U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    PRMT3 protein arginine methyltransferase 3 [ Homo sapiens (human) ]

    Gene ID: 10196, updated on 10-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    PRMT3-Mediated Arginine Methylation of METTL14 Promotes Malignant Progression and Treatment Resistance in Endometrial Carcinoma.

    PRMT3-Mediated Arginine Methylation of METTL14 Promotes Malignant Progression and Treatment Resistance in Endometrial Carcinoma.
    Wang Y, Wang C, Guan X, Ma Y, Zhang S, Li F, Yin Y, Sun Z, Chen X, Yin H., Free PMC Article

    01/4/2024
    PRMT3 regulates the progression of invasive micropapillary carcinoma of the breast.

    PRMT3 regulates the progression of invasive micropapillary carcinoma of the breast.
    Zhi R, Wu K, Zhang J, Liu H, Niu C, Li S, Fu L., Free PMC Article

    05/5/2023
    PRMT3-mediated arginine methylation of IGF2BP1 promotes oxaliplatin resistance in liver cancer.

    PRMT3-mediated arginine methylation of IGF2BP1 promotes oxaliplatin resistance in liver cancer.
    Shi Y, Niu Y, Yuan Y, Li K, Zhong C, Qiu Z, Li K, Lin Z, Yang Z, Zuo D, Qiu J, He W, Wang C, Liao Y, Wang G, Yuan Y, Li B., Free PMC Article

    04/12/2023
    Protein arginine methyltransferase 3: A crucial regulator in metabolic reprogramming and gene expression in cancers.

    Protein arginine methyltransferase 3: A crucial regulator in metabolic reprogramming and gene expression in cancers.
    Hsu SH, Hung WC.

    01/14/2023
    Decreased nitric oxide content mediated by asymmetrical dimethylarginine and protein l-arginine methyltransferase 3 in macrophages induces trophoblast apoptosis: a potential cause of recurrent miscarriage.

    Decreased nitric oxide content mediated by asymmetrical dimethylarginine and protein l-arginine methyltransferase 3 in macrophages induces trophoblast apoptosis: a potential cause of recurrent miscarriage.
    Hao F, Tang LC, Sun JX, Li WX, Zhao Y, Xu XH, Jin LP.

    03/5/2022
    PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting retinoic acid signaling.

    PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting retinoic acid signaling.
    Verma M, Khan MIK, Kadumuri RV, Chakrapani B, Awasthi S, Mahesh A, Govindaraju G, Chavali PL, Rajavelu A, Chavali S, Dhayalan A., Free PMC Article

    08/21/2021
    Arginine methyltransferase PRMT3 promote tumorigenesis through regulating c-MYC stabilization in colorectal cancer.

    Arginine methyltransferase PRMT3 promote tumorigenesis through regulating c-MYC stabilization in colorectal cancer.
    Hu Y, Su Y, He Y, Liu W, Xiao B.

    07/10/2021
    PRMT3 is an essential regulator of mesenchymal stem cell-mediated osteogenesis and bone homeostasis.

    Asymmetrical methyltransferase PRMT3 regulates human mesenchymal stem cell osteogenesis via miR-3648.
    Min Z, Xiaomeng L, Zheng L, Yangge D, Xuejiao L, Longwei L, Xiao Z, Yunsong L, Ping Z, Yongsheng Z., Free PMC Article

    07/18/2020
    ZNF277 and PRMT3 compete for uS5 binding, because overexpression of PRMT3 inhibited the formation of the ZNF277-uS5 complex, whereas depletion of cellular ZNF277 resulted in increased levels of uS5-PRMT3.

    The 40S ribosomal protein uS5 (RPS2) assembles into an extraribosomal complex with human ZNF277 that competes with the PRMT3-uS5 interaction.
    Dionne KL, Bergeron D, Landry-Voyer AM, Bachand F., Free PMC Article

    06/29/2019
    Findings uncover the existence of an extra-ribosomal complex consisting of PDCD2L, RPS2, and PRMT3 and support a role for PDCD2L in the late maturation of 40S ribosomal subunits.

    Human PDCD2L Is an Export Substrate of CRM1 That Associates with 40S Ribosomal Subunit Precursors.
    Landry-Voyer AM, Bilodeau S, Bergeron D, Dionne KL, Port SA, Rouleau C, Boisvert FM, Kehlenbach RH, Bachand F., Free PMC Article

    06/24/2017
    PRMT3 translocation by palmitic acid is coupled to the binding of LXRalpha, which is responsible for the onset of fatty liver.

    PRMT3 regulates hepatic lipogenesis through direct interaction with LXRα.
    Kim DI, Park MJ, Lim SK, Park JI, Yoon KC, Han HJ, Gustafsson JÅ, Lim JH, Park SH.

    03/21/2015
    This work profilies substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues.

    Profiling substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues.
    Guo H, Wang R, Zheng W, Chen Y, Blum G, Deng H, Luo M., Free PMC Article

    10/18/2014
    Mutational defects in PRMT3 is not the cause of frontotemporal lobar degeneration.

    Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS.
    Ravenscroft TA, Baker MC, Rutherford NJ, Neumann M, Mackenzie IR, Josephs KA, Boeve BF, Petersen R, Halliday GM, Kril J, van Swieten JC, Seeley WW, Dickson DW, Rademakers R., Free PMC Article

    01/18/2014
    results show that protein arginine methyl transferase (PRMT)-3 and -5 methylate NaV1.5 in vitro, interact with NaV1.5 in human embryonic kidney (HEK) cells, and increase NaV1.5 current density

    Protein arginine methyl transferases-3 and -5 increase cell surface expression of cardiac sodium channel.
    Beltran-Alvarez P, Espejo A, Schmauder R, Beltran C, Mrowka R, Linke T, Batlle M, Pérez-Villa F, Pérez GJ, Scornik FS, Benndorf K, Pagans S, Zimmer T, Brugada R.

    11/16/2013
    The crystal structure of PRMT3 in complex with an inhibitor as well as kinetic analysis reveals an allosteric site of inhibition.

    An allosteric inhibitor of protein arginine methyltransferase 3.
    Siarheyeva A, Senisterra G, Allali-Hassani A, Dong A, Dobrovetsky E, Wasney GA, Chau I, Marcellus R, Hajian T, Liu F, Korboukh I, Smil D, Bolshan Y, Min J, Wu H, Zeng H, Loppnau P, Poda G, Griffin C, Aman A, Brown PJ, Jin J, Al-Awar R, Arrowsmith CH, Schapira M, Vedadi M.

    12/29/2012
    release of VHL30 from the E3 ligase complex, promotes the binding of VHL30 to a protein arginine methyltransferase, PRMT3

    Proteomic dissection of the von Hippel-Lindau (VHL) interactome.
    Lai Y, Song M, Hakala K, Weintraub ST, Shiio Y., Free PMC Article

    03/10/2012
    The Tyr87Cys and Tyr87Glu-PRMT3 variants had markedly decreased affinity to ribosomal protein S2 and, consequently, reduced enzymatic activity compared to the wild-type enzyme.

    Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3).
    Handrkova H, Petrak J, Halada P, Pospisilova D, Cmejla R.

    03/19/2011
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
    Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium., Free PMC Article

    09/15/2010
    results suggest that the pathological mutation in the PABPN1 gene alters the protein conformation and induces a preferential interaction with type I PRMTs and Hsp70 chaperones

    Hsp70 chaperones and type I PRMTs are sequestered at intranuclear inclusions caused by polyalanine expansions in PABPN1.
    Tavanez JP, Bengoechea R, Berciano MT, Lafarga M, Carmo-Fonseca M, Enguita FJ., Free PMC Article

    01/21/2010
    Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively

    Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively.
    Kölbel K, Ihling C, Bellmann-Sickert K, Neundorf I, Beck-Sickinger AG, Sinz A, Kühn U, Wahle E., Free PMC Article

    01/21/2010
    DAL-1/4.1B protein significantly inhibits PRMT3 methylation of cellular substrates, which may affect mechanism through which DAL-1/4.1B affects tumor cell growth.

    DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo.
    Singh V, Miranda TB, Jiang W, Frankel A, Roemer ME, Robb VA, Gutmann DH, Herschman HR, Clarke S, Newsham IF.

    01/21/2010
    PRMT3 is a ribosomal protein methyltransferase that affects the cellular level of ribosomal subunits.

    PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits.
    Bachand F, Silver PA., Free PMC Article

    01/21/2010
    firstprevious page of 1 nextlast