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RecName: Full=mRNA cap guanine-N(7) methyltransferase; AltName: Full=RG7MT1; AltName: Full=mRNA (guanine-N(7))-methyltransferase; AltName: Full=mRNA cap methyltransferase

UniProtKB/Swiss-Prot: Q9D0L8.1

Identical Proteins FASTA Graphics 

LOCUS       MCES_MOUSE               465 aa            linear   ROD 27-NOV-2024
DEFINITION  RecName: Full=mRNA cap guanine-N(7) methyltransferase; AltName:
            Full=RG7MT1; AltName: Full=mRNA (guanine-N(7))-methyltransferase;
            AltName: Full=mRNA cap methyltransferase.
ACCESSION   Q9D0L8
VERSION     Q9D0L8.1
DBSOURCE    UniProtKB: locus MCES_MOUSE, accession Q9D0L8;
            class: standard.
            extra accessions:Q3V3U9,Q6ZQC6,Q9D5F1
            created: Sep 5, 2006.
            sequence updated: Jun 1, 2001.
            annotation updated: Nov 27, 2024.
            xrefs: AK129130.1, BAC97940.1, AK011300.1, BAB27527.1, AK015403.1,
            BAB29834.1, AK031780.1, BAE43278.1, BC021794.1, AAH21794.1,
            AK082331.1, BAC38469.1, NP_001164424.1, NP_080716.1,
            XP_006526256.1, XP_006526257.1, XP_006526259.1, XP_006526260.1,
            XP_011245293.1
            xrefs (non-sequence databases): CCDS:CCDS37852.1, CCDS:CCDS50314.1,
            AlphaFoldDB:Q9D0L8, SMR:Q9D0L8, BioGRID:212521, IntAct:Q9D0L8,
            STRING:10090.ENSMUSP00000009679, GlyGen:Q9D0L8, iPTMnet:Q9D0L8,
            PhosphoSitePlus:Q9D0L8, SwissPalm:Q9D0L8, jPOST:Q9D0L8,
            PaxDb:10090-ENSMUSP00000009679, PeptideAtlas:Q9D0L8,
            ProteomicsDB:252743, ProteomicsDB:252744, ProteomicsDB:252745,
            Pumba:Q9D0L8, Antibodypedia:21962, DNASU:67897,
            Ensembl:ENSMUST00000009679.11, Ensembl:ENSMUSP00000009679.5,
            Ensembl:ENSMUSG00000009535.14, Ensembl:ENSMUST00000025427.14,
            Ensembl:ENSMUSP00000025427.8, GeneID:67897, KEGG:mmu:67897,
            UCSC:uc008fnj.2, UCSC:uc012bem.1, AGR:MGI:1915147, CTD:8731,
            MGI:1915147, VEuPathDB:HostDB:ENSMUSG00000009535, eggNOG:KOG1975,
            GeneTree:ENSGT00390000002368, HOGENOM:CLU_020346_0_1_1,
            InParanoid:Q9D0L8, OMA:SHYNTLQ, OrthoDB:167537at2759,
            PhylomeDB:Q9D0L8, TreeFam:TF314347, Reactome:R-MMU-72086,
            Reactome:R-MMU-77075, BioGRID-ORCS:67897, ChiTaRS:Rnmt,
            PRO:PR:Q9D0L8, Proteomes:UP000000589, RNAct:Q9D0L8,
            Bgee:ENSMUSG00000009535, ExpressionAtlas:Q9D0L8, GO:0001650,
            GO:0160130, GO:0031533, GO:0005654, GO:0005634, GO:0043235,
            GO:0004482, GO:0003723, GO:0006370, GO:1990830, CDD:cd02440,
            Gene3D:3.40.50.150, InterPro:IPR004971, InterPro:IPR016899,
            InterPro:IPR039753, InterPro:IPR029063, PANTHER:PTHR12189:SF2,
            PANTHER:PTHR12189, Pfam:PF03291, PIRSF:PIRSF028762,
            SUPFAM:SSF53335, PROSITE:PS51562
KEYWORDS    Alternative splicing; Methyltransferase; mRNA capping; mRNA
            processing; Nucleus; Phosphoprotein; Reference proteome;
            RNA-binding; S-adenosyl-L-methionine; Transferase.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).;
            TISSUE=Brain
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Carninci,P., Kasukawa,T., Katayama,S., Gough,J., Frith,M.C.,
            Maeda,N., Oyama,R., Ravasi,T., Lenhard,B., Wells,C., Kodzius,R.,
            Shimokawa,K., Bajic,V.B., Brenner,S.E., Batalov,S., Forrest,A.R.,
            Zavolan,M., Davis,M.J., Wilming,L.G., Aidinis,V., Allen,J.E.,
            Ambesi-Impiombato,A., Apweiler,R., Aturaliya,R.N., Bailey,T.L.,
            Bansal,M., Baxter,L., Beisel,K.W., Bersano,T., Bono,H., Chalk,A.M.,
            Chiu,K.P., Choudhary,V., Christoffels,A., Clutterbuck,D.R.,
            Crowe,M.L., Dalla,E., Dalrymple,B.P., de Bono,B., Della Gatta,G.,
            di Bernardo,D., Down,T., Engstrom,P., Fagiolini,M., Faulkner,G.,
            Fletcher,C.F., Fukushima,T., Furuno,M., Futaki,S., Gariboldi,M.,
            Georgii-Hemming,P., Gingeras,T.R., Gojobori,T., Green,R.E.,
            Gustincich,S., Harbers,M., Hayashi,Y., Hensch,T.K., Hirokawa,N.,
            Hill,D., Huminiecki,L., Iacono,M., Ikeo,K., Iwama,A., Ishikawa,T.,
            Jakt,M., Kanapin,A., Katoh,M., Kawasawa,Y., Kelso,J., Kitamura,H.,
            Kitano,H., Kollias,G., Krishnan,S.P., Kruger,A., Kummerfeld,S.K.,
            Kurochkin,I.V., Lareau,L.F., Lazarevic,D., Lipovich,L., Liu,J.,
            Liuni,S., McWilliam,S., Madan Babu,M., Madera,M., Marchionni,L.,
            Matsuda,H., Matsuzawa,S., Miki,H., Mignone,F., Miyake,S.,
            Morris,K., Mottagui-Tabar,S., Mulder,N., Nakano,N., Nakauchi,H.,
            Ng,P., Nilsson,R., Nishiguchi,S., Nishikawa,S., Nori,F., Ohara,O.,
            Okazaki,Y., Orlando,V., Pang,K.C., Pavan,W.J., Pavesi,G.,
            Pesole,G., Petrovsky,N., Piazza,S., Reed,J., Reid,J.F., Ring,B.Z.,
            Ringwald,M., Rost,B., Ruan,Y., Salzberg,S.L., Sandelin,A.,
            Schneider,C., Schonbach,C., Sekiguchi,K., Semple,C.A., Seno,S.,
            Sessa,L., Sheng,Y., Shibata,Y., Shimada,H., Shimada,K., Silva,D.,
            Sinclair,B., Sperling,S., Stupka,E., Sugiura,K., Sultana,R.,
            Takenaka,Y., Taki,K., Tammoja,K., Tan,S.L., Tang,S., Taylor,M.S.,
            Tegner,J., Teichmann,S.A., Ueda,H.R., van Nimwegen,E., Verardo,R.,
            Wei,C.L., Yagi,K., Yamanishi,H., Zabarovsky,E., Zhu,S., Zimmer,A.,
            Hide,W., Bult,C., Grimmond,S.M., Teasdale,R.D., Liu,E.T.,
            Brusic,V., Quackenbush,J., Wahlestedt,C., Mattick,J.S., Hume,D.A.,
            Kai,C., Sasaki,D., Tomaru,Y., Fukuda,S., Kanamori-Katayama,M.,
            Suzuki,M., Aoki,J., Arakawa,T., Iida,J., Imamura,K., Itoh,M.,
            Kato,T., Kawaji,H., Kawagashira,N., Kawashima,T., Kojima,M.,
            Kondo,S., Konno,H., Nakano,K., Ninomiya,N., Nishio,T., Okada,M.,
            Plessy,C., Shibata,K., Shiraki,T., Suzuki,S., Tagami,M., Waki,K.,
            Watahiki,A., Okamura-Oho,Y., Suzuki,H., Kawai,J. and Hayashizaki,Y.
  CONSRTM   FANTOM Consortium; RIKEN Genome Exploration Research Group and
            Genome Science Group (Genome Network Project Core Group)
  TITLE     The transcriptional landscape of the mammalian genome
  JOURNAL   Science 309 (5740), 1559-1563 (2005)
   PUBMED   16141072
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).;
            STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Testis
            Erratum:[Science. 2006 Mar 24;311(5768):1713]
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).;
            STRAIN=FVB/N; TISSUE=Colon
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-15, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Embryonic brain
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Villen,J., Beausoleil,S.A., Gerber,S.A. and Gygi,S.P.
  TITLE     Large-scale phosphorylation analysis of mouse liver
  JOURNAL   Proc Natl Acad Sci U S A 104 (5), 1488-1493 (2007)
   PUBMED   17242355
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Liver
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Trost,M., English,L., Lemieux,S., Courcelles,M., Desjardins,M. and
            Thibault,P.
  TITLE     The phagosomal proteome in interferon-gamma-activated macrophages
  JOURNAL   Immunity 30 (1), 143-154 (2009)
   PUBMED   19144319
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Sweet,S.M., Bailey,C.M., Cunningham,D.L., Heath,J.K. and
            Cooper,H.J.
  TITLE     Large scale localization of protein phosphorylation by use of
            electron capture dissociation mass spectrometry
  JOURNAL   Mol Cell Proteomics 8 (5), 904-912 (2009)
   PUBMED   19131326
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Embryonic fibroblast
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15; SER-64
            AND SER-100, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
            ANALYSIS].;
            TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
            Pancreas, Spleen, and Testis
COMMENT     On or before Sep 7, 2006 this sequence version replaced
            gi:81893726, gi:81881427.
            [FUNCTION] Catalytic subunit of the mRNA-capping methyltransferase
            RNMT:RAMAC complex that methylates the N7 position of the added
            guanosine to the 5'-cap structure of mRNAs. Binds RNA containing
            5'-terminal GpppC. {ECO:0000250|UniProtKB:O43148}.
            [CATALYTIC ACTIVITY] Reaction=a 5'-end
            (5'-triphosphoguanosine)-ribonucleoside in mRNA +
            S-adenosyl-L-methionine = a 5'-end (N(7)-methyl
            5'-triphosphoguanosine)-ribonucleoside in mRNA +
            S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008,
            Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856,
            ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617;
            EC=2.1.1.56; Evidence={ECO:0000250|UniProtKB:O43148,
            ECO:0000255|PROSITE-ProRule:PRU00895}.
            ACTIVITY REGULATION: Methyltransferase activity is activated by
            RAMAC. {ECO:0000250|UniProtKB:O43148}.
            [SUBUNIT] Interacts with importin alpha, leading to stimulate both
            RNA-binding and methyltransferase activity. Interaction with
            importin alpha and beta is required for its nuclear localization,
            importin beta dissociating in response to RanGTP, allowing
            RNMT-importin alpha to bind RNA substrates. Interacts with
            elongating form of polymerase II and RNGTT. Interacts with RAMAC,
            this interaction significantly enhances RNA-binding and cap
            methyltransferase activity. {ECO:0000250|UniProtKB:O43148}.
            [SUBCELLULAR LOCATION] Nucleus {ECO:0000250|UniProtKB:O43148}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=3; Name=1; IsoId=Q9D0L8-1; Sequence=Displayed; Name=2;
            IsoId=Q9D0L8-2; Sequence=VSP_020243; Name=3; IsoId=Q9D0L8-3;
            Sequence=VSP_020242.
            [SIMILARITY] Belongs to the class I-like SAM-binding
            methyltransferase superfamily. mRNA cap 0 methyltransferase family.
            {ECO:0000255|PROSITE-ProRule:PRU00895}.
            [SEQUENCE CAUTION] Sequence=BAC97940.1; Type=Erroneous initiation;
            Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..465
                     /gene="Rnmt"
                     /gene_synonym="Kiaa0398"
     Protein         1..465
                     /product="mRNA cap guanine-N(7) methyltransferase"
                     /EC_number="2.1.1.56"
                     /note="RG7MT1; mRNA (guanine-N(7))-methyltransferase; mRNA
                     cap methyltransferase"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..465
                     /region_name="Mature chain"
                     /note="mRNA cap guanine-N(7) methyltransferase.
                     /id=PRO_0000248323."
     Region          1..132
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:21183079."
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:21183079."
     Region          32
                     /region_name="Conflict"
                     /note="E -> K (in Ref. 2; BAB29834).
                     /evidence=ECO:0000305."
     Region          53
                     /region_name="Conflict"
                     /note="L -> H (in Ref. 2; BAE43278).
                     /evidence=ECO:0000305."
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079."
     Region          65..129
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079."
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5U2U7."
     Region          113..115
                     /region_name="Short sequence motif of biological interest"
                     /note="Nuclear localization signal.
                     /evidence=ECO:0000250."
     Region          125..464
                     /region_name="Pox_MCEL"
                     /note="mRNA capping enzyme; pfam03291"
                     /db_xref="CDD:281307"
     Region          156..464
                     /region_name="Domain"
                     /note="mRNA cap 0 methyltransferase.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895."
     Site            order(193..199,216..217,249..251,273)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
     Site            197
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895."
     Site            203
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895."
     Site            228
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895."
     Site            277
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895."
     Region          315..369
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 3).
                     /evidence=ECO:0000303|PubMed:16141072. /id=VSP_020242."
     Site            359
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895."
     Region          370..465
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:16141072. /id=VSP_020243."
     Site            456
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895."
ORIGIN      
        1 megsakasva sdpesppggn epaaasgqrl pentppcqqv dqpkmqkefg edlveqnssy
       61 vqdspskkrk ldveiileek hseddggsak rsklergdvs edepslgrln qtkrklqpqd
      121 devpqklqkl eeghssavaa hynelqevgl akrsqsrify lrnfnnwiks iligeilekv
      181 rqrktrditv ldlgcgkggd llkwrkgris rlvcadiadi smkqcqqrye dmrcrrdneh
      241 ifsaefitad cskellvekf rdpemyfdvc scqfachysf esqvqadtml rnacgrlnpg
      301 gyfigttpns felirrleas etesfgneiy tvkfqkkgny plfgckydfn legvvdvpef
      361 lvyfplltem akkynmkliy kktflefyee kiknnenkml lkrmqaleqy pahensklas
      421 ekvgdythaa eylkksqvrl plgtlsksew eatsiylvfa fekqq
//
1..465
/gene="Rnmt"
/gene_synonym="Kiaa0398"
Feature Q9D0L8 : 1 segment
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