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RNMT
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3BGV, 3EPP, 5E9J, 5E9W, 5E8J
Identifiers
Aliases	RNMT, MET, RG7MT1, hCMT1c, CMT1, CMT1c, cm1p, hCMT1, hMet, MRNA-methyltransferase, RNA guanine-7 methyltransferase, N7-MTase
External IDs	OMIM: 603514; MGI: 1915147; HomoloGene: 2816; GeneCards: RNMT; OMA:RNMT - orthologs
Gene location (Human) Chr. Chromosome 18 (human) Band 18p11.21 Start 13,726,660 bp End 13,764,556 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 E2 Start 68,433,426 bp End 68,457,923 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle amniotic fluid lateral nuclear group of thalamus middle temporal gyrus Brodmann area 23 pars compacta tendon Achilles tendon cartilage tissue internal globus pallidus Top expressed in secondary oocyte morula zygote epiblast primitive streak embryo substantia nigra blastocyst dentate gyrus of hippocampal formation granule cell tail of embryo More reference expression data BioGPS More reference expression data
Gene ontology Molecular function methyltransferase activity transferase activity mRNA (guanine-N7-)-methyltransferase activity protein binding RNA binding Cellular component mRNA cap binding complex receptor complex nucleus nucleoplasm fibrillar center mRNA cap methyltransferase complex Biological process mRNA processing methylation transcription by RNA polymerase II RNA 5'-cap (guanine-N7)-methylation cellular response to leukemia inhibitory factor 7-methylguanosine mRNA capping Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8731 67897 Ensembl ENSG00000101654 ENSMUSG00000009535 UniProt O43148 Q9D0L8 RefSeq (mRNA) NM_001308263 NM_003799 NM_001378132 NM_001378134 NM_001378135 NM_001170953 NM_026440 NM_001361002 NM_001361003 RefSeq (protein) NP_001295192 NP_003790 NP_001365061 NP_001365063 NP_001365064 NP_001164424 NP_080716 NP_001347931 NP_001347932 Location (UCSC) Chr 18: 13.73 – 13.76 Mb Chr 18: 68.43 – 68.46 Mb PubMed search
Wikidata
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In enzymology, a mRNA (guanine-N7-)-methyltransferase also known as mRNA cap guanine-N7 methyltransferase is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + G(5')pppR-RNA ${\displaystyle \rightleftharpoons }$ S-adenosyl-L-homocysteine + m₇G(5')pppR-RNA (mRNA containing an N-methylguanine cap)

Thus, the two substrates of this enzyme are S-adenosyl methionine and G(5')pppR-RNA, whereas its two products are S-adenosylhomocysteine and m7G(5')pppR-RNA. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases.

In humans, mRNA cap guanine-N7 methyltransferase is encoded by the RNMT gene.

Nomenclature

The systematic name of this enzyme class is S-adenosyl-L-methionine:mRNA (guanine-N7-)-methyltransferase. Other names in common use include:

• messenger ribonucleate guanine 7-methyltransferase,
• guanine-7-methyltransferase,
• messenger RNA guanine 7-methyltransferase, and
• S-adenosyl-L-methionine:mRNA (guanine-7-N-)-methyltransferase.
• cap MTase

See also

• 7-Methylguanosine

References

1. ^ GRCh38: Ensembl release 89: ENSG00000101654 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000009535 – 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. Pillutla RC, Shimamoto A, Furuichi Y, Shatkin AJ (Jan 1999). "Human mRNA capping enzyme (RNGTT) and cap methyltransferase (RNMT) map to 6q16 and 18p11.22-p11.23, respectively". Genomics. 54 (2): 351–3. doi:10.1006/geno.1998.5604. PMID 9828141.
6. Pillutla RC, Yue Z, Maldonado E, Shatkin AJ (Sep 1998). "Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes". J Biol Chem. 273 (34): 21443–6. doi:10.1074/jbc.273.34.21443. PMID 9705270.
7. "Entrez Gene: RNMT RNA (guanine-7-) methyltransferase".

Further reading

• Ensinger MJ, Martin SA, Paoletti E, Moss B (1975). "Modification of the 5'-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus". Proc. Natl. Acad. Sci. U.S.A. 72 (7): 2525–9. Bibcode:1975PNAS...72.2525E. doi:10.1073/pnas.72.7.2525. PMC 432801. PMID 1058472.
• Groner Y, Gilboa E, Aviv H (1978). "Methylation and capping of RNA polymerase II primary transcripts by HeLa nuclear homogenates". Biochemistry. 17 (6): 977–82. doi:10.1021/bi00599a005. PMID 629955.
• Martin SA, Moss B (1975). "Modification of RNA by mRNA guanylyltransferase and mRNA (guanine-7-)methyltransferase from vaccinia virions". J. Biol. Chem. 250 (24): 9330–5. doi:10.1016/S0021-9258(19)40647-9. PMID 1194287.
• Martin SA, Paoletti E, Moss B (1975). "Purification of mRNA guanylyltransferase and mRNA (guanine-7-) methyltransferase from vaccinia virions". J. Biol. Chem. 250 (24): 9322–9. doi:10.1016/S0021-9258(19)40646-7. PMID 1194286.
• Langberg SR, Moss B (1981). "Post-transcriptional modifications of mRNA. Purification and characterization of cap I and cap II RNA (nucleoside-2'-)-methyltransferases from HeLa cells". J. Biol. Chem. 256 (19): 10054–60. doi:10.1016/S0021-9258(19)68740-5. PMID 7275966.
• Ishikawa K, Nagase T, Nakajima D, et al. (1998). "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 4 (5): 307–13. doi:10.1093/dnares/4.5.307. PMID 9455477.
• Tsukamoto T, Shibagaki Y, Niikura Y, Mizumoto K (1998). "Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase". Biochem. Biophys. Res. Commun. 251 (1): 27–34. doi:10.1006/bbrc.1998.9402. PMID 9790902.
• Saha N, Schwer B, Shuman S (1999). "Characterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes". J. Biol. Chem. 274 (23): 16553–62. doi:10.1074/jbc.274.23.16553. PMID 10347220.
• Yamada-Okabe T, Mio T, Kashima Y, et al. (2000). "The Candida albicans gene for mRNA 5-cap methyltransferase: identification of additional residues essential for catalysis". Microbiology. 145 (11): 3023–33. doi:10.1099/00221287-145-11-3023. PMID 10589710.
• Wen Y, Shatkin AJ (2001). "Cap methyltransferase selective binding and methylation of GpppG-RNA are stimulated by importin-α". Genes Dev. 14 (23): 2944–9. doi:10.1101/gad.848200. PMC 317093. PMID 11114884.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Shafer B, Chu C, Shatkin AJ (2005). "Human mRNA Cap Methyltransferase: Alternative Nuclear Localization Signal Motifs Ensure Nuclear Localization Required for Viability". Mol. Cell. Biol. 25 (7): 2644–9. doi:10.1128/MCB.25.7.2644-2649.2005. PMC 1061643. PMID 15767670.

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