The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

PRMT1  -  protein arginine methyltransferase 1

Homo sapiens

Synonyms: ANM1, HCP1, HMT2, HRMT1L2, Histone-arginine N-methyltransferase PRMT1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PRMT1

  • Antisense PRMT1 cDNA constructs expressed under the early cytomegalovirus (CMV) promoter were transfected into HeLa cells, and stable transformants were selected [1].
  • Here we report that several proteins extracted from HeLa cells were methylated by PRMT1 (protein arginine N-methyltransferease 1) even on a nitrocellulose membrane, while proteins from Escherichia coli are not methylated with this protein [2].
  • Although PRMT1 was not found to be hormonally regulated by steroid hormones in breast cancer cells, our results suggest that two variants of PRMT1 are down regulated in breast cancer [3].
  • Our data suggest a novel mechanism by which the protein arginine methyltransferase is involved in the control of AR-driven transcription. p44 expression is dramatically enhanced in prostate cancer tissue compared with adjacent benign prostate tissue [4].
  • The results presented here suggest that decreased DDAH levels as well as increased PRMT gene expression could cause the elevation of plasma ADMA levels, thereby eliciting hypertension in CKD [5].

Psychiatry related information on PRMT1


High impact information on PRMT1


Biological context of PRMT1


Anatomical context of PRMT1

  • Sam68 was also detected in the cytoplasm of PRMT1-deficient embryonic stem cells [15].
  • Flag-IR1B4 fusion proteins bind to the isolated IFNAR1 intracytoplasmic domain produced in Escherichia coli, as well as to the intact IFNAR1 chain extracted by detergent from human U266 cell membranes [16].
  • Remarkably, PRMT1, whose methylation activity on histone H4 strongly correlates with induction of HNF4 target genes in differentiating enterocytes, regulates HNF4 activity through a bipartite mechanism [17].
  • Our results thus reveal the role of a PRMT in protein localization in germ cells [18].
  • All PRMT isoforms investigated were detected at the mRNA and protein level in mouse lung, and were localized primarily to the bronchial and alveolar epithelium [19].

Associations of PRMT1 with chemical compounds

  • A(63-)VLD(-65) to AAA mutation of PRMT1 suppressed the methylation of recombinant SAMT1 and other RGG proteins in the HeLa extracts [2].
  • The methyl transferase PRMT1 functions as co-activator of farnesoid X receptor (FXR)/9-cis retinoid X receptor and regulates transcription of FXR responsive genes [20].
  • Here we describe the crystal structure of rat PRMT1 in complex with the reaction product AdoHcy and a 19 residue substrate peptide containing three arginines [21].
  • Moreover, inhibition of methyltransferase activity, pre-acetylation, or activation of the enzyme PAD4 attenuated retinoid-regulated gene expression, while overexpression of PRMT1, a methyltransferase, enhanced retinoid responsiveness [22].
  • SET-mediated Promoter Hypoacetylation Is a Prerequisite for Coactivation of the Estrogen-responsive pS2 Gene by PRMT1 [23].

Physical interactions of PRMT1


Enzymatic interactions of PRMT1


Regulatory relationships of PRMT1


Other interactions of PRMT1


Analytical, diagnostic and therapeutic context of PRMT1

  • Moreover, PRMT1 and ILF3 co-precipitate in immunoprecipitation assays and can be isolated together in "pull-down" experiments using recombinant fusion proteins [29].
  • Chromatin immunoprecipitation assay suggests that 6-ECDCA induces both the recruitment of PRMT1 and the H4 methylation to the promoter of BSEP and SHP genes [20].
  • Western blot analyses of zebrafish tissue extracts confirmed the expression of some PRMT proteins in zebra fish [10].
  • In summary, our data show that the yeast two-hybrid assay is an effective system for identifying novel PRMT arginine-methylation substrates and may be successfully applied to other members of the growing family of PRMTs [32].
  • Using quantitative real-time PCR, we examined the expression of Hcp1 and other intestinal iron-transporting proteins in male C57BL/6 mice with experimentally altered iron homeostasis [33].


  1. Involvement of receptor-bound protein methyltransferase PRMT1 in antiviral and antiproliferative effects of type I interferons. Altschuler, L., Wook, J.O., Gurari, D., Chebath, J., Revel, M. J. Interferon Cytokine Res. (1999) [Pubmed]
  2. Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy. Wada, K., Inoue, K., Hagiwara, M. Biochim. Biophys. Acta (2002) [Pubmed]
  3. Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene. Scorilas, A., Black, M.H., Talieri, M., Diamandis, E.P. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  4. Purification and identification of a novel complex which is involved in androgen receptor-dependent transcription. Hosohata, K., Li, P., Hosohata, Y., Qin, J., Roeder, R.G., Wang, Z. Mol. Cell. Biol. (2003) [Pubmed]
  5. Molecular mechanism for elevation of asymmetric dimethylarginine and its role for hypertension in chronic kidney disease. Matsuguma, K., Ueda, S., Yamagishi, S., Matsumoto, Y., Kaneyuki, U., Shibata, R., Fujimura, T., Matsuoka, H., Kimoto, M., Kato, S., Imaizumi, T., Okuda, S. J. Am. Soc. Nephrol. (2006) [Pubmed]
  6. Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein. Dolzhanskaya, N., Merz, G., Denman, R.B. Biochemistry (2006) [Pubmed]
  7. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. An, W., Kim, J., Roeder, R.G. Cell (2004) [Pubmed]
  8. Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription. Mowen, K.A., Tang, J., Zhu, W., Schurter, B.T., Shuai, K., Herschman, H.R., David, M. Cell (2001) [Pubmed]
  9. Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor. Wang, H., Huang, Z.Q., Xia, L., Feng, Q., Erdjument-Bromage, H., Strahl, B.D., Briggs, S.D., Allis, C.D., Wong, J., Tempst, P., Zhang, Y. Science (2001) [Pubmed]
  10. Identification and phylogenetic analyses of the protein arginine methyltransferase gene family in fish and ascidians. Hung, C.M., Li, C. Gene (2004) [Pubmed]
  11. Activation of nuclear receptor coactivator PGC-1alpha by arginine methylation. Teyssier, C., Ma, H., Emter, R., Kralli, A., Stallcup, M.R. Genes Dev. (2005) [Pubmed]
  12. Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control. Boisvert, F.M., Déry, U., Masson, J.Y., Richard, S. Genes Dev. (2005) [Pubmed]
  13. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. Frankel, A., Yadav, N., Lee, J., Branscombe, T.L., Clarke, S., Bedford, M.T. J. Biol. Chem. (2002) [Pubmed]
  14. Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. Koh, S.S., Chen, D., Lee, Y.H., Stallcup, M.R. J. Biol. Chem. (2001) [Pubmed]
  15. Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1. Côté, J., Boisvert, F.M., Boulanger, M.C., Bedford, M.T., Richard, S. Mol. Biol. Cell (2003) [Pubmed]
  16. A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor. Abramovich, C., Yakobson, B., Chebath, J., Revel, M. EMBO J. (1997) [Pubmed]
  17. Two functional modes of a nuclear receptor-recruited arginine methyltransferase in transcriptional activation. Barrero, M.J., Malik, S. Mol. Cell (2006) [Pubmed]
  18. Arginine methyltransferase Capsuleen is essential for methylation of spliceosomal Sm proteins and germ cell formation in Drosophila. Anne, J., Ollo, R., Ephrussi, A., Mechler, B.M. Development (2007) [Pubmed]
  19. Increased protein arginine methylation in chronic hypoxia: role of protein arginine methyltransferases. Yildirim, A.O., Bulau, P., Zakrzewicz, D., Kitowska, K.E., Weissmann, N., Grimminger, F., Morty, R.E., Eickelberg, O. Am. J. Respir. Cell Mol. Biol. (2006) [Pubmed]
  20. The methyl transferase PRMT1 functions as co-activator of farnesoid X receptor (FXR)/9-cis retinoid X receptor and regulates transcription of FXR responsive genes. Rizzo, G., Renga, B., Antonelli, E., Passeri, D., Pellicciari, R., Fiorucci, S. Mol. Pharmacol. (2005) [Pubmed]
  21. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Zhang, X., Cheng, X. Structure (Camb.) (2003) [Pubmed]
  22. Arginine methylation provides epigenetic transcription memory for retinoid-induced differentiation in myeloid cells. Balint, B.L., Szanto, A., Madi, A., Bauer, U.M., Gabor, P., Benko, S., Puskás, L.G., Davies, P.J., Nagy, L. Mol. Cell. Biol. (2005) [Pubmed]
  23. SET-mediated Promoter Hypoacetylation Is a Prerequisite for Coactivation of the Estrogen-responsive pS2 Gene by PRMT1. Wagner, S., Weber, S., Kleinschmidt, M.A., Nagata, K., Bauer, U.M. J. Biol. Chem. (2006) [Pubmed]
  24. The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity. Boisvert, F.M., Rhie, A., Richard, S., Doherty, A.J. Cell Cycle (2005) [Pubmed]
  25. Methylation of DNA polymerase beta by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen. El-Andaloussi, N., Valovka, T., Toueille, M., Hassa, P.O., Gehrig, P., Covic, M., H??bscher, U., Hottiger, M.O. FASEB J. (2007) [Pubmed]
  26. Protein N-arginine methylation in subcellular fractions of lymphoblastoid cells. Lin, C.H., Hsieh, M., Li, Y.C., Li, S.Y., Pearson, D.L., Pollard, K.M., Li, C. J. Biochem. (2000) [Pubmed]
  27. Asymmetric Arginine Dimethylation of Heterogeneous Nuclear Ribonucleoprotein K by Protein-arginine Methyltransferase 1 Inhibits Its Interaction with c-Src. Ostareck-Lederer, A., Ostareck, D.H., Rucknagel, K.P., Schierhorn, A., Moritz, B., Huttelmaier, S., Flach, N., Handoko, L., Wahle, E. J. Biol. Chem. (2006) [Pubmed]
  28. Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. Rho, J., Choi, S., Seong, Y.R., Cho, W.K., Kim, S.H., Im, D.S. J. Biol. Chem. (2001) [Pubmed]
  29. Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3. Tang, J., Kao, P.N., Herschman, H.R. J. Biol. Chem. (2000) [Pubmed]
  30. 53BP1 oligomerization is independent of its methylation by PRMT1. Adams, M.M., Wang, B., Xia, Z., Morales, J.C., Lu, X., Donehower, L.A., Bochar, D.A., Elledge, S.J., Carpenter, P.B. Cell Cycle (2005) [Pubmed]
  31. PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine. Lee, J.H., Cook, J.R., Yang, Z.H., Mirochnitchenko, O., Gunderson, S.I., Felix, A.M., Herth, N., Hoffmann, R., Pestka, S. J. Biol. Chem. (2005) [Pubmed]
  32. Ki-1/57 interacts with PRMT1 and is a substrate for arginine methylation. Passos, D.O., Bressan, G.C., Nery, F.C., Kobarg, J. FEBS J. (2006) [Pubmed]
  33. Effect of lipopolysaccharide and bleeding on the expression of intestinal proteins involved in iron and haem transport. Krijt, J., Vokurka, M., Sefc, L., Duricov??, D., Necas, E. Folia Biol. (Praha) (2006) [Pubmed]
WikiGenes - Universities