CMTR1_HUMAN
ID CMTR1_HUMAN Reviewed; 835 AA.
AC Q8N1G2; A8K949; Q14670; Q96FJ9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE EC=2.1.1.57 {ECO:0000269|PubMed:21310715};
DE AltName: Full=Cap methyltransferase 1;
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE Short=MTr1;
DE Short=hMTr1;
DE AltName: Full=FtsJ methyltransferase domain-containing protein 2;
DE AltName: Full=Interferon-stimulated gene 95 kDa protein;
DE Short=ISG95;
GN Name=CMTR1; Synonyms=FTSJD2, KIAA0082, MTR1;
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 [6]
RP INDUCTION BY INTERFERONS ALPHA AND BETA.
RX PubMed=12743294; DOI=10.1128/jvi.77.11.6367-6375.2003;
RA Geiss G.K., Carter V.S., He Y., Kwieciszewski B.K., Holzman T., Korth M.J.,
RA Lazaro C.A., Fausto N., Bumgarner R.E., Katze M.G.;
RT "Gene expression profiling of the cellular transcriptional network
RT regulated by alpha/beta interferon and its partial attenuation by the
RT hepatitis C virus nonstructural 5A protein.";
RL J. Virol. 77:6367-6375(2003).
RN [7]
RP INDUCTION BY VIRAL INFECTION.
RX PubMed=12743306; DOI=10.1128/jvi.77.11.6493-6506.2003;
RA Guerra S., Lopez-Fernandez L.A., Pascual-Montano A., Munoz M., Harshman K.,
RA Esteban M.;
RT "Cellular gene expression survey of vaccinia virus infection of human HeLa
RT cells.";
RL J. Virol. 77:6493-6506(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, INTERACTION WITH POLR2A, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=18533109; DOI=10.1016/j.bbrc.2008.05.137;
RA Haline-Vaz T., Silva T.C.L., Zanchin N.I.T.;
RT "The human interferon-regulated ISG95 protein interacts with RNA polymerase
RT II and shows methyltransferase activity.";
RL Biochem. Biophys. Res. Commun. 372:719-724(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP FUNCTION.
RX PubMed=20713356; DOI=10.1074/jbc.m110.155283;
RA Belanger F., Stepinski J., Darzynkiewicz E., Pelletier J.;
RT "Characterization of hMTr1, a human Cap1 2'-O-Ribose methyltransferase.";
RL J. Biol. Chem. 285:33037-33044(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-239; ASP-364 AND LYS-404.
RX PubMed=21310715; DOI=10.1093/nar/gkr038;
RA Werner M., Purta E., Kaminska K.H., Cymerman I.A., Campbell D.A.,
RA Mittra B., Zamudio J.R., Sturm N.R., Jaworski J., Bujnicki J.M.;
RT "2'-O-ribose methylation of cap2 in human: function and evolution in a
RT horizontally mobile family.";
RL Nucleic Acids Res. 39:4756-4768(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-91, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 126-550 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND A CAPPED OLIGORIBONUCLEOTIDE SUBSTRATE, AND
RP MUTAGENESIS OF LYS-203 AND ARG-228.
RX PubMed=24402442; DOI=10.1038/ncomms4004;
RA Smietanski M., Werner M., Purta E., Kaminska K.H., Stepinski J.,
RA Darzynkiewicz E., Nowotny M., Bujnicki J.M.;
RT "Structural analysis of human 2'-O-ribose methyltransferases involved in
RT mRNA cap structure formation.";
RL Nat. Commun. 5:3004-3004(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1).
CC Displays a preference for cap0 transcripts. Cap1 modification is linked
CC to higher levels of translation. May be involved in the interferon
CC response pathway. {ECO:0000269|PubMed:18533109,
CC ECO:0000269|PubMed:20713356, ECO:0000269|PubMed:21310715}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000269|PubMed:21310715};
CC -!- SUBUNIT: Interacts with POLR2A (via C-terminus).
CC {ECO:0000269|PubMed:18533109}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18533109,
CC ECO:0000269|PubMed:21310715}.
CC -!- INDUCTION: By interferons alpha and beta, and by Vaccinia virus
CC infection. {ECO:0000269|PubMed:12743294, ECO:0000269|PubMed:12743306,
CC ECO:0000269|PubMed:18533109}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07893.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D43949; BAA07893.2; ALT_INIT; mRNA.
DR EMBL; AK292564; BAF85253.1; -; mRNA.
DR EMBL; AL353597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010731; AAH10731.2; -; mRNA.
DR EMBL; BC031890; AAH31890.1; -; mRNA.
DR CCDS; CCDS4835.1; -.
DR RefSeq; NP_055865.1; NM_015050.2.
DR PDB; 4N48; X-ray; 2.70 A; A/B=126-550.
DR PDB; 4N49; X-ray; 1.90 A; A=126-550.
DR PDB; 4N4A; X-ray; 2.35 A; A=126-550.
DR PDBsum; 4N48; -.
DR PDBsum; 4N49; -.
DR PDBsum; 4N4A; -.
DR AlphaFoldDB; Q8N1G2; -.
DR SMR; Q8N1G2; -.
DR BioGRID; 116703; 201.
DR IntAct; Q8N1G2; 14.
DR MINT; Q8N1G2; -.
DR STRING; 9606.ENSP00000362550; -.
DR DrugBank; DB00118; Ademetionine.
DR iPTMnet; Q8N1G2; -.
DR PhosphoSitePlus; Q8N1G2; -.
DR BioMuta; CMTR1; -.
DR DMDM; 74750894; -.
DR EPD; Q8N1G2; -.
DR jPOST; Q8N1G2; -.
DR MassIVE; Q8N1G2; -.
DR MaxQB; Q8N1G2; -.
DR PaxDb; Q8N1G2; -.
DR PeptideAtlas; Q8N1G2; -.
DR PRIDE; Q8N1G2; -.
DR ProteomicsDB; 71600; -.
DR TopDownProteomics; Q8N1G2; -.
DR Antibodypedia; 29815; 60 antibodies from 14 providers.
DR DNASU; 23070; -.
DR Ensembl; ENST00000373451.9; ENSP00000362550.4; ENSG00000137200.13.
DR GeneID; 23070; -.
DR KEGG; hsa:23070; -.
DR MANE-Select; ENST00000373451.9; ENSP00000362550.4; NM_015050.3; NP_055865.1.
DR UCSC; uc003ons.4; human.
DR CTD; 23070; -.
DR DisGeNET; 23070; -.
DR GeneCards; CMTR1; -.
DR HGNC; HGNC:21077; CMTR1.
DR HPA; ENSG00000137200; Low tissue specificity.
DR MIM; 616189; gene.
DR neXtProt; NX_Q8N1G2; -.
DR OpenTargets; ENSG00000137200; -.
DR PharmGKB; PA162389052; -.
DR VEuPathDB; HostDB:ENSG00000137200; -.
DR eggNOG; KOG3673; Eukaryota.
DR GeneTree; ENSGT00940000157172; -.
DR HOGENOM; CLU_011097_0_0_1; -.
DR OMA; GGILMFC; -.
DR OrthoDB; 1336442at2759; -.
DR PhylomeDB; Q8N1G2; -.
DR TreeFam; TF314897; -.
DR BioCyc; MetaCyc:ENSG00000137200-MON; -.
DR BRENDA; 2.1.1.57; 2681.
DR PathwayCommons; Q8N1G2; -.
DR SignaLink; Q8N1G2; -.
DR BioGRID-ORCS; 23070; 583 hits in 1074 CRISPR screens.
DR ChiTaRS; CMTR1; human.
DR GenomeRNAi; 23070; -.
DR Pharos; Q8N1G2; Tbio.
DR PRO; PR:Q8N1G2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8N1G2; protein.
DR Bgee; ENSG00000137200; Expressed in right testis and 183 other tissues.
DR ExpressionAtlas; Q8N1G2; baseline and differential.
DR Genevisible; Q8N1G2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
DR GO; GO:0097309; P:cap1 mRNA methylation; IDA:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR DisProt; DP02611; -.
DR InterPro; IPR030376; Cap_mRNA_MeTrfase_1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR025816; RrmJ-type_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001202; WW_dom.
DR PANTHER; PTHR16121:SF0; PTHR16121:SF0; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Methyltransferase; mRNA capping;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..835
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000251239"
FT DOMAIN 87..133
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 231..450
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT DOMAIN 752..786
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..835
FT /note="Interaction with POLR2A"
FT /evidence="ECO:0000269|PubMed:18533109"
FT MOTIF 2..19
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768,
FT ECO:0000305|PubMed:24402442"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /evidence="ECO:0000305|PubMed:21310715"
FT ACT_SITE 364
FT /evidence="ECO:0000305|PubMed:21310715"
FT ACT_SITE 404
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21310715"
FT BINDING 203..207
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24402442,
FT ECO:0007744|PDB:4N48, ECO:0007744|PDB:4N49"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24402442,
FT ECO:0007744|PDB:4N48, ECO:0007744|PDB:4N49"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24402442,
FT ECO:0007744|PDB:4N48, ECO:0007744|PDB:4N49"
FT BINDING 277..283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24402442,
FT ECO:0007744|PDB:4N48, ECO:0007744|PDB:4N49"
FT BINDING 335..336
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24402442,
FT ECO:0007744|PDB:4N48, ECO:0007744|PDB:4N49"
FT BINDING 374..376
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24402442,
FT ECO:0007744|PDB:4N48, ECO:0007744|PDB:4N49"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24402442,
FT ECO:0007744|PDB:4N48, ECO:0007744|PDB:4N49"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC3"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC3"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 203
FT /note="K->A: Reduces both mRNA cap binding and catalytic
FT activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 228
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:24402442"
FT MUTAGEN 239
FT /note="K->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21310715"
FT MUTAGEN 364
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21310715"
FT MUTAGEN 404
FT /note="K->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21310715"
FT CONFLICT 795
FT /note="Y -> H (in Ref. 3; BAF85253)"
FT /evidence="ECO:0000305"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4N4A"
FT TURN 168..174
FT /evidence="ECO:0007829|PDB:4N49"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:4N4A"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4N48"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4N49"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:4N49"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:4N49"
FT TURN 247..252
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4N49"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:4N49"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:4N49"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:4N4A"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:4N4A"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:4N4A"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:4N48"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:4N49"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:4N49"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:4N49"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:4N48"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 381..394
FT /evidence="ECO:0007829|PDB:4N49"
FT STRAND 395..405
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 411..423
FT /evidence="ECO:0007829|PDB:4N49"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:4N49"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 454..470
FT /evidence="ECO:0007829|PDB:4N49"
FT STRAND 473..481
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 483..487
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 490..519
FT /evidence="ECO:0007829|PDB:4N49"
FT HELIX 528..539
FT /evidence="ECO:0007829|PDB:4N49"
SQ SEQUENCE 835 AA; 95321 MW; 03919512A73C30FB CRC64;
MKRRTDPECT APIKKQKKRV AELALSLSST SDDEPPSSVS HGAKASTTSL SGSDSETEGK
QHSSDSFDDA FKADSLVEGT SSRYSMYNSV SQKLMAKMGF REGEGLGKYS QGRKDIVEAS
SQKGRRGLGL TLRGFDQELN VDWRDEPEPS ACEQVSWFPE CTTEIPDTQE MSDWMVVGKR
KMIIEDETEF CGEELLHSVL QCKSVFDVLD GEEMRRARTR ANPYEMIRGV FFLNRAAMKM
ANMDFVFDRM FTNPRDSYGK PLVKDREAEL LYFADVCAGP GGFSEYVLWR KKWHAKGFGM
TLKGPNDFKL EDFYSASSEL FEPYYGEGGI DGDGDITRPE NISAFRNFVL DNTDRKGVHF
LMADGGFSVE GQENLQEILS KQLLLCQFLM ALSIVRTGGH FICKTFDLFT PFSVGLVYLL
YCCFERVCLF KPITSRPANS ERYVVCKGLK VGIDDVRDYL FAVNIKLNQL RNTDSDVNLV
VPLEVIKGDH EFTDYMIRSN ESHCSLQIKA LAKIHAFVQD TTLSEPRQAE IRKECLRLWG
IPDQARVAPS SSDPKSKFFE LIQGTEIDIF SYKPTLLTSK TLEKIRPVFD YRCMVSGSEQ
KFLIGLGKSQ IYTWDGRQSD RWIKLDLKTE LPRDTLLSVE IVHELKGEGK AQRKISAIHI
LDVLVLNGTD VREQHFNQRI QLAEKFVKAV SKPSRPDMNP IRVKEVYRLE EMEKIFVRLE
MKIIKGSSGT PKLSYTGRDD RHFVPMGLYI VRTVNEPWTM GFSKSFKKKF FYNKKTKDST
FDLPADSIAP FHICYYGRLF WEWGDGIRVH DSQKPQDQDK LSKEDVLSFI QMHRA
