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PRMT1
Identifiers
Aliases	PRMT1, ANM1, HCP1, HRMT1L2, IR1B4, protein arginine methyltransferase 1
External IDs	OMIM: 602950; MGI: 107846; HomoloGene: 21477; GeneCards: PRMT1; OMA:PRMT1 - orthologs
EC number	2.1.1.321
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.33 Start 49,675,786 bp End 49,689,029 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 B3|7 29.07 cM Start 44,625,413 bp End 44,635,992 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in embryo right uterine tube ganglionic eminence anterior pituitary body of uterus canal of the cervix muscle of thigh right hemisphere of cerebellum left uterine tube right ovary Top expressed in abdominal wall mandibular prominence ventricular zone maxillary prominence medial ganglionic eminence hand yolk sac somite dermis tail of embryo More reference expression data BioGPS More reference expression data
Gene ontology Molecular function methyltransferase activity histone methyltransferase activity transferase activity histone methyltransferase activity (H4-R3 specific) methyl-CpG binding mitogen-activated protein kinase p38 binding protein binding identical protein binding enzyme binding N-methyltransferase activity protein-arginine omega-N asymmetric methyltransferase activity RNA binding protein methyltransferase activity protein-arginine N-methyltransferase activity histone-arginine N-methyltransferase activity protein-arginine omega-N monomethyltransferase activity S-adenosyl-L-methionine binding Cellular component cytoplasm nucleoplasm methylosome nucleus cytosol Biological process positive regulation of p38MAPK cascade positive regulation of hemoglobin biosynthetic process histone H4-R3 methylation positive regulation of erythrocyte differentiation negative regulation of megakaryocyte differentiation cell surface receptor signaling pathway methylation peptidyl-arginine methylation histone methylation neuron projection development peptidyl-arginine N-methylation peptidyl-arginine methylation, to asymmetrical-dimethyl arginine DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest regulation of transcription, DNA-templated protein methylation positive regulation of cell population proliferation regulation of megakaryocyte differentiation in utero embryonic development histone arginine methylation protein homooligomerization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3276 15469 Ensembl ENSG00000126457 ENSMUSG00000109324 UniProt Q99873 Q9JIF0 RefSeq (mRNA) NM_001207042 NM_001536 NM_198318 NM_198319 NM_001252476 NM_001252477 NM_019830 RefSeq (protein) NP_001193971 NP_001527 NP_938074 NP_001239405 NP_001239406 NP_062804 Location (UCSC) Chr 19: 49.68 – 49.69 Mb Chr 7: 44.63 – 44.64 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Protein arginine N-methyltransferase 1 is an enzyme that in humans is encoded by the PRMT1 gene. The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4.

Function

PRMT1 gene encodes for the protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4 in eukaryotic cells. Specifically altering histone H4 in eukaryotes gives it the ability to remodel chromatin acting as a post-translational modifier.

Through regulation of gene expression, arginine methyltransferases control the cell cycle and death of eukaryotic cells.

Reaction pathway

While all PRMT enzymes catalyze the methylation of arginine residues in proteins, PRMT1 is unique in that is catalyzes the formation of asymmetric dimethylarginine as opposed to the PRMT2 that catalyzes the formation of symmetrically dimethylated arginine. Individual PRMT utilize S-adenosyl-L-methionine (SAM) as the methyl donor and catalyze methyl group transfer to the ω-nitrogen of an arginine residue.

Clinical significance

In humans, these enzymes regulate gene expression and hence are involved in pathogenesis of many human diseases. Using enzyme inhibitors for arginine methyltransferase 1, studies were able to demonstrate the enzyme's potential as an early catalyst of various cancers.

Interactions

PRMT1 has been shown to interact with:

• BTG1,
• BTG2,
• DHX9,
• FUS,
• HNRNPR,
• HNRPK,
• IFNAR1,
• ILF3,
• KHDRBS1, and
• SUPT5H.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000126457 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000109324 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Scott HS, Antonarakis SE, Lalioti MD, Rossier C, Silver PA, Henry MF (June 1998). "Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)". Genomics. 48 (3): 330–40. doi:10.1006/geno.1997.5190. PMID 9545638.
6. ^ "Entrez Gene: PRMT1 protein arginine methyltransferase 1".
7. ^ Qian K, Zhen G (2016-01-01). "Chapter 8 - Current Development of Protein Arginine Methyltransferase Inhibitors". In Medina-Franco JL (ed.). Epi-Informatics. Boston: Academic Press. pp. 231–256. doi:10.1016/b978-0-12-802808-7.00008-3. ISBN 978-0-12-802808-7.
8. ^ Obianyo O, Osborne TC, Thompson PR (September 2008). "Kinetic mechanism of protein arginine methyltransferase 1". Biochemistry. 47 (39): 10420–7. doi:10.1021/bi800904m. PMC 2933744. PMID 18771293.
9. ^ Zeng H, Xu W (2015-01-01). "Chapter 16 - Enzymatic Assays of Histone Methyltransferase Enzymes". In Zheng YG (ed.). Epigenetic Technological Applications. Boston: Academic Press. pp. 333–361. doi:10.1016/b978-0-12-801080-8.00016-8. ISBN 978-0-12-801080-8.
10. Carbone F, Montecucco F, Xu S, Banach M, Jamialahmadi T, Sahebkar A (August 2020). "Epigenetics in atherosclerosis: key features and therapeutic implications". Expert Opinion on Therapeutic Targets. 24 (8): 719–721. doi:10.1080/14728222.2020.1764535. PMID 32354276.
11. ^ Lin WJ, Gary JD, Yang MC, Clarke S, Herschman HR (June 1996). "The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase". J. Biol. Chem. 271 (25): 15034–44. doi:10.1074/jbc.271.25.15034. PMID 8663146.
12. ^ Berthet C, Guéhenneux F, Revol V, Samarut C, Lukaszewicz A, Dehay C, Dumontet C, Magaud JP, Rouault JP (January 2002). "Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects". Genes Cells. 7 (1): 29–39. doi:10.1046/j.1356-9597.2001.00497.x. PMID 11856371. S2CID 15016952.
13. Smith WA, Schurter BT, Wong-Staal F, David M (May 2004). "Arginine methylation of RNA helicase a determines its subcellular localization". J. Biol. Chem. 279 (22): 22795–8. doi:10.1074/jbc.C300512200. PMID 15084609.
14. ^ Lee J, Bedford MT (March 2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Rep. 3 (3): 268–73. doi:10.1093/embo-reports/kvf052. PMC 1084016. PMID 11850402.
15. ^ Wada K, Inoue K, Hagiwara M (August 2002). "Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy". Biochim. Biophys. Acta. 1591 (1–3): 1–10. doi:10.1016/s0167-4889(02)00202-1. PMID 12183049.
16. ^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
17. ^ Côté J, Boisvert FM, Boulanger MC, Bedford MT, Richard S (January 2003). "Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1". Mol. Biol. Cell. 14 (1): 274–87. doi:10.1091/mbc.E02-08-0484. PMC 140244. PMID 12529443.
18. Abramovich C, Yakobson B, Chebath J, Revel M (January 1997). "A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor". EMBO J. 16 (2): 260–6. doi:10.1093/emboj/16.2.260. PMC 1169633. PMID 9029147.
19. Tang J, Kao PN, Herschman HR (June 2000). "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. 275 (26): 19866–76. doi:10.1074/jbc.M000023200. PMID 10749851.
20. Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB (April 2003). "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties". Mol. Cell. 11 (4): 1055–66. doi:10.1016/s1097-2765(03)00101-1. PMID 12718890.

Further reading

• Kim S, Park GH, Paik WK (1999). "Recent advances in protein methylation: enzymatic methylation of nucleic acid binding proteins". Amino Acids. 15 (4): 291–306. doi:10.1007/BF01320895. PMID 9891755. S2CID 28412209.
• Baldwin GS, Carnegie PR (1971). "Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin". Science. 171 (3971): 579–81. Bibcode:1971Sci...171..579B. doi:10.1126/science.171.3971.579. PMID 4924231. S2CID 36959912.
• Rajpurohit R, Lee SO, Park JO, Paik WK, Kim S (1994). "Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase". J. Biol. Chem. 269 (2): 1075–82. doi:10.1016/S0021-9258(17)42223-X. PMID 8288564.
• Lin WJ, Gary JD, Yang MC, Clarke S, Herschman HR (1996). "The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase". J. Biol. Chem. 271 (25): 15034–44. doi:10.1074/jbc.271.25.15034. PMID 8663146.
• Nikawa J, Nakano H, Ohi N (1996). "Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant". Gene. 171 (1): 107–11. doi:10.1016/0378-1119(96)00073-X. PMID 8675017.
• Abramovich C, Yakobson B, Chebath J, Revel M (1997). "A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor". EMBO J. 16 (2): 260–6. doi:10.1093/emboj/16.2.260. PMC 1169633. PMID 9029147.
• Klein S, Carroll JA, Chen Y, Henry MF, Henry PA, Ortonowski IE, Pintucci G, Beavis RC, Burgess WH, Rifkin DB (2000). "Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2". J. Biol. Chem. 275 (5): 3150–7. doi:10.1074/jbc.275.5.3150. PMID 10652299.
• Tang J, Kao PN, Herschman HR (2000). "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. 275 (26): 19866–76. doi:10.1074/jbc.M000023200. PMID 10749851.
• Nichols RC, Wang XW, Tang J, Hamilton BJ, High FA, Herschman HR, Rigby WF (2000). "The RGG domain in hnRNP A2 affects subcellular localization". Exp. Cell Res. 256 (2): 522–32. doi:10.1006/excr.2000.4827. PMID 10772824.
• Zhang X, Zhou L, Cheng X (2000). "Crystal structure of the conserved core of protein arginine methyltransferase PRMT3". EMBO J. 19 (14): 3509–19. doi:10.1093/emboj/19.14.3509. PMC 313989. PMID 10899106.
• Koh SS, Chen D, Lee YH, Stallcup MR (2001). "Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities". J. Biol. Chem. 276 (2): 1089–98. doi:10.1074/jbc.M004228200. PMID 11050077.
• Scorilas A, Black MH, Talieri M, Diamandis EP (2001). "Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene". Biochem. Biophys. Res. Commun. 278 (2): 349–59. doi:10.1006/bbrc.2000.3807. PMID 11097842.
• Rho J, Choi S, Seong YR, Cho WK, Kim SH, Im DS (2001). "Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family". J. Biol. Chem. 276 (14): 11393–401. doi:10.1074/jbc.M008660200. PMID 11152681.
• Mowen KA, Tang J, Zhu W, Schurter BT, Shuai K, Herschman HR, David M (2001). "Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription". Cell. 104 (5): 731–41. doi:10.1016/S0092-8674(01)00269-0. PMID 11257227. S2CID 17584895.
• Wang H, Huang ZQ, Xia L, Feng Q, Erdjument-Bromage H, Strahl BD, Briggs SD, Allis CD, Wong J, Tempst P, Zhang Y (2001). "Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor". Science. 293 (5531): 853–7. doi:10.1126/science.1060781. PMID 11387442. S2CID 33566292.
• Strahl BD, Briggs SD, Brame CJ, Caldwell JA, Koh SS, Ma H, Cook RG, Shabanowitz J, Hunt DF, Stallcup MR, Allis CD (2001). "Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1". Curr. Biol. 11 (12): 996–1000. Bibcode:2001CBio...11..996S. doi:10.1016/S0960-9822(01)00294-9. PMID 11448779. S2CID 17783289.
• Rho J, Choi S, Seong YR, Choi J, Im DS (2001). "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". J. Virol. 75 (17): 8031–44. doi:10.1128/JVI.75.17.8031-8044.2001. PMC 115047. PMID 11483748.
• Lee J, Bedford MT (2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Rep. 3 (3): 268–73. doi:10.1093/embo-reports/kvf052. PMC 1084016. PMID 11850402.

External links

• Overview of all the structural information available in the PDB for UniProt: Q99873 (Protein arginine N-methyltransferase 1) at the PDBe-KB.

• Genes on human chromosome 19
• Genes mutated in mice