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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Protein arginine methyltransferase 7

PRMT7, protein arginine N-methyltransferase 7, protein arginine methyltransferase 7
Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport, and RNA splicing (Miranda et al., 2004 [PubMed 15044439]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: PRMT5, Histone, Protein-Arginine N-Methyltransferase, H4, CARM1
Papers on PRMT7
Histone Arginine Methylation by PRMT7 Controls Germinal Center Formation via Regulating Bcl6 Transcription.
Bao et al., Beijing, China. In J Immunol, Sep 2015
To explore the effects of aberrant histone arginine methylation on B cells, we generated mice with a B cell-specific knockout of PRMT7, a member of the methyltransferases that mediate arginine methylation of histones.
Discovery of a Dual PRMT5-PRMT7 Inhibitor.
Schapira et al., Toronto, Canada. In Acs Med Chem Lett, May 2015
The protein arginine methyltransferases PRMT7 and PRMT5, respectively, monomethylate and symmetrically dimethylate arginine side-chains of proteins involved in diverse cellular mechanisms, including chromatin-mediated control of gene transcription, splicing, and the RAS to ERK transduction cascade.
A novel BLAST-Based Relative Distance (BBRD) method can effectively group members of protein arginine methyltransferases and suggest their evolutionary relationship.
Li et al., T'ai-chung-shih, Taiwan. In Mol Phylogenet Evol, Mar 2015
The tree placed the uncharacterized PRMT9 with PRMT7 in the same clade, outside of all the Type I PRMTs including PRMT1 and its vertebrate paralogue PRMT8, PRMT3, PRMT6, PRMT2 and PRMT4.
Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression.
Côté et al., Ottawa, Canada. In Oncotarget, Mar 2015
PRMT7 has been identified in several gene expression studies to be associated with increased metastasis and decreased survival in breast cancer patients.
Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop.
Clarke et al., Los Angeles, United States. In J Biol Chem, 2014
Protein arginine methyltransferase 7 (PRMT7) methylates arginine residues on various protein substrates and is involved in DNA transcription, RNA splicing, DNA repair, cell differentiation, and metastasis.
Altered expression of an RBP-associated arginine methyltransferase 7 in Leishmania major affects parasite infection.
Cruz et al., Ribeirão Preto, Brazil. In Mol Microbiol, 2014
The Leishmania major genome encodes five PRMT homologs, including PRMT7.
PRMT7 induces epithelial-to-mesenchymal transition and promotes metastasis in breast cancer.
Lu et al., Changchun, China. In Cancer Res, 2014
The protein arginine methyltransferase PRMT7 functions in various physiologic processes, including mRNA splicing, DNA repair, and neural differentiation, but its possible roles in cancer and metastasis have not been explored.
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.
Cavarelli et al., Illkirch-Graffenstaden, France. In Acta Crystallogr D Biol Crystallogr, 2014
Protein arginine methyltransferase 7 (PRMT7) is a type III arginine methyltransferase which has been implicated in several biological processes such as transcriptional regulation, DNA damage repair, RNA splicing, cell differentiation and metastasis.
Role of PRMTs in cancer: Could minor isoforms be leaving a mark?
Côté et al., Ottawa, Canada. In World J Biol Chem, 2014
Specifically, PRMT1, PRMT2, CARM1 and PRMT7 have been shown to have alternative isoforms and others may be currently unrealized.
Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats.
Shimizu et al., Tokyo, Japan. In Febs Lett, 2014
Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues.
Structural determinants for the strict monomethylation activity by trypanosoma brucei protein arginine methyltransferase 7.
Shi et al., Hefei, China. In Structure, 2014
Trypanosoma brucei protein arginine methyltransferase 7 (TbPRMT7) exclusively generates monomethylarginine (MMA), which directs biological consequences distinct from that of symmetric dimethylarginine (SDMA) and asymmetric dimethylarginine (ADMA).
Cloning, expression, purification and preliminary X-ray crystallographic analysis of mouse protein arginine methyltransferase 7.
Cavarelli et al., Illkirch-Graffenstaden, France. In Acta Crystallogr Sect F Struct Biol Commun, 2014
Protein arginine methyltransferase 7 (PRMT7) is a unique but less characterized member of the family of protein arginine methyltransferases (PRMTs) that plays a role in male germline gene imprinting.
Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions.
Clarke et al., In J Biol Chem, 2014
The mammalian protein arginine methyltransferase 7 (PRMT7) has been implicated in roles of transcriptional regulation, DNA damage repair, RNA splicing, cell differentiation, and metastasis.
Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4.
Lee et al., Houston, United States. In Genes Dev, 2013
The protein arginine methyltransferase 7 (PRMT7), but not PRMT5, represses MLL4 target genes by up-regulating H4R3me2s levels and antagonizes MLL4-mediated differentiation.
Prmt7 is dispensable in tissue culture models for adipogenic differentiation.
Imbalzano et al., Worcester, United States. In F1000res, 2012
Protein arginine methyltransferase 7 (Prmt7) is categorized as a type II and type III enzyme that produces symmetric dimethylated arginine and monomethylated arginine, respectively.
Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1.
Sif et al., Columbus, United States. In J Biol Chem, 2012
reducing expression of individual PRMT7 target DNA repair genes showed that only the catalytic subunit of DNA polymerase, POLD1, was able to resensitize PRMT7 knock-down cells to DNA-damaging agents.
Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.
Clarke et al., Los Angeles, United States. In J Biol Chem, 2012
Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues.
Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance.
Guccione et al., Singapore, Singapore. In Nat Struct Mol Biol, 2012
Here the authors report that H3R2 is also symmetrically dimethylated (H3R2me2s) by PRMT5 and PRMT7 and present in euchromatic regions.
Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins.
Matera et al., Cleveland, United States. In J Cell Biol, 2007
that in human cells, PRMT5 and PRMT7 are required for Sm protein sDMA modification, and that Sm protein symmetric dimethylarginine modification is required for snRNP biogenesis in human cells.
The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation.
Shaw et al., Lausanne, Switzerland. In Plos Biol, 2006
CTCFL and PRMT7 may play a role in male germline imprinted gene methylation.
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