9bhd

Structural highlights

Function

ANM1_HUMAN Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4 and SERBP1 (PubMed:10749851, PubMed:16879614, PubMed:26876602). Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates RBM15, promoting ubiquitination and degradation of RBM15 (PubMed:26575292). Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity. Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (PubMed:25284789). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789).^{[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15]}

References

1. ↑ Tang J, Kao PN, Herschman HR. Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3. J Biol Chem. 2000 Jun 30;275(26):19866-76. doi: 10.1074/jbc.M000023200. PMID:10749851 doi:http://dx.doi.org/10.1074/jbc.M000023200
2. ↑ Wang H, Huang ZQ, Xia L, Feng Q, Erdjument-Bromage H, Strahl BD, Briggs SD, Allis CD, Wong J, Tempst P, Zhang Y. Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor. Science. 2001 Aug 3;293(5531):853-7. Epub 2001 May 31. PMID:11387442 doi:http://dx.doi.org/10.1126/science.1060781
3. ↑ Strahl BD, Briggs SD, Brame CJ, Caldwell JA, Koh SS, Ma H, Cook RG, Shabanowitz J, Hunt DF, Stallcup MR, Allis CD. Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1. Curr Biol. 2001 Jun 26;11(12):996-1000. PMID:11448779
4. ↑ Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol Cell. 2003 Apr;11(4):1055-66. PMID:12718890
5. ↑ Passos DO, Bressan GC, Nery FC, Kobarg J. Ki-1/57 interacts with PRMT1 and is a substrate for arginine methylation. FEBS J. 2006 Sep;273(17):3946-61. doi: 10.1111/j.1742-4658.2006.05399.x. Epub, 2006 Jul 19. PMID:16879614 doi:http://dx.doi.org/10.1111/j.1742-4658.2006.05399.x
6. ↑ Pahlich S, Zakaryan RP, Gehring H. Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state. Proteins. 2008 Sep;72(4):1125-37. doi: 10.1002/prot.22004. PMID:18320585 doi:http://dx.doi.org/10.1002/prot.22004
7. ↑ Le Romancer M, Treilleux I, Leconte N, Robin-Lespinasse Y, Sentis S, Bouchekioua-Bouzaghou K, Goddard S, Gobert-Gosse S, Corbo L. Regulation of estrogen rapid signaling through arginine methylation by PRMT1. Mol Cell. 2008 Jul 25;31(2):212-21. doi: 10.1016/j.molcel.2008.05.025. PMID:18657504 doi:http://dx.doi.org/10.1016/j.molcel.2008.05.025
8. ↑ Miyata S, Mori Y, Tohyama M. PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells. Neurosci Lett. 2008 Nov 14;445(2):162-5. doi: 10.1016/j.neulet.2008.08.065. Epub , 2008 Aug 28. PMID:18773938 doi:http://dx.doi.org/10.1016/j.neulet.2008.08.065
9. ↑ Jobert L, Argentini M, Tora L. PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function. Exp Cell Res. 2009 Apr 15;315(7):1273-86. doi: 10.1016/j.yexcr.2008.12.008. Epub , 2008 Dec 24. PMID:19124016 doi:http://dx.doi.org/10.1016/j.yexcr.2008.12.008
10. ↑ Lakowski TM, Frankel A. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Biochem J. 2009 Jun 26;421(2):253-61. doi: 10.1042/BJ20090268. PMID:19405910 doi:10.1042/BJ20090268
11. ↑ Chang YI, Hua WK, Yao CL, Hwang SM, Hung YC, Kuan CJ, Leou JS, Lin WJ. Protein-arginine methyltransferase 1 suppresses megakaryocytic differentiation via modulation of the p38 MAPK pathway in K562 cells. J Biol Chem. 2010 Jul 2;285(27):20595-606. doi: 10.1074/jbc.M109.092411. Epub, 2010 May 4. PMID:20442406 doi:http://dx.doi.org/10.1074/jbc.M109.092411
12. ↑ Takai H, Masuda K, Sato T, Sakaguchi Y, Suzuki T, Suzuki T, Koyama-Nasu R, Nasu-Nishimura Y, Katou Y, Ogawa H, Morishita Y, Kozuka-Hata H, Oyama M, Todo T, Ino Y, Mukasa A, Saito N, Toyoshima C, Shirahige K, Akiyama T. 5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex. Cell Rep. 2014 Oct 9;9(1):48-60. doi: 10.1016/j.celrep.2014.08.071. Epub 2014 Oct, 2. PMID:25284789 doi:http://dx.doi.org/10.1016/j.celrep.2014.08.071
13. ↑ Zhang L, Tran NT, Su H, Wang R, Lu Y, Tang H, Aoyagi S, Guo A, Khodadadi-Jamayran A, Zhou D, Qian K, Hricik T, Cote J, Han X, Zhou W, Laha S, Abdel-Wahab O, Levine RL, Raffel G, Liu Y, Chen D, Li H, Townes T, Wang H, Deng H, Zheng YG, Leslie C, Luo M, Zhao X. Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing. Elife. 2015 Nov 17;4. pii: 07938. doi: 10.7554/eLife.07938. PMID:26575292 doi:http://dx.doi.org/10.7554/eLife.07938
14. ↑ Toma-Fukai S, Kim JD, Park KE, Kuwabara N, Shimizu N, Krayukuhina E, Uchiyama S, Fukamizu A, Shimizu T. Novel helical assembly in arginine methyltransferase 8. J Mol Biol. 2016 Feb 11. pii: S0022-2836(16)00112-1. doi:, 10.1016/j.jmb.2016.02.007. PMID:26876602 doi:http://dx.doi.org/10.1016/j.jmb.2016.02.007
15. ↑ Akter KA, Mansour MA, Hyodo T, Senga T. FAM98A associates with DDX1-C14orf166-FAM98B in a novel complex involved in colorectal cancer progression. Int J Biochem Cell Biol. 2017 Mar;84:1-13. doi: 10.1016/j.biocel.2016.12.013., Epub 2016 Dec 28. PMID:28040436 doi:http://dx.doi.org/10.1016/j.biocel.2016.12.013