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PRMT1

From Wikipedia, the free encyclopedia

PRMT1
Identifiers
AliasesPRMT1, ANM1, HCP1, HRMT1L2, IR1B4, protein arginine methyltransferase 1
External IDsOMIM: 602950; MGI: 107846; HomoloGene: 21477; GeneCards: PRMT1; OMA:PRMT1 - orthologs
EC number2.1.1.321
Orthologs
SpeciesHumanMouse
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 MbChr 7: 44.63 – 44.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein arginine N-methyltransferase 1 is an enzyme that in humans is encoded by the PRMT1 gene.[5] The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4.[6]

Function

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PRMT1 gene encodes for the protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4 in eukaryotic cells.[6] Specifically altering histone H4 in eukaryotes gives it the ability to remodel chromatin acting as a post-translational modifier.[7]

Through regulation of gene expression, arginine methyltransferases control the cell cycle and death of eukaryotic cells.[7]

Reaction pathway

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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.[8] 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.[8]

Clinical significance

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In humans, these enzymes regulate gene expression and hence are involved in pathogenesis of many human diseases.[9] Using enzyme inhibitors for arginine methyltransferase 1, studies were able to demonstrate the enzyme's potential as an early catalyst of various cancers.[9][8][10]

Interactions

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PRMT1 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000126457 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: PRMT1 protein arginine methyltransferase 1".
  7. ^ a b 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. ^ a b c 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b c 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. ^ a b 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. ^ a b 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

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