2.1.1.321: type III protein arginine methyltransferase
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For detailed information about type III protein arginine methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.321
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2.1.1.321
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prmt7
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histone
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monomethylation
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metastasis
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monomethylarginine
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dimethylarginine
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nanog
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adomet
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medicine
- 2.1.1.321
- prmt7
- histone
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monomethylation
- metastasis
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monomethylarginine
- dimethylarginine
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nanog
- adomet
- medicine
Reaction
Synonyms
EC 2.1.1.124, EC 2.1.1.125, EC 2.1.1.126, EC 2.1.1.23, PRMT-7, PRMT7, protein arginine methyltransferase 7
ECTree
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General Information on EC 2.1.1.321 - type III protein arginine methyltransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
malfunction
metabolism
overexpression of the PRMT7 gene is correlated with cancer metastasis in humans
physiological function
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
