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CMTR1_MOUSE
ID   CMTR1_MOUSE             Reviewed;         837 AA.
AC   Q9DBC3; Q3U3G5; Q3U7Y9; Q6A0D5; Q8C7V0;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE            EC=2.1.1.57 {ECO:0000250|UniProtKB:Q8N1G2};
DE   AltName: Full=Cap methyltransferase 1;
DE   AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE            Short=MTr1;
DE   AltName: Full=FtsJ methyltransferase domain-containing protein 2;
GN   Name=Cmtr1; Synonyms=Ftsjd2, Kiaa0082;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Brain cortex, Dendritic cell, Embryonic stem cell, Liver,
RC   Macrophage, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-837.
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-30, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-30, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q8N1G2}.
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:0000250|UniProtKB:Q8N1G2};
CC   -!- SUBUNIT: Interacts with POLR2A (via C-terminus).
CC       {ECO:0000250|UniProtKB:Q8N1G2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N1G2}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32161.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK005044; BAB23771.1; -; mRNA.
DR   EMBL; AK042060; BAC31146.1; -; mRNA.
DR   EMBL; AK043733; BAC31634.1; -; mRNA.
DR   EMBL; AK049190; BAC33600.1; -; mRNA.
DR   EMBL; AK080379; BAC37899.1; -; mRNA.
DR   EMBL; AK150392; BAE29520.1; -; mRNA.
DR   EMBL; AK151194; BAE30191.1; -; mRNA.
DR   EMBL; AK152276; BAE31091.1; -; mRNA.
DR   EMBL; AK152452; BAE31230.1; -; mRNA.
DR   EMBL; AK152799; BAE31504.1; -; mRNA.
DR   EMBL; AK153021; BAE31655.1; -; mRNA.
DR   EMBL; AK153066; BAE31692.1; -; mRNA.
DR   EMBL; AK154773; BAE32821.1; -; mRNA.
DR   EMBL; BC024691; AAH24691.1; -; mRNA.
DR   EMBL; AK172883; BAD32161.1; ALT_FRAME; Transcribed_RNA.
DR   CCDS; CCDS37539.1; -.
DR   RefSeq; NP_083067.1; NM_028791.6.
DR   AlphaFoldDB; Q9DBC3; -.
DR   SMR; Q9DBC3; -.
DR   BioGRID; 216534; 6.
DR   STRING; 10090.ENSMUSP00000024816; -.
DR   iPTMnet; Q9DBC3; -.
DR   PhosphoSitePlus; Q9DBC3; -.
DR   EPD; Q9DBC3; -.
DR   jPOST; Q9DBC3; -.
DR   MaxQB; Q9DBC3; -.
DR   PaxDb; Q9DBC3; -.
DR   PeptideAtlas; Q9DBC3; -.
DR   PRIDE; Q9DBC3; -.
DR   ProteomicsDB; 283866; -.
DR   Antibodypedia; 29815; 60 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000024816; ENSMUSP00000024816; ENSMUSG00000024019.
DR   GeneID; 74157; -.
DR   KEGG; mmu:74157; -.
DR   UCSC; uc008bth.1; mouse.
DR   CTD; 23070; -.
DR   MGI; MGI:1921407; Cmtr1.
DR   VEuPathDB; HostDB:ENSMUSG00000024019; -.
DR   eggNOG; KOG3673; Eukaryota.
DR   GeneTree; ENSGT00940000157172; -.
DR   HOGENOM; CLU_011097_0_0_1; -.
DR   InParanoid; Q9DBC3; -.
DR   OMA; GGILMFC; -.
DR   OrthoDB; 1336442at2759; -.
DR   PhylomeDB; Q9DBC3; -.
DR   TreeFam; TF314897; -.
DR   BioGRID-ORCS; 74157; 25 hits in 73 CRISPR screens.
DR   PRO; PR:Q9DBC3; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9DBC3; protein.
DR   Bgee; ENSMUSG00000024019; Expressed in granulocyte and 80 other tissues.
DR   ExpressionAtlas; Q9DBC3; baseline and differential.
DR   Genevisible; Q9DBC3; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
DR   GO; GO:0097309; P:cap1 mRNA methylation; ISS:UniProtKB.
DR   GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR   CDD; cd00201; WW; 1.
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; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW   Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..837
FT                   /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT                   methyltransferase 1"
FT                   /id="PRO_0000251240"
FT   DOMAIN          86..132
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   DOMAIN          230..449
FT                   /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT   DOMAIN          751..785
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..834
FT                   /note="Interaction with POLR2A"
FT                   /evidence="ECO:0000250"
FT   MOTIF           2..18
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   ACT_SITE        403
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT   BINDING         202..206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         233
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         276..282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         334..335
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         373..375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   BINDING         438
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   MOD_RES         107
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT   CONFLICT        151
FT                   /note="C -> W (in Ref. 1; BAE32821)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="L -> F (in Ref. 1; BAE31091/BAE31230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="L -> I (in Ref. 1; BAE31091/BAE31230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        500
FT                   /note="E -> V (in Ref. 1; BAE31091/BAE31230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        689
FT                   /note="V -> I (in Ref. 1; BAC33600)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   837 AA;  95676 MW;  8DB980D2FFA4F9C7 CRC64;
     MKRRTDPECT APLKKQKRIG ELARHLSSTS DDEPLSSVNH AAKASATSLS GSDSETEGKQ
     PCSDDFKDAF KADSLVEGTS SRYSMYNSVS QRLMAKMGFR EGEGLGKYSQ GRKDIVETSN
     QKGRRGLGLT LQGFDQELNV DWRDEPEPNA CEQVSWFPEC TTEIPDSREM SDWMVVGKRK
     MVIEDETEFC GEELLHSMLK CKSVFDILDG EEMRRARTRA NPYEMIRGVF FLNRAAMKMA
     NMDFVFDRMF TNPLDSSGKP LLKESDIDLL YFADVCAGPG GFSEYVLWRK KWHAKGFGMT
     LKGPNDFKLE DFYSASSELF EPYYGEGGVD GDGDITRPEN INAFRNFVLD NTDRKGVHFV
     MADGGFSVEG QENLQEILSK QLLLCQFLMA LSVVRTGGHF VCKTFDLFTP FSVGLIYLLY
     CCFERVCLFK PITSRPANSE RYVVCKGLKV GIDDVREYLF SVNIKLNQLR NTESDVNLVV
     PLMVIKGDHE FNDYMIRSNE SYCSLQIKAL AKIHAFVQDT TLSEPRQAEI RKECLQLWKI
     PDQARVAPSS SDPKFKFFEL IKDTDINIFS YKPTLLTAKT LEKIRPVLEY RCMVSGSEQK
     FLLGLGKSQI YTWDGRQSDR WVKLDLKTEL PRDTLLCVEI VHELKGEGKA QRKISAIHIL
     DVLVLNGSDV REQHFNQRIQ LAEKFVKAVS KPSRPDMNPI RVKEVYRLEE MEKIFVRLEM
     KLIKGSGGTP KLSYTGRDDR HFVPTGVYIV RTVNEPWTMG FSKSNNRKFF YNKKTQKSVY
     ALPTESIAPF HTCYYSRLFW EWGDGFHMRD SQKPQDPDKL SKEDVLSFIQ SHNPLGP
 
 
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