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    PRMT7 protein arginine methyltransferase 7 [ Homo sapiens (human) ]

    Gene ID: 54496, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites.

    The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites.
    Bondoc TJ, Lowe TL, Clarke SG., Free PMC Article

    05/30/2023
    Short stature in PRMT7 Mutations: first evidence of response to growth hormone treatment.

    Short stature in PRMT7 Mutations: first evidence of response to growth hormone treatment.
    Rodari G, Villa R, Porro M, Gangi S, Iascone M, Elli F, Giacchetti F, Profka E, Collini V, Dall'Antonia A, Arosio M, Mantovani G, Bedeschi MF, Giavoli C., Free PMC Article

    02/13/2023
    Biallelic PRMT7 pathogenic variants are associated with a recognizable syndromic neurodevelopmental disorder with short stature, obesity, and craniofacial and digital abnormalities.

    Biallelic PRMT7 pathogenic variants are associated with a recognizable syndromic neurodevelopmental disorder with short stature, obesity, and craniofacial and digital abnormalities.
    Cali E, Suri M, Scala M, Ferla MP, Alavi S, Faqeih EA, Bijlsma EK, Wigby KM, Baralle D, Mehrjardi MYV, Schwab J, Platzer K, Steindl K, Hashem M, Jones M, Niyazov DM, Jacober J, Littlejohn RO, Weis D, Zadeh N, Rodan L, Goldenberg A, Lecoquierre F, Dutra-Clarke M, Horvath G, Young D, Orenstein N, Bawazeer S, Vulto-van Silfhout AT, Herenger Y, Dehghani M, Seyedhassani SM, Bahreini A, Nasab ME, Ercan-Sencicek AG, Firoozfar Z, Movahedinia M, Efthymiou S, Striano P, Karimiani EG, Salpietro V, Taylor JC, Redman M, Stegmann APA, Laner A, Abdel-Salam G, Li M, Bengala M, Müller AJ, Digilio MC, Rauch A, Gunel M, Titheradge H, Schweitzer DN, Kraus A, Valenzuela I, McLean SD, Phornphutkul C, Salih M, Begtrup A, Schnur RE, Torti E, Haack TB, Prada CE, Alkuraya FS, Houlden H, Maroofian R., Free PMC Article

    01/14/2023
    An enhancer variant at 16q22.1 predisposes to hepatocellular carcinoma via regulating PRMT7 expression.

    An enhancer variant at 16q22.1 predisposes to hepatocellular carcinoma via regulating PRMT7 expression.
    Shen T, Ni T, Chen J, Chen H, Ma X, Cao G, Wu T, Xie H, Zhou B, Wei G, Saiyin H, Shen S, Yu P, Xiao Q, Liu H, Gao Y, Long X, Yin J, Guo Y, Wu J, Wei GH, Hou J, Jiang DK., Free PMC Article

    04/23/2022
    The arginine methyltransferase PRMT7 promotes extravasation of monocytes resulting in tissue injury in COPD.

    The arginine methyltransferase PRMT7 promotes extravasation of monocytes resulting in tissue injury in COPD.
    Günes Günsel G, Conlon TM, Jeridi A, Kim R, Ertüz Z, Lang NJ, Ansari M, Novikova M, Jiang D, Strunz M, Gaianova M, Hollauer C, Gabriel C, Angelidis I, Doll S, Pestoni JC, Edelmann SL, Kohlhepp MS, Guillot A, Bassler K, Van Eeckhoutte HP, Kayalar Ö, Konyalilar N, Kanashova T, Rodius S, Ballester-López C, Genes Robles CM, Smirnova N, Rehberg M, Agarwal C, Krikki I, Piavaux B, Verleden SE, Vanaudenaerde B, Königshoff M, Dittmar G, Bracke KR, Schultze JL, Watz H, Eickelberg O, Stoeger T, Burgstaller G, Tacke F, Heissmeyer V, Rinkevich Y, Bayram H, Schiller HB, Conrad M, Schneider R, Yildirim AÖ., Free PMC Article

    04/9/2022
    Arginine monomethylation by PRMT7 controls MAVS-mediated antiviral innate immunity.

    Arginine monomethylation by PRMT7 controls MAVS-mediated antiviral innate immunity.
    Zhu J, Li X, Cai X, Zha H, Zhou Z, Sun X, Rong F, Tang J, Zhu C, Liu X, Fan S, Wang J, Liao Q, Ouyang G, Xiao W.

    08/28/2021
    The role of protein arginine methyltransferase 7 in human developmentally arrested embryos cultured in vitro.

    The role of protein arginine methyltransferase 7 in human developmentally arrested embryos cultured in vitro.
    Zhang W, Li S, Li K, Li LI, Yin P, Tong G.

    08/7/2021
    Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth.

    Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth.
    Li WJ, He YH, Yang JJ, Hu GS, Lin YA, Ran T, Peng BL, Xie BL, Huang MF, Gao X, Huang HH, Zhu HH, Ye F, Liu W., Free PMC Article

    04/13/2021
    PRMT7 promotes the growth of renal cell carcinoma through modulating the beta-catenin/C-MYC axis.

    PRMT7 promotes the growth of renal cell carcinoma through modulating the β-catenin/C-MYC axis.
    Liu F, Wan L, Zou H, Pan Z, Zhou W, Lu X.

    10/31/2020
    Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response.

    Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response.
    Szewczyk MM, Ishikawa Y, Organ S, Sakai N, Li F, Halabelian L, Ackloo S, Couzens AL, Eram M, Dilworth D, Fukushi H, Harding R, Dela Seña CC, Sugo T, Hayashi K, McLeod D, Zepeda C, Aman A, Sánchez-Osuna M, Bonneil E, Takagi S, Al-Awar R, Tyers M, Richard S, Takizawa M, Gingras AC, Arrowsmith CH, Vedadi M, Brown PJ, Nara H, Barsyte-Lovejoy D., Free PMC Article

    09/5/2020
    Our patients provide additional clinical and pathological data and expand the phenotypic manifestations associated with PRMT7 homozygote/compound heterozygote mutations to include brain calcifications and delayed myelination, and congenital orbital tumor.

    Prenatal and postnatal presentation of PRMT7 related syndrome: Expanding the phenotypic manifestations.
    Birnbaum R, Yosha-Orpaz N, Yanoov-Sharav M, Kidron D, Gur H, Yosovich K, Lerman-Sagie T, Malinger G, Lev D.

    02/15/2020
    Our findings expand the clinical and molecular spectrum of homozygous PRMT7 mutations, associated to the SBIDDS syndrome, showing a possible correlation between the type of mutation and the severity of the phenotype.

    Expanding the clinical and molecular spectrum of PRMT7 mutations: 3 additional patients and review.
    Agolini E, Dentici ML, Bellacchio E, Alesi V, Radio FC, Torella A, Musacchia F, Tartaglia M, Dallapiccola B, Nigro V, Digilio MC, Novelli A.

    09/14/2019
    These kinetic studies suggest a biochemical explanation for the interplay between PRMT5- and PRMT7-mediated methylation of the same substrate at different residues and also suggest a general model for regulation of PRMTs.

    Epigenetic control via allosteric regulation of mammalian protein arginine methyltransferases.
    Jain K, Jin CY, Clarke SG., Free PMC Article

    06/9/2018
    The authors showed that ASS1 mutations linked to type I citrullinemia disrupt the ASS1-PRMT7 interaction, which might explain the molecular pathogenesis of the disease.

    PRMT7 Interacts with ASS1 and Citrullinemia Mutations Disrupt the Interaction.
    Verma M, Charles RCM, Chakrapani B, Coumar MS, Govindaraju G, Rajavelu A, Chavali S, Dhayalan A.

    07/29/2017
    Loss of PRMT7 causes decreases in arginine methylation throughout the proteome.Loss of the arginine methyltranserase PRMT7 causes syndromic intellectual disability with microcephaly and brachydactyly.

    Loss of the arginine methyltranserase PRMT7 causes syndromic intellectual disability with microcephaly and brachydactyly.
    Kernohan KD, McBride A, Xi Y, Martin N, Schwartzentruber J, Dyment DA, Majewski J, Blaser S, Care4Rare Canada Consortium, Boycott KM, Chitayat D.

    06/3/2017
    Upregulation of PRMT7 in breast cancer may have a significant role in promoting cell invasion through the regulation of MMP9.

    Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression.
    Baldwin RM, Haghandish N, Daneshmand M, Amin S, Paris G, Falls TJ, Bell JC, Islam S, Côté J., Free PMC Article

    11/28/2015
    results define PRMT7 as an inducer of breast cancer metastasis and present the opportunity for applying PRMT7-targeted therapeutics to treat highly invasive breast cancers

    PRMT7 induces epithelial-to-mesenchymal transition and promotes metastasis in breast cancer.
    Yao R, Jiang H, Ma Y, Wang L, Wang L, Du J, Hou P, Gao Y, Zhao L, Wang G, Zhang Y, Liu DX, Huang B, Lu J.

    03/7/2015
    Data indicate that two acidic residues within the double E loop, Asp-147 and Glu-149, confer specificity to protein arginine methyltransferase 7 (PRMT7.

    Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop.
    Feng Y, Hadjikyriacou A, Clarke SG., Free PMC Article

    02/14/2015
    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.

    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.
    Karkhanis V, Wang L, Tae S, Hu YJ, Imbalzano AN, Sif S., Free PMC Article

    11/24/2012
    Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues.

    Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.
    Zurita-Lopez CI, Sandberg T, Kelly R, Clarke SG., Free PMC Article

    05/5/2012
    Here the authors report that H3R2 is also symmetrically dimethylated (H3R2me2s) by PRMT5 and PRMT7 and present in euchromatic regions.

    Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance.
    Migliori V, Müller J, Phalke S, Low D, Bezzi M, Mok WC, Sahu SK, Gunaratne J, Capasso P, Bassi C, Cecatiello V, De Marco A, Blackstock W, Kuznetsov V, Amati B, Mapelli M, Guccione E.

    03/24/2012
    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.

    Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins.
    Gonsalvez GB, Tian L, Ospina JK, Boisvert FM, Lamond AI, Matera AG., Free PMC Article

    01/21/2010
    PRMT7 (like PRMT5) is a Type II methyltransferase capable of producing symmetric dimethylarginine modifications in proteins.

    PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine.
    Lee JH, Cook JR, Yang ZH, Mirochnitchenko O, Gunderson SI, Felix AM, Herth N, Hoffmann R, Pestka S.

    01/21/2010
    both domains are required for functionality

    PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity.
    Miranda TB, Miranda M, Frankel A, Clarke S.

    01/21/2010
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