MCES_HUMAN
ID MCES_HUMAN Reviewed; 476 AA.
AC O43148; B0YJ90; D3DUJ5; O94996; Q9UIJ9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase;
DE EC=2.1.1.56 {ECO:0000269|PubMed:10347220, ECO:0000269|PubMed:27422871, ECO:0000269|PubMed:9705270, ECO:0000269|PubMed:9790902};
DE AltName: Full=RG7MT1;
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase;
DE AltName: Full=mRNA cap methyltransferase;
DE Short=hCMT1;
DE Short=hMet;
DE Short=hcm1p;
GN Name=RNMT; Synonyms=KIAA0398;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=9790902; DOI=10.1006/bbrc.1998.9402;
RA Tsukamoto T., Shibagaki Y., Niikura Y., Kiyohisa M.;
RT "Cloning and characterization of three human cDNAs encoding mRNA (guanine-
RT 7-)methyltransferase, an mRNA cap methylase.";
RL Biochem. Biophys. Res. Commun. 251:27-34(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND INTERACTION WITH POLYMERASE II AND RNGTT.
RX PubMed=9705270; DOI=10.1074/jbc.273.34.21443;
RA Pillutla R.C., Yue Z., Maldonado E., Shatkin A.J.;
RT "Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA
RT polymerase IIo complexes.";
RL J. Biol. Chem. 273:21443-21446(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10589710; DOI=10.1099/00221287-145-11-3023;
RA Yamada-Okabe T., Mio T., Kashima Y., Matsui M., Arisawa M.,
RA Yamada-Okabe H.;
RT "The Candida albicans gene for mRNA 5'-cap methyltransferase:
RT identification of the additional residues essential for catalysis.";
RL Microbiology 145:3023-3033(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-203; ARG-239; TYR-289;
RP PHE-291 AND PHE-354.
RX PubMed=10347220; DOI=10.1074/jbc.274.23.16553;
RA Saha N., Schwer B., Shuman S.;
RT "Characterization of human, Schizosaccharomyces pombe, and Candida albicans
RT mRNA cap methyltransferases and complete replacement of the yeast capping
RT apparatus by mammalian enzymes.";
RL J. Biol. Chem. 274:16553-16562(1999).
RN [9]
RP SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH IMPORTIN ALPHA.
RX PubMed=11114884; DOI=10.1101/gad.848200;
RA Wen Y., Shatkin A.J.;
RT "Cap methyltransferase selective binding and methylation of GpppG-RNA are
RT stimulated by importin-alpha.";
RL Genes Dev. 14:2944-2949(2000).
RN [10]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 80-LYS--LYS-83; 103-LYS--ARG-107
RP AND ARG-127.
RX PubMed=15767670; DOI=10.1128/mcb.25.7.2644-2649.2005;
RA Shafer B., Chu C., Shatkin A.J.;
RT "Human mRNA cap methyltransferase: alternative nuclear localization signal
RT motifs ensure nuclear localization required for viability.";
RL Mol. Cell. Biol. 25:2644-2649(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH RAMAC.
RX PubMed=22099306; DOI=10.1016/j.molcel.2011.08.041;
RA Gonatopoulos-Pournatzis T., Dunn S., Bounds R., Cowling V.H.;
RT "RAM/Fam103a1 is required for mRNA cap methylation.";
RL Mol. Cell 44:585-596(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 165-476 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RA Wu H., Lunin V.V., Zeng H., Antoshenko T., MacKenzie F., Weigelt J.,
RA Arrowsmith C.H., Edwards A.M., Bochkarev A., Min J., Plotnikov A.N.;
RT "The crystal structure of human RNA (guanine-7-) methyltransferase in
RT complex with SAH.";
RL Submitted (NOV-2007) to the PDB data bank.
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 165-476.
RA Zeng H., Amaya M.F., Loppnau P., Bountra C., Weigelt J., Arrowsmith C.H.,
RA Edwards A.M., Botchkarev A., Min J., Plotnikov A.N., Wu H.;
RT "Crystal structure of mRNA cap guanine-N7 methyltransferase (RNMT) in
RT complex with sinefungin.";
RL Submitted (SEP-2008) to the PDB data bank.
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 167-476 IN COMPLEX WITH RAMAC AND
RP S-ADENOSYL-L-HOMOCYSTEINE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP INTERACTION WITH RAMAC, AND MUTAGENESIS OF TRP-178; LYS-393; PHE-398;
RP LYS-409; LYS-413; ALA-417; ARG-450 AND PRO-452.
RX PubMed=27422871; DOI=10.1093/nar/gkw637;
RA Varshney D., Petit A.P., Bueren-Calabuig J.A., Jansen C., Fletcher D.A.,
RA Peggie M., Weidlich S., Scullion P., Pisliakov A.V., Cowling V.H.;
RT "Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation by
RT RAM.";
RL Nucleic Acids Res. 44:10423-10436(2016).
CC -!- FUNCTION: Catalytic subunit of the mRNA-capping methyltransferase
CC RNMT:RAMAC complex that methylates the N7 position of the added
CC guanosine to the 5'-cap structure of mRNAs (PubMed:9790902,
CC PubMed:9705270, PubMed:10347220, PubMed:11114884, PubMed:22099306,
CC PubMed:27422871). Binds RNA containing 5'-terminal GpppC
CC (PubMed:11114884). {ECO:0000269|PubMed:10347220,
CC ECO:0000269|PubMed:11114884, ECO:0000269|PubMed:22099306,
CC ECO:0000269|PubMed:27422871, ECO:0000269|PubMed:9705270,
CC ECO:0000269|PubMed:9790902}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00895, ECO:0000269|PubMed:10347220,
CC ECO:0000269|PubMed:27422871, ECO:0000269|PubMed:9705270,
CC ECO:0000269|PubMed:9790902};
CC -!- ACTIVITY REGULATION: Methyltransferase activity is activated by RAMAC
CC (PubMed:27422871). {ECO:0000269|PubMed:27422871}.
CC -!- SUBUNIT: Interacts with importin alpha, leading to stimulate both RNA-
CC binding and methyltransferase activity (PubMed:11114884). Interaction
CC with importin alpha and beta is required for its nuclear localization,
CC importin beta dissociating in response to RanGTP, allowing RNMT-
CC importin alpha to bind RNA substrates (PubMed:11114884). Interacts with
CC elongating form of polymerase II and RNGTT (PubMed:9705270). Interacts
CC with RAMAC, this interaction significantly enhances RNA-binding and cap
CC methyltransferase activity (PubMed:22099306, Ref.14).
CC {ECO:0000269|PubMed:11114884, ECO:0000269|PubMed:22099306,
CC ECO:0000269|PubMed:9705270, ECO:0000269|Ref.14}.
CC -!- INTERACTION:
CC O43148; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-877832, EBI-2548508;
CC O43148; P52292: KPNA2; NbExp=3; IntAct=EBI-877832, EBI-349938;
CC O43148; O60684: KPNA6; NbExp=3; IntAct=EBI-877832, EBI-359923;
CC O43148; Q9HB20: PLEKHA3; NbExp=3; IntAct=EBI-877832, EBI-11079894;
CC O43148; Q9BTL3: RAMAC; NbExp=7; IntAct=EBI-877832, EBI-744023;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11114884,
CC ECO:0000269|PubMed:15767670}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=hCMT1a;
CC IsoId=O43148-1; Sequence=Displayed;
CC Name=2; Synonyms=hCMT1b;
CC IsoId=O43148-2; Sequence=VSP_020241;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9705270,
CC ECO:0000269|PubMed:9790902}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00895}.
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DR EMBL; AB022604; BAA74464.1; -; mRNA.
DR EMBL; AB022605; BAA74463.1; -; mRNA.
DR EMBL; AF067791; AAC63269.1; -; mRNA.
DR EMBL; AB020966; BAA82447.1; -; mRNA.
DR EMBL; AB007858; BAA23694.1; -; mRNA.
DR EMBL; EF445026; ACA06068.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01505.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01506.1; -; Genomic_DNA.
DR EMBL; BC036798; AAH36798.1; -; mRNA.
DR CCDS; CCDS11867.1; -. [O43148-1]
DR CCDS; CCDS77156.1; -. [O43148-2]
DR RefSeq; NP_001295192.1; NM_001308263.1. [O43148-2]
DR RefSeq; NP_003790.1; NM_003799.2. [O43148-1]
DR RefSeq; XP_005258219.1; XM_005258162.1.
DR RefSeq; XP_016881550.1; XM_017026061.1.
DR PDB; 3BGV; X-ray; 2.30 A; A/B/C/D=165-476.
DR PDB; 3EPP; X-ray; 2.41 A; A/B=165-476.
DR PDB; 5E8J; X-ray; 2.35 A; A/B=167-476.
DR PDB; 5E9J; X-ray; 3.47 A; A/B=167-416, A/B=457-476.
DR PDB; 5E9W; X-ray; 2.28 A; A/B/C/D=167-476.
DR PDBsum; 3BGV; -.
DR PDBsum; 3EPP; -.
DR PDBsum; 5E8J; -.
DR PDBsum; 5E9J; -.
DR PDBsum; 5E9W; -.
DR AlphaFoldDB; O43148; -.
DR SMR; O43148; -.
DR BioGRID; 114269; 38.
DR IntAct; O43148; 23.
DR MINT; O43148; -.
DR STRING; 9606.ENSP00000372804; -.
DR BindingDB; O43148; -.
DR ChEMBL; CHEMBL4295662; -.
DR GlyGen; O43148; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43148; -.
DR PhosphoSitePlus; O43148; -.
DR BioMuta; RNMT; -.
DR EPD; O43148; -.
DR jPOST; O43148; -.
DR MassIVE; O43148; -.
DR MaxQB; O43148; -.
DR PaxDb; O43148; -.
DR PeptideAtlas; O43148; -.
DR PRIDE; O43148; -.
DR ProteomicsDB; 48765; -. [O43148-1]
DR ProteomicsDB; 48766; -. [O43148-2]
DR Antibodypedia; 21962; 309 antibodies from 26 providers.
DR DNASU; 8731; -.
DR Ensembl; ENST00000262173.7; ENSP00000262173.3; ENSG00000101654.18. [O43148-1]
DR Ensembl; ENST00000383314.7; ENSP00000372804.2; ENSG00000101654.18. [O43148-1]
DR Ensembl; ENST00000543302.6; ENSP00000446426.1; ENSG00000101654.18. [O43148-1]
DR Ensembl; ENST00000589866.5; ENSP00000466252.1; ENSG00000101654.18. [O43148-1]
DR Ensembl; ENST00000592764.5; ENSP00000466111.1; ENSG00000101654.18. [O43148-2]
DR GeneID; 8731; -.
DR KEGG; hsa:8731; -.
DR MANE-Select; ENST00000383314.7; ENSP00000372804.2; NM_003799.3; NP_003790.1.
DR UCSC; uc002ksk.2; human. [O43148-1]
DR CTD; 8731; -.
DR DisGeNET; 8731; -.
DR GeneCards; RNMT; -.
DR HGNC; HGNC:10075; RNMT.
DR HPA; ENSG00000101654; Low tissue specificity.
DR MIM; 603514; gene.
DR neXtProt; NX_O43148; -.
DR OpenTargets; ENSG00000101654; -.
DR PharmGKB; PA34448; -.
DR VEuPathDB; HostDB:ENSG00000101654; -.
DR eggNOG; KOG1975; Eukaryota.
DR GeneTree; ENSGT00390000002368; -.
DR HOGENOM; CLU_020346_0_1_1; -.
DR InParanoid; O43148; -.
DR OMA; WDATSIY; -.
DR OrthoDB; 1390749at2759; -.
DR PhylomeDB; O43148; -.
DR TreeFam; TF314347; -.
DR BioCyc; MetaCyc:HS02296-MON; -.
DR BRENDA; 2.1.1.56; 2681.
DR PathwayCommons; O43148; -.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR SignaLink; O43148; -.
DR SIGNOR; O43148; -.
DR BioGRID-ORCS; 8731; 730 hits in 1093 CRISPR screens.
DR ChiTaRS; RNMT; human.
DR EvolutionaryTrace; O43148; -.
DR GeneWiki; MRNA_(guanine-N7-)-methyltransferase; -.
DR GeneWiki; RNMT; -.
DR GenomeRNAi; 8731; -.
DR Pharos; O43148; Tbio.
DR PRO; PR:O43148; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O43148; protein.
DR Bgee; ENSG00000101654; Expressed in amniotic fluid and 200 other tissues.
DR ExpressionAtlas; O43148; baseline and differential.
DR Genevisible; O43148; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR016899; mRNA_G-N7_MeTrfase_euk.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189; PTHR12189; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR PIRSF; PIRSF028762; ABD1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Methyltransferase; mRNA capping;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..476
FT /note="mRNA cap guanine-N7 methyltransferase"
FT /id="PRO_0000248321"
FT DOMAIN 128..476
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 126..128
FT /note="Nuclear localization signal"
FT COMPBIAS 17..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..177
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895,
FT ECO:0000269|PubMed:27422871, ECO:0007744|PDB:3BGV,
FT ECO:0007744|PDB:5E9J, ECO:0007744|PDB:5E9W"
FT BINDING 205
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895,
FT ECO:0000269|PubMed:27422871, ECO:0007744|PDB:3BGV,
FT ECO:0007744|PDB:5E9J, ECO:0007744|PDB:5E9W"
FT BINDING 227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895,
FT ECO:0000269|PubMed:27422871, ECO:0007744|PDB:3BGV,
FT ECO:0007744|PDB:5E9J, ECO:0007744|PDB:5E9W"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27422871,
FT ECO:0007744|PDB:3BGV, ECO:0007744|PDB:5E9J,
FT ECO:0007744|PDB:5E9W"
FT BINDING 284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27422871,
FT ECO:0007744|PDB:3BGV, ECO:0007744|PDB:5E9J,
FT ECO:0007744|PDB:5E9W"
FT BINDING 289
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27422871,
FT ECO:0007744|PDB:3BGV, ECO:0007744|PDB:5E9J,
FT ECO:0007744|PDB:5E9W"
FT SITE 208
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 214
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 239
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 288
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 370
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 467
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0L8"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0L8"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2U7"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2U7"
FT VAR_SEQ 465..476
FT /note="SIYLVFAFEKQQ -> RLTVTIMREAWLSTVGPGRAPVAASSVKWGTPRPAM
FT QFIL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9790902"
FT /id="VSP_020241"
FT MUTAGEN 80..83
FT /note="KKRK->AAAA: Does not abolish nuclear localization.
FT Abolishes nuclear localization; when associated with 103-
FT AAAAA-107 and I-127."
FT /evidence="ECO:0000269|PubMed:15767670"
FT MUTAGEN 103..107
FT /note="KKRKR->AAAAA: Does not abolish nuclear localization.
FT Abolishes nuclear localization; when associated with 80-
FT AAAA-83 and I-127."
FT /evidence="ECO:0000269|PubMed:15767670"
FT MUTAGEN 127
FT /note="R->I: Does not abolish nuclear localization.
FT Abolishes nuclear localization; when associated with 80-
FT AAAA-83 and 103-AAAAA-107."
FT /evidence="ECO:0000269|PubMed:15767670"
FT MUTAGEN 178
FT /note="W->C: Loss of methyltransferase activity in presence
FT or absence of RAMAC; when associated with C-417. Complete
FT restored RAMAC-mediated methyltransferase activity under
FT reducing conditions; when associated with C-417. Loss of
FT methyltransferase activity in presence or absence of RAMAC;
FT when associated with C-417; C-393 and C-398. Partially
FT restored RAMAC-mediated methyltransferase activity under
FT reducing conditions; when associated with C-417; C-393 and
FT C-398."
FT /evidence="ECO:0000269|PubMed:27422871"
FT MUTAGEN 203
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10347220"
FT MUTAGEN 239
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10347220"
FT MUTAGEN 289
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10347220"
FT MUTAGEN 291
FT /note="F->A: Strongly impairs enzyme activity."
FT /evidence="ECO:0000269|PubMed:10347220"
FT MUTAGEN 354
FT /note="F->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10347220"
FT MUTAGEN 393
FT /note="K->C: Loss of methyltransferase activity in presence
FT or absence of RAMAC; when associated with C-178; C-398 and
FT C-417. Partially restored RAMAC-mediated methyltransferase
FT activity under reducing conditions; when associated with C-
FT 178; C-398 and C-417."
FT /evidence="ECO:0000269|PubMed:27422871"
FT MUTAGEN 398
FT /note="F->C: Loss of methyltransferase activity in presence
FT or absence of RAMAC; when associated with C-178; C-393 and
FT C-417. Partially restored RAMAC-mediated methyltransferase
FT activity under reducing conditions; when associated with C-
FT 178; C-393 and C-417."
FT /evidence="ECO:0000269|PubMed:27422871"
FT MUTAGEN 409
FT /note="K->E: Decreased S-adenosyl-L-methionine binding and
FT methyltransferase activity in absence of RAMAC; when
FT associated with E-413. Decreased interaction with RAMAC;
FT when associated with E-413."
FT /evidence="ECO:0000269|PubMed:27422871"
FT MUTAGEN 413
FT /note="K->E: Decreased S-adenosyl-L-methionine binding and
FT methyltransferase activity in absence of RAMAC; when
FT associated with E-409. Decreased interaction with RAMAC;
FT when associated with E-409."
FT /evidence="ECO:0000269|PubMed:27422871"
FT MUTAGEN 417
FT /note="A->C: Loss of methyltransferase activity in presence
FT or absence of RAMAC; when associated with C-178. Complete
FT restored RAMAC-mediated methyltransferase activity under
FT reducing conditions; when associated with C-178. Loss of
FT methyltransferase activity in presence or absence of RAMAC;
FT when associated with C-178. Loss of methyltransferase
FT activity in presence or absence of RAMAC; when associated
FT with C-178; C-393 and C-398. Partially restored RAMAC-
FT mediated methyltransferase activity under reducing
FT conditions; when associated with C-178; C-393 and C-398."
FT /evidence="ECO:0000269|PubMed:27422871"
FT MUTAGEN 450
FT /note="R->E: Increased S-adenosyl-L-methionine binding and
FT methyltransferase activity in absence of RAMAC; when
FT associated with E-452. No change in interaction with RAMAC;
FT when associated with E-452."
FT /evidence="ECO:0000269|PubMed:27422871"
FT MUTAGEN 452
FT /note="P->E: Increased S-adenosyl-L-methionine binding and
FT methyltransferase activity in absence of RAMAC; when
FT associated with E-450. No change in interaction with RAMAC;
FT when associated with E-450."
FT /evidence="ECO:0000269|PubMed:27422871"
FT CONFLICT 179
FT /note="M -> I (in Ref. 3; BAA82447)"
FT /evidence="ECO:0000305"
FT HELIX 170..193
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:5E9W"
FT TURN 207..211
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:5E9W"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:5E8J"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 308..319
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:5E9W"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:5E8J"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 387..394
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:5E8J"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:5E8J"
FT HELIX 438..443
FT /evidence="ECO:0007829|PDB:5E8J"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:5E9W"
FT HELIX 458..464
FT /evidence="ECO:0007829|PDB:5E9W"
FT STRAND 467..474
FT /evidence="ECO:0007829|PDB:5E9W"
SQ SEQUENCE 476 AA; 54844 MW; EC919BC41BD5E2B3 CRC64;
MANSAKAEEY EKMSLEQAKA SVNSETESSF NINENTTASG TGLSEKTSVC RQVDIARKRK
EFEDDLVKES SSCGKDTPSK KRKLDPEIVP EEKDCGDAEG NSKKRKRETE DVPKDKSSTG
DGTQNKRKIA LEDVPEKQKN LEEGHSSTVA AHYNELQEVG LEKRSQSRIF YLRNFNNWMK
SVLIGEFLEK VRQKKKRDIT VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSVKQCQQRY
EDMKNRRDSE YIFSAEFITA DSSKELLIDK FRDPQMCFDI CSCQFVCHYS FESYEQADMM
LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD YPLFGCKYDF
NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE EKIKNNENKM LLKRMQALEP
YPANESSKLV SEKVDDYEHA AKYMKNSQVR LPLGTLSKSE WEATSIYLVF AFEKQQ
