Protein arginine N-methyltransferase 1

NameProtein arginine N-methyltransferase 1
Synonyms
  • 2.1.1.319
  • Histone-arginine N-methyltransferase PRMT1
  • HMT2
  • HRMT1L2
  • Interferon receptor 1-bound protein 4
  • IR1B4
Gene NamePRMT1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0009518|Protein arginine N-methyltransferase 1
MENFVATLANGMSLQPPLEEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDE
VRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIV
KANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLYARDKWLAPDGL
IFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNAC
LIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYT
HWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRM
R
Number of residues361
Molecular Weight41515.2
Theoretical pINot Available
GO Classification
Functions
  • protein-arginine N-methyltransferase activity
  • protein-arginine omega-N asymmetric methyltransferase activity
  • N-methyltransferase activity
  • protein methyltransferase activity
  • histone methyltransferase activity
  • enzyme binding
  • histone methyltransferase activity (H4-R3 specific)
  • mitogen-activated protein kinase p38 binding
  • identical protein binding
  • poly(A) RNA binding
  • methyltransferase activity
Processes
  • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine
  • histone H4-R3 methylation
  • regulation of transcription, DNA-templated
  • histone methylation
  • peptidyl-arginine methylation
  • cell surface receptor signaling pathway
  • positive regulation of hemoglobin biosynthetic process
  • neuron projection development
  • protein methylation
  • negative regulation of megakaryocyte differentiation
  • chromatin organization
  • positive regulation of p38MAPK cascade
  • positive regulation of erythrocyte differentiation
Components
  • nucleus
  • cytosol
  • nucleoplasm
  • cytoplasm
General FunctionProtein-arginine omega-n asymmetric methyltransferase activity
Specific FunctionArginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. 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. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. 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 FOXO1 and retains it in the nucleus increasing its transcriptional activity.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDQ99873
UniProtKB Entry NameANM1_HUMAN
Cellular LocationNucleus
Gene sequenceNot Available
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:5187
Chromosome LocationNot Available
LocusNot Available
References
  1. Scott HS, Antonarakis SE, Lalioti MD, Rossier C, Silver PA, Henry MF: Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). Genomics. 1998 Mar 15;48(3):330-40. 9545638
  2. Nikawa J, Nakano H, Ohi N: Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant. Gene. 1996 May 24;171(1):107-11. 8675017
  3. Scorilas A, Black MH, Talieri M, Diamandis EP: Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene. Biochem Biophys Res Commun. 2000 Nov 19;278(2):349-59. 11097842
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. 14702039
  5. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. 15057824
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  7. 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. 10749851
  8. Weiss VH, McBride AE, Soriano MA, Filman DJ, Silver PA, Hogle JM: The structure and oligomerization of the yeast arginine methyltransferase, Hmt1. Nat Struct Biol. 2000 Dec;7(12):1165-71. 11101900
  9. 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. 11448779
  10. 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. 11387442
  11. 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. 12718890
  12. 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. 18657504
  13. Yamagata K, Daitoku H, Takahashi Y, Namiki K, Hisatake K, Kako K, Mukai H, Kasuya Y, Fukamizu A: Arginine methylation of FOXO transcription factors inhibits their phosphorylation by Akt. Mol Cell. 2008 Oct 24;32(2):221-31. doi: 10.1016/j.molcel.2008.09.013. 18951090
  14. 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. 18773938
  15. 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. 18320585
  16. 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. 19405910
  17. 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. 19124016
  18. Weber S, Maass F, Schuemann M, Krause E, Suske G, Bauer UM: PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling. Genes Dev. 2009 Jan 1;23(1):118-32. doi: 10.1101/gad.489409. 19136629
  19. 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. 20442406
  20. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  21. Kaehler C, Guenther A, Uhlich A, Krobitsch S: PRMT1-mediated arginine methylation controls ATXN2L localization. Exp Cell Res. 2015 May 15;334(1):114-25. doi: 10.1016/j.yexcr.2015.02.022. Epub 2015 Mar 5. 25748791