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

PRMT2  -  protein arginine methyltransferase 2

Homo sapiens

Synonyms: HMT1, HRMT1L1, Histone-arginine N-methyltransferase PRMT2, MGC111373, Protein arginine N-methyltransferase 2
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 PRMT2

  • These results demonstrate that PRMTs are expressed and functional in the lung, and that hypoxia is a potent regulator of PRMT2 expression and lung ADMA concentrations [1].

High impact information on PRMT2


Biological context of PRMT2


Associations of PRMT2 with chemical compounds

  • PRMT2 enhanced both ERalpha AF-1 and AF-2 transcriptional activity, and the potential methyltransferase activity of PRMT2 appeared pivotal for its coactivator function [4].
  • The arginine methyltransferase PRMT2 binds RB and regulates E2F function [8].

Physical interactions of PRMT2

  • Using yeast two-hybrid screening we identified HRMT1L1 (PRMT2) as one of the proteins interacting with E1B-AP5 [6].

Co-localisations of PRMT2


Other interactions of PRMT2


Analytical, diagnostic and therapeutic context of PRMT2

  • To further explore the role of endogenous PRMT2 in the regulation of E2F activity, the PRMT2 gene was ablated in mice by gene targeting [8].


  1. 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]
  2. Heavy metal tolerance in the fission yeast requires an ATP-binding cassette-type vacuolar membrane transporter. Ortiz, D.F., Kreppel, L., Speiser, D.M., Scheel, G., McDonald, G., Ow, D.W. EMBO J. (1992) [Pubmed]
  3. Protein Methyltransferase 2 Inhibits NF-{kappa}B Function and Promotes Apoptosis. Ganesh, L., Yoshimoto, T., Moorthy, N.C., Akahata, W., Boehm, M., Nabel, E.G., Nabel, G.J. Mol. Cell. Biol. (2006) [Pubmed]
  4. Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. Qi, C., Chang, J., Zhu, Y., Yeldandi, A.V., Rao, S.M., Zhu, Y.J. J. Biol. Chem. (2002) [Pubmed]
  5. Identification and phylogenetic analyses of the protein arginine methyltransferase gene family in fish and ascidians. Hung, C.M., Li, C. Gene (2004) [Pubmed]
  6. Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1. Kzhyshkowska, J., Schütt, H., Liss, M., Kremmer, E., Stauber, R., Wolf, H., Dobner, T. Biochem. J. (2001) [Pubmed]
  7. Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). Scott, H.S., Antonarakis, S.E., Lalioti, M.D., Rossier, C., Silver, P.A., Henry, M.F. Genomics (1998) [Pubmed]
  8. The arginine methyltransferase PRMT2 binds RB and regulates E2F function. Yoshimoto, T., Boehm, M., Olive, M., Crook, M.F., San, H., Langenickel, T., Nabel, E.G. Exp. Cell Res. (2006) [Pubmed]
WikiGenes - Universities