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2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega-dimethyl-L-arginine
3 S-adenosyl-L-methionine + SGRGKGGKGLGKGGAKRHRK-NH2
3 S-adenosyl-L-homocysteine + SG-(Nomega-Me)RGKGGKGLGKGGAK-(Nomega-Me)RH-(Nomega-Me)RK-NH2
-
-
-
?
5 S-adenosyl-L-methionine + AGRGRGKAAILKAQVAARGRGRGMGRGN-NH2
5 S-adenosyl-L-homocysteine + AG-(Nomega-Me)RG-(Nomega-Me)RGKAAILKAQVAA-(Nomega-Me)RG-(Nomega-Me)RGRGMG-(Nomega-Me)RGN-NH2
-
-
-
?
S-adenosyl-L-methionine + acetyl-GGRGG-NH2
S-adenosyl-L-homocysteine + acetyl-GG-(Nomega-methyl-)RGG-NH2
substrate is a synthetic peptide
-
-
?
S-adenosyl-L-methionine + GGFGGRGGFG-NH2
S-adenosyl-L-homocysteine + GGFGG-(Nomega-methyl-)RGGFG-NH2
substrate is a synthetic peptide
product is monomethylated at residue R6
-
?
S-adenosyl-L-methionine + GGPGGRGGPGG-NH2
S-adenosyl-L-homocysteine + GGPGG-Nomega-methyl-RGGPGG
substrate is a synthetic peptide
enzyme catalyzes monomethylation of Arg-residues
-
?
S-adenosyl-L-methionine + SG-(Nomega-methyl-)RGKGGKGLGKGGAKRHRK-NH2
S-adenosyl-L-homocysteine + SG-(Nomega-methyl-)RGKGGKGLGKGGAK-(Nomega-methyl-)RHRK-NH2
-
-
-
?
S-adenosyl-L-methionine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-L-arginine
S-adenosyl-L-homocysteine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [beta-catenin]-L-arginine
S-adenosyl-L-homocysteine + [beta-catenin]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [eukaryotic translation initiation factor 2alpha]-L-arginine
S-adenosyl-L-homocysteine + [eukaryotic translation initiation factor 2alpha]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [GLI2]-L-arginine
S-adenosyl-L-homocysteine + [GLI2]-Nomega-methyl-L-arginine
PRMT7 interacts with and methylates GLI2 on arginine residues 225 and 227 nearby a binding region of SUFU, a negative regulator of GLI2
-
-
?
S-adenosyl-L-methionine + [GST-GAR]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR]-Nomega-methyl-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 H2B peptide 23-37]-L-arginine
S-adenosyl-L-homocysteine + [histone H2B peptide 23-37]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H2B]-L-arginine
S-adenosyl-L-homocysteine + [histone H2B]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-arginine
S-adenosyl-L-homocysteine + [histone H3]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4 peptide 1-20]-L-arginine
S-adenosyl-L-homocysteine + [histone H4 peptide 1-20]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4 peptide 14-22]-L-arginine
S-adenosyl-L-homocysteine + [histone H4 peptide 14-22]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
S-adenosyl-L-methionine + [human histone H2B peptide]-L-arginine
S-adenosyl-L-homocysteine + [human histone H2B peptide]-Nomega-methyl-L-arginine
Caenorhabditis elegans PRMT-7 is able to methylate synthetic human histone H2B peptides containing residues 23-37. The C. elegans enzyme recognizes the human peptide better than the Caenorhabditis elegans peptide. The histone H2B R29K peptide reduces methylation counts to a level about 40%, of that of the wild type peptide sequence. The R31K and R33K mutant peptides further decrease the activity to about 10% and 22% respectively, signifying the importance of arginine residues in a sequential R-X-R motif
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?
S-adenosyl-L-methionine + [myelin basic protein]-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
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-
-
?
S-adenosyl-L-methionine + [protein]-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [Smb protein]-L-arginine
S-adenosyl-L-homocysteine + [Smb protein]-Nomega-methyl-L-arginine
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-
-
?
additional information
?
-
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega-dimethyl-L-arginine
the enzyme has a strong preference for RXR motifs surrounded by basic amino acids
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-
?
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega-dimethyl-L-arginine
the enzyme has a strong preference for RXR motifs surrounded by basic amino acids
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?
S-adenosyl-L-methionine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-L-arginine
S-adenosyl-L-homocysteine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-Nomega-methyl-L-arginine
peptides based on the Arg-Gly-Gly (RGG)-containing RNA binding proteins are substrates in the naked form but are not substrates in the monomethylated form
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-
?
S-adenosyl-L-methionine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-L-arginine
S-adenosyl-L-homocysteine + [Ac-GGRGGFGGKGGCGGKGGFGGKGGFG peptide]-Nomega-methyl-L-arginine
peptides based on the Arg-Gly-Gly (RGG)-containing RNA binding proteins are substrates in the naked form but are not substrates in the monomethylated form
-
-
?
S-adenosyl-L-methionine + [beta-catenin]-L-arginine
S-adenosyl-L-homocysteine + [beta-catenin]-Nomega-methyl-L-arginine
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-
-
?
S-adenosyl-L-methionine + [beta-catenin]-L-arginine
S-adenosyl-L-homocysteine + [beta-catenin]-Nomega-methyl-L-arginine
the enzyme (PRMT7) upregulates the expression of C-MYC via methylating beta-catenin and inhibiting the ubiquitin-mediated degradation of beta-catenin
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-
?
S-adenosyl-L-methionine + [eukaryotic translation initiation factor 2alpha]-L-arginine
S-adenosyl-L-homocysteine + [eukaryotic translation initiation factor 2alpha]-Nomega-methyl-L-arginine
PRMT7 methylates eukaryotic translation initiation factor 2alpha (eIF2alpha) and regulates its role in stress granule formation
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-
?
S-adenosyl-L-methionine + [eukaryotic translation initiation factor 2alpha]-L-arginine
S-adenosyl-L-homocysteine + [eukaryotic translation initiation factor 2alpha]-Nomega-methyl-L-arginine
PRMT7 methylates eukaryotic translation initiation factor 2alpha (eIF2alpha) within an RXR motif and regulates its role in stress granule formation
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-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3
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-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
PRMT7-mediated monomethylation of histone H4 Arg17 regulates PRMT5 activity at Arg3 in the same protein
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-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3
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-
?
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [protein]-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
substrate preference for arginine residues in R-X-R motifs with additional flanking basic amino acid residues
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-
?
S-adenosyl-L-methionine + [protein]-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
PRMT7 interacts with and methylates GLI2 on arginine residues 225 and 227 nearby a binding region of SUFU, a negative regulator of GLI2
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-
?
S-adenosyl-L-methionine + [protein]-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
substrate preference for arginine residues in R-X-R motifs with additional flanking basic amino acid residues
-
-
?
additional information
?
-
enzyme is capable of forming only omega-NG-monomethylarginine, not asymmetric omega-NG,NG-dimethylarginine or symmetric omega-NG,NG-dimethylarginine. No substrates: SGAGKGGKGLGKGGAKAHAK-NH2, GRG-NH2
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-
?
additional information
?
-
-
enzyme is capable of forming only omega-NG-monomethylarginine, not asymmetric omega-NG,NG-dimethylarginine or symmetric omega-NG,NG-dimethylarginine. No substrates: SGAGKGGKGLGKGGAKAHAK-NH2, GRG-NH2
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?
additional information
?
-
no substrate: GST-fibrillarin fusion protein containing fibrillarin residues 1-148, substrate of isoforms PRMT1, PRMT3, PRMT4, PRMT5, EC 2.1.1.319. Isoform PRMT7 neither methylates myelin basic protein or histone H2A, in vitro substrates of PRMT5
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?
additional information
?
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argininosuccinate synthetase (ASS1) specifically interacts with PRMT7 and that mutations in ASS1 at the interaction interface of PRMT7-ASS1 are detrimental. The interaction of PRMT7 with ASS1 implies that ASS1 might be a plausible substrate of PRMT7
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-
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S-adenosyl-L-methionine + [beta-catenin]-L-arginine
S-adenosyl-L-homocysteine + [beta-catenin]-Nomega-methyl-L-arginine
the enzyme (PRMT7) upregulates the expression of C-MYC via methylating beta-catenin and inhibiting the ubiquitin-mediated degradation of beta-catenin
-
-
?
S-adenosyl-L-methionine + [eukaryotic translation initiation factor 2alpha]-L-arginine
S-adenosyl-L-homocysteine + [eukaryotic translation initiation factor 2alpha]-Nomega-methyl-L-arginine
PRMT7 methylates eukaryotic translation initiation factor 2alpha (eIF2alpha) and regulates its role in stress granule formation
-
-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
S-adenosyl-L-methionine + [protein]-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
PRMT7 interacts with and methylates GLI2 on arginine residues 225 and 227 nearby a binding region of SUFU, a negative regulator of GLI2
-
-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3
-
-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
PRMT7-mediated monomethylation of histone H4 Arg17 regulates PRMT5 activity at Arg3 in the same protein
-
-
?
S-adenosyl-L-methionine + [histone H4R17]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R17]-Nomega-methyl-L-arginine
crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3
-
-
?
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
-
-
?
S-adenosyl-L-methionine + [histone H4R3]-L-arginine
S-adenosyl-L-homocysteine + [histone H4R3]-Nomega-dimethyl-L-arginine
-
-
-
?
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drug target
overexpressed PRMT7 in clear cell renal cell carcinoma (ccRCC) cells acts as an oncogene to promote the growth of renal cell carcinoma through regulating the beta-catenin/C-MYC axis, thereby providing new strategies and targets for the treatment of ccRCC patients
metabolism
overexpression of the PRMT7 gene is correlated with cancer metastasis in humans
malfunction
defects in muscle stem cells (satellite cells) and immune cells are found in mouse Prmt7 homozygous knockout
malfunction
defects in muscle stem cells (satellite cells) and immune cells are found in mouse Prmt7 homozygous knockouts
malfunction
humans lacking PRMT7 are characterized by significant intellectual developmental delays, hypotonia, and facial dysmorphisms
malfunction
humans lacking PRMT7 are characterized by significant intellectual developmental delays, hypotonia, and facial dysmorphisms. The overexpression of the PRMT7 gene is correlated with cancer metastasis in humans
malfunction
knockdown of medaka prmt7 does not reduce the total number of primordial germ cells (PGCs) in vivo but significantly affects PGCs distribution during embryonic development
malfunction
PRMT7-deficient mouse embryonic fibroblasts (MEFs) exhibit a premature cellular senescence with accompanied increase in the cell cycle inhibitors p16 and p21. PRMT7 depletion results in reduced Shh signaling activity in MEFs
malfunction
stress granule formation, in the face of eIF2alpha-dependent cellular stresses, is significantly diminished in PRMT7-knockdown
physiological function
imprinting control region-binding protein CTCFL/BORIS stimulates the histone-methyltransferase activity of PRMT7 via interactions with both histones and PRMT7
physiological function
knockdown of isoform PRMT5, EC 2.1.1.320, 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 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
loss of PRMT7 leads to decreased mature marginal zone B cells and increased follicular B cells and promotes germinal center formation after immunization. Mice lacking PRMT7 expression in B cells secrete low levels of IgG1 and IgA. Conditional knockout mice show abnormal expression of germinal center genes (i.e., Bcl6, Prdm1, and Irf4).Overexpression of PRMT7 in the Raji and A20 cell lines derived from B cell lymphomas negatively regulates Bcl6 expression. PRMT7 can recruit histone H4R3me1 and symmetric H4R3me2 to the Bcl6 promoter
physiological function
PRMT7 negatively regulates expression of genes involved in DNA repair, including ALKBH5, APEX2, POLD1, and POLD2. PRMT7 and dimethylated histones H2AR3 and H4R3are enriched at target DNA repair genes in parental cells, whereas PRMT7 knockdown causes a significant decrease in PRMT7 recruitment and H2AR3/H4R3 methylation. Decreased PRMT7 expression also results in derepression of target DNA repair genes and enhanced cell resistance to DNA-damaging agents. BRG1 colocalizes with PRMT7 on target promoters and expression of a catalytically inactive form of BRG1results in derepression of PRMT7 target DNA repair genes
physiological function
reducing PRMT7 levels in invasive breast cancer cells using RNA interference significantly decreases cell invasion in vitro and metastasis in vivo. Overexpression of PRMT7 in non-aggressive MCF-7 cells enhances their invasiveness. PRMT7 induces the expression of matrix metalloproteinase MMP9. Invasion of aggressive breast cancer cells depleted of PRMT7 may be rescued by the exogenous expression of MMP9
physiological function
arginine methylation is an important posttranslational modification and catalyzed by a family of protein arginine methyltransferases. PRMT7 plays important roles in multiple biological processes in mammals. PRMT7 may be involved in germ cell development in Oryzias latipes
physiological function
arginine methyltransferase 7 (PRMT7), an epigenetic modifier, is an essential pluripotency factor that maintains the stemness of mouse embryonic stem cells (ESCs), at least in part, by down-regulating the expression of the anti-stemness microRNA (miRNA) miR-24-2. miR-221 gene-encoded miR-221-3p and miR-221-5p are anti-stemness miRNAs whose expression levels in mouse ESCs are directly repressed by PRMT7. Both miR-221-3p and miR-221-5p target the 3' untranslated regions of mRNA transcripts of the major pluripotency factors Oct4, Nanog, and Sox2 to antagonize mouse ESC stemness. miR-221-5p silences also the expression of its own transcriptional repressor PRMT7. Transfection of miR-221-3p and miR-221-5p mimics induced spontaneous differentiation of mouse ESCs. CRISPR-mediated deletion of the miR-221 gene, as well as specific antisense inhibitors of miR-221-3p and miR-221-5p, inhibit the spontaneous differentiation of PRMT7-depleted mouse ESCs. PRMT7-mediated repression of miR-221-3p and miR-221-5p expression plays a critical role in maintaining mouse ESC stemness
physiological function
in human cell lines PRMT7 expression and subsequent methylation of histone H4R3 leads to repression of DNA damage repair genes such as APEX2, POLD1, and POLD2. The enzyme (PRMT7) is involved in regulation of the DNA repair machinery of the cell
physiological function
PRMT7 methylates eukaryotic translation initiation factor 2alpha and regulates its role in stress granule formation
physiological function
the enzyme (PRMT7) catalyzes the introduction of mono methylation marks at the arginine residues of substrate proteins. PRMT7 plays important roles in the regulation of gene expression, splicing, DNA damage, paternal imprinting, cancer and metastasis
physiological function
the enzyme (PRMT7) promotes Shh signaling via GLI2 methylation which is critical for suppression of cellular senescence. PRMT7 overexpression enhances GLI2-reporter activities that are sensitive to methylation inhibition. PRMT7 interacts with and methylates GLI2 on arginine residues 225 and 227 nearby a binding region of SUFU, a negative regulator of GLI2. This methylation interferes with GLI2-SUFU binding, leading to facilitation of GLI2 nuclear accumulation and Shh signaling. PRMT7 induces GLI2 methylation, reducing its binding to SUFU and increasing Shh signaling, ultimately leading to prevention of cellular senescence
physiological function
the enzyme (PRMT7) regulates the expression of C-MYC, which plays an important role in promoting ccRCC cell proliferation, and it accelerates the tumor development of RCC in a C-MYC-dependent manner. It upregulates the expression of C-MYC via methylating beta-catenin and inhibiting the ubiquitin-mediated degradation of beta-catenin
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Miranda, T.B.; Miranda, M.; Frankel, A.; Clarke, S.
PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
J. Biol. Chem.
279
22902-22907
2004
Homo sapiens (Q9NVM4)
brenda
Jelinic, P.; Stehle, J.C.; Shaw, P.
The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation
PLoS Biol.
4
e355
2006
Homo sapiens (Q9NVM4)
brenda
Karkhanis, V.; Wang, L.; Tae, S.; Hu, Y.J.; Imbalzano, A.N.; Sif, S.
Protein arginine methyltransferase 7 regulates cellular response to DNA Damage by Methylating promoter histones H2A and H4 of the polymerase delta catalytic subunit gene, POLD1
J. Biol. Chem.
287
29801-29814
2012
Homo sapiens (Q9NVM4)
brenda
Zurita-Lopez, C.; Sandberg, T.; Kelly, R.; Clarke, S.
Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues
J. Biol. Chem.
287
7859-7870
2012
Homo sapiens (Q9NVM4), Homo sapiens
brenda
Cura, V.; Troffer-Charlier, N.; Wurtz, J.M.; Bonnefond, L.; Cavarelli, J.
Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site
Acta Crystallogr. Sect. D
70
2401-2412
2014
Mus musculus (Q922X9), Mus musculus
brenda
Feng, Y.; Maity, R.; Whitelegge, J.P.; Hadjikyriacou, A.; Li, Z.; Zurita-Lopez, C.; Al-Hadid, Q.; Clark, A.T.; Bedford, M.T.; Masson, J.Y.; Clarke, S.G.
Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions
J. Biol. Chem.
288
37010-37025
2013
Mus musculus (Q922X9), Mus musculus
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 (Q9NVM4)
brenda
Ying, Z.; Mei, M.; Zhang, P.; Liu, C.; He, H.; Gao, F.; Bao, S.
Histone arginine methylation by PRMT7 controls germinal center formation via regulating Bcl6 transcription
J. Immunol.
195
1538-1547
2015
Mus musculus (Q922X9)
brenda
Baldwin, R.M.; Haghandish, N.; Daneshmand, M.; Amin, S.; Paris, G.; Falls, T.J.; Bell, J.C.; Islam, S.; Cote, J.
Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression
Oncotarget
6
3013-3032
2015
Homo sapiens (Q9NVM4), Homo sapiens
brenda
Jain, K.; Clarke, S.G.
PRMT7 as a unique member of the protein arginine methyltransferase family A review
Arch. Biochem. Biophys.
665
36-45
2019
Trypanosoma brucei brucei (Q582G4), Mus musculus (Q922X9), Homo sapiens (Q9NVM4), Caenorhabditis elegans (Q9XW42), Trypanosoma brucei brucei 927 (Q582G4)
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 (Q9XW42), Caenorhabditis elegans
brenda
Vuong, T.A.; Jeong, H.J.; Lee, H.J.; Kim, B.G.; Leem, Y.E.; Cho, H.; Kang, J.S.
PRMT7 methylates and suppresses GLI2 binding to SUFU thereby promoting its activation
Cell Death Differ.
27
15-28
2020
Mus musculus (Q922X9), Mus musculus
brenda
Liu, F.; Wan, L.; Zou, H.; Pan, Z.; Zhou, W.; Lu, X.
PRMT7 promotes the growth of renal cell carcinoma through modulating the beta-catenin/C-MYC axis
Int. J. Biochem. Cell Biol.
120
105686
2020
Homo sapiens (Q9NVM4)
brenda
Chen, T.Y.; Lee, S.H.; Dhar, S.S.; Lee, M.G.
Protein arginine methyltransferase 7-mediated microRNA-221 repression maintains Oct4, Nanog, and Sox2 levels in mouse embryonic stem cells
J. Biol. Chem.
293
3925-3936
2018
Mus musculus (Q922X9), Mus musculus
brenda
Thakur, A.; Hevel, J.M.; Acevedo, O.
Examining product specificity in protein arginine methyltransferase 7 (PRMT7) using quantum and molecular mechanical simulations
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