreadis, S.T.; Clark, S.D.; Yu, M.C.; Ferkey, D.M.
The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling
Sci. Signal.
8
ra115
2015
Homo sapiens (O14744), Homo sapiens, Caenorhabditis elegans (P46580), Caenorhabditis elegans
brenda
Stouth, D.W.; Manta, A.; Ljubicic, V.
Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity
Am. J. Physiol. Cell Physiol.
314
C177-C190
2018
Mus musculus (Q8CIG8)
brenda
Hadjikyriacou, A.; Clarke, S.G.
Caenorhabditis elegans PRMT-7 and PRMT-9 are evolutionarily conserved protein arginine methyltransferases with distinct substrate specificities
Biochemistry
56
2612-2626
2017
Caenorhabditis elegans (O02325), Caenorhabditis elegans
brenda
Fan, Z.; Kong, X.; Xia, J.; Wu, X.; Li, H.; Xu, H.; Fang, M.; Xu, Y.
The arginine methyltransferase PRMT5 regulates CIITA-dependent MHC II transcription
Biochim. Biophys. Acta
1859
687-696
2016
Homo sapiens (O14744), Mus musculus (Q8CIG8)
brenda
di Caprio, R.; Ciano, M.; Montano, G.; Costanzo, P.; Cesaro, E.
KAP1 is a novel substrate for the arginine methyltransferase PRMT5
Biology
4
41-49
2015
Homo sapiens (O14744)
brenda
Zhu, K.; Song, J.L.; Tao, H.R.; Cheng, Z.Q.; Jiang, C.S.; Zhang, H.
Discovery of new potent protein arginine methyltransferase 5 (PRMT5) inhibitors by assembly of key pharmacophores from known inhibitors
Bioorg. Med. Chem. Lett.
28
3693-3699
2018
Homo sapiens (O14744), Homo sapiens
brenda
Lin, H.; Luengo, J.I.
Nucleoside protein arginine methyltransferase 5 (PRMT5) inhibitors
Bioorg. Med. Chem. Lett.
29
1264-1269
2019
Homo sapiens (O14744)
brenda
Sheng, X.; Wang, Z.
Protein arginine methyltransferase 5 regulates multiple signaling pathways to promote lung cancer cell proliferation
BMC Cancer
16
567
2016
Homo sapiens (O14744)
brenda
Stopa, N.; Krebs, J.E.; Shechter, D.
The PRMT5 arginine methyltransferase many roles in development, cancer and beyond
Cell. Mol. Life Sci.
72
2041-2059
2015
Homo sapiens (O14744), Homo sapiens, Caenorhabditis elegans (P46580), Caenorhabditis elegans, Xenopus laevis (Q6NUA1)
brenda
Zhu, J.; Zhang, D.; Liu, X.; Yu, G.; Cai, X.; Xu, C.; Rong, F.; Ouyang, G.; Wang, J.; Xiao, W.
Zebrafish prmt5 arginine methyltransferase is essential for germ cell development
Development
146
dev179572
2019
Danio rerio (B0R026), Danio rerio
brenda
Bowitch, A.; Michaels, K.; Yu, M.; Ferkey, D.
The protein arginine methyltransferase PRMT-5 regulates SER-2 tyramine receptor-mediated behaviors in Caenorhabditis elegans
G3 (Bethesda)
8
2389-2398
2018
Caenorhabditis elegans (P46580), Caenorhabditis elegans
brenda
Chung, J.; Karkhanis, V.; Baiocchi, R.A.; Sif, S.
Protein arginine methyltransferase 5 (PRMT5) promotes survival of lymphoma cells via activation of WNT/?-catenin and AKT/GSK3? proliferative signaling
J. Biol. Chem.
294
7692-7710
2019
Homo sapiens (O14744), Mus musculus (Q8CIG8), Mus musculus
brenda
Li, M.; An, W.; Xu, L.; Lin, Y.; Su, L.; Liu, X.
The arginine methyltransferase PRMT5 and PRMT1 distinctly regulate the degradation of anti-apoptotic protein CFLARL in human lung cancer cells
J. Exp. Clin. Cancer Res.
38
64
2019
Homo sapiens (O14744), Homo sapiens
brenda
Wang, Y.; Hu, W.; Yuan, Y.
Protein arginine methyltransferase 5 (PRMT5) as an anticancer target and its inhibitor discovery
J. Med. Chem.
61
9429-9441
2018
Homo sapiens (O14744)
brenda
Chatterjee, B.; Ghosh, K.; Suresh, L.; Kanade, S.
Curcumin ameliorates PRMT5-MEP50 arginine methyltransferase expression by decreasing the Sp1 and NF-YA transcription factors in the A549 and MCF-7 cells
Mol. Cell. Biochem.
455
73-90
2019
Homo sapiens (O14744), Homo sapiens
brenda
Liu, M.; Li, F.; Li, C.; Li, X.; Chen, L.; Wu, K.; Yang, P.; Lai, Z.; Liu, T.; Sullivan, W.J.; Cui, L.; Chen, X.
Characterization of protein arginine methyltransferase of TgPRMT5 in Toxoplasma gondii
Parasit. Vectors
12
221
2019
Toxoplasma gondii (S7UQT1), Toxoplasma gondii, Toxoplasma gondii ATCC 50853 (S7UQT1)
brenda
Jain, K.; Jin, C.; Clarke, S.
Epigenetic control via allosteric regulation of mammalian protein arginine methyltransferases
Proc. Natl. Acad. Sci. USA
114
10101-10106
2017
Homo sapiens (O14744)
brenda
Favia, A.; Salvatori, L.; Nanni, S.; Iwamoto-Stohl, L.; Valente, S.; Mai, A.; Scagnoli, F.; Fontanella, R.; Totta, P.; Nasi, S.; Illi, B.
The protein arginine methyltransferases 1 and 5 affect Myc properties in glioblastoma stem cells
Sci. Rep.
9
15925
2019
Homo sapiens (O14744)
brenda
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