PRMT1

Protein arginine methyltransferase 1, also known as PRMT1, is a human gene.

PBB_Summary
section_title =
summary_text = The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone methyltransferase specific for H4 (see MIM 602822). [supplied by OMIM] cite web | title = Entrez Gene: PRMT1 protein arginine methyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3276| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Kim S, Park GH, Paik WK |title=Recent advances in protein methylation: enzymatic methylation of nucleic acid binding proteins. |journal=Amino Acids |volume=15 |issue= 4 |pages= 291–306 |year= 1999 |pmid= 9891755 |doi=
*cite journal | author=Baldwin GS, Carnegie PR |title=Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin. |journal=Science |volume=171 |issue= 971 |pages= 579–81 |year= 1971 |pmid= 4924231 |doi=
*cite journal | author=Rajpurohit R, Lee SO, Park JO, "et al." |title=Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase. |journal=J. Biol. Chem. |volume=269 |issue= 2 |pages= 1075–82 |year= 1994 |pmid= 8288564 |doi=
*cite journal | author=Lin WJ, Gary JD, Yang MC, "et al." |title=The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 15034–44 |year= 1996 |pmid= 8663146 |doi=
*cite journal | author=Nikawa J, Nakano H, Ohi N |title=Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant. |journal=Gene |volume=171 |issue= 1 |pages= 107–11 |year= 1996 |pmid= 8675017 |doi=
*cite journal | author=Abramovich C, Yakobson B, Chebath J, Revel M |title=A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor. |journal=EMBO J. |volume=16 |issue= 2 |pages= 260–6 |year= 1997 |pmid= 9029147 |doi= 10.1093/emboj/16.2.260
*cite journal | author=Scott HS, Antonarakis SE, Lalioti MD, "et al." |title=Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). |journal=Genomics |volume=48 |issue= 3 |pages= 330–40 |year= 1998 |pmid= 9545638 |doi= 10.1006/geno.1997.5190
*cite journal | author=Klein S, Carroll JA, Chen Y, "et al." |title=Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2. |journal=J. Biol. Chem. |volume=275 |issue= 5 |pages= 3150–7 |year= 2000 |pmid= 10652299 |doi=
*cite journal | author=Tang J, Kao PN, Herschman HR |title=Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19866–76 |year= 2000 |pmid= 10749851 |doi= 10.1074/jbc.M000023200
*cite journal | author=Nichols RC, Wang XW, Tang J, "et al." |title=The RGG domain in hnRNP A2 affects subcellular localization. |journal=Exp. Cell Res. |volume=256 |issue= 2 |pages= 522–32 |year= 2000 |pmid= 10772824 |doi= 10.1006/excr.2000.4827
*cite journal | author=Zhang X, Zhou L, Cheng X |title=Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. |journal=EMBO J. |volume=19 |issue= 14 |pages= 3509–19 |year= 2000 |pmid= 10899106 |doi= 10.1093/emboj/19.14.3509
*cite journal | author=Koh SS, Chen D, Lee YH, Stallcup MR |title=Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. |journal=J. Biol. Chem. |volume=276 |issue= 2 |pages= 1089–98 |year= 2001 |pmid= 11050077 |doi= 10.1074/jbc.M004228200
*cite journal | author=Scorilas A, Black MH, Talieri M, Diamandis EP |title=Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene. |journal=Biochem. Biophys. Res. Commun. |volume=278 |issue= 2 |pages= 349–59 |year= 2001 |pmid= 11097842 |doi= 10.1006/bbrc.2000.3807
*cite journal | author=Rho J, Choi S, Seong YR, "et al." |title=Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. |journal=J. Biol. Chem. |volume=276 |issue= 14 |pages= 11393–401 |year= 2001 |pmid= 11152681 |doi= 10.1074/jbc.M008660200
*cite journal | author=Mowen KA, Tang J, Zhu W, "et al." |title=Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription. |journal=Cell |volume=104 |issue= 5 |pages= 731–41 |year= 2001 |pmid= 11257227 |doi=
*cite journal | author=Wang H, Huang ZQ, Xia L, "et al." |title=Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor. |journal=Science |volume=293 |issue= 5531 |pages= 853–7 |year= 2001 |pmid= 11387442 |doi= 10.1126/science.1060781
*cite journal | author=Strahl BD, Briggs SD, Brame CJ, "et al." |title=Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1. |journal=Curr. Biol. |volume=11 |issue= 12 |pages= 996–1000 |year= 2001 |pmid= 11448779 |doi=
*cite journal | author=Rho J, Choi S, Seong YR, "et al." |title=The arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1. |journal=J. Virol. |volume=75 |issue= 17 |pages= 8031–44 |year= 2001 |pmid= 11483748 |doi=
*cite journal | author=Lee J, Bedford MT |title=PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays. |journal=EMBO Rep. |volume=3 |issue= 3 |pages= 268–73 |year= 2002 |pmid= 11850402 |doi= 10.1093/embo-reports/kvf052

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