TRMB_HUMAN
ID TRMB_HUMAN Reviewed; 276 AA.
AC Q9UBP6; B2RBX1; H7BXF2; Q14105; Q53FS9;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_03055};
DE AltName: Full=Methyltransferase-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03055};
DE AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:31031084};
DE AltName: Full=miRNA (guanine-N(7)-)-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:31031083};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055};
GN Name=METTL1 {ECO:0000255|HAMAP-Rule:MF_03055, ECO:0000312|HGNC:HGNC:7030};
GN Synonyms=C12orf1 {ECO:0000312|HGNC:HGNC:7030};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10329009; DOI=10.1006/geno.1999.5780;
RA Bahr A., Hankeln T., Fiedler T., Hegemann J., Schmidt E.R.;
RT "Molecular analysis of METTL1, a novel human methyltransferase-like gene
RT with a high degree of phylogenetic conservation.";
RL Genomics 57:424-428(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 FUNCTION, PATHWAY, AND INTERACTION WITH WDR4.
RX PubMed=12403464; DOI=10.1017/s1355838202024019;
RA Alexandrov A., Martzen M.R., Phizicky E.M.;
RT "Two proteins that form a complex are required for 7-methylguanosine
RT modification of yeast tRNA.";
RL RNA 8:1253-1266(2002).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH WDR4, PHOSPHORYLATION AT SER-27, AND
RP MUTAGENESIS OF SER-27.
RX PubMed=15861136; DOI=10.1038/sj.emboj.7600648;
RA Cartlidge R.A., Knebel A., Peggie M., Alexandrov A., Phizicky E.M.,
RA Cohen P.;
RT "The tRNA methylase METTL1 is phosphorylated and inactivated by PKB and RSK
RT in vitro and in cells.";
RL EMBO J. 24:1696-1705(2005).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, 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 [12]
RP SUBCELLULAR LOCATION.
RX PubMed=26751069; DOI=10.1371/journal.pbio.1002349;
RA Cheng I.C., Chen B.C., Shuai H.H., Chien F.C., Chen P., Hsieh T.S.;
RT "Wuho is a new member in maintaining genome stability through its
RT interaction with flap endonuclease 1.";
RL PLoS Biol. 14:E1002349-E1002349(2016).
RN [13]
RP FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=31031084; DOI=10.1016/j.molcel.2019.03.036;
RA Zhang L.S., Liu C., Ma H., Dai Q., Sun H.L., Luo G., Zhang Z., Zhang L.,
RA Hu L., Dong X., He C.;
RT "Transcriptome-wide mapping of internal N7-methylguanosine methylome in
RT mammalian mRNA.";
RL Mol. Cell 0:0-0(2019).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 107-GLU--ARG-109.
RX PubMed=31031083; DOI=10.1016/j.molcel.2019.03.040;
RA Pandolfini L., Barbieri I., Bannister A.J., Hendrick A., Andrews B.,
RA Webster N., Murat P., Mach P., Brandi R., Robson S.C., Migliori V.,
RA Alendar A., d'Onofrio M., Balasubramanian S., Kouzarides T.;
RT "METTL1 promotes let-7 microRNA processing via m7G methylation.";
RL Mol. Cell 0:0-0(2019).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 32-265 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human methyltransferase-like protein 1.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Methyltransferase that mediates the formation of N(7)-
CC methylguanine in a subset of RNA species, such as tRNAs, mRNAs and
CC microRNAs (miRNAs) (PubMed:12403464, PubMed:31031084, PubMed:31031083).
CC Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in
CC tRNA (PubMed:12403464, PubMed:31031084). Also acts as a
CC methyltransferase for a subset of internal N(7)-methylguanine in mRNAs
CC (PubMed:31031084). Internal N(7)-methylguanine methylation of mRNAs
CC regulates translation (PubMed:31031084). Also methylates a specific
CC subset of miRNAs, such as let-7 (PubMed:31031083). N(7)-methylguanine
CC methylation of let-7 miRNA promotes let-7 miRNA processing by
CC disrupting an inhibitory secondary structure within the primary miRNA
CC transcript (pri-miRNA) (PubMed:31031083). Acts as a regulator of
CC embryonic stem cell self-renewal and differentiation (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_03055, ECO:0000269|PubMed:12403464,
CC ECO:0000269|PubMed:31031083, ECO:0000269|PubMed:31031084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a guanosine in mRNA + S-adenosyl-L-methionine = an N(7)-
CC methylguanosine in mRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60508, Rhea:RHEA-COMP:15584, Rhea:RHEA-COMP:15585,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; Evidence={ECO:0000269|PubMed:31031084};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60509;
CC Evidence={ECO:0000269|PubMed:31031084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a guanosine in miRNA + S-adenosyl-L-methionine = an N(7)-
CC methylguanosine in miRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60512, Rhea:RHEA-COMP:15587, Rhea:RHEA-COMP:15588,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; Evidence={ECO:0000269|PubMed:31031083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60513;
CC Evidence={ECO:0000269|PubMed:31031083};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000269|PubMed:12403464, ECO:0000269|PubMed:31031084}.
CC -!- SUBUNIT: Forms a complex with WDR4. {ECO:0000269|Ref.15}.
CC -!- INTERACTION:
CC Q9UBP6; P57081: WDR4; NbExp=13; IntAct=EBI-750415, EBI-750427;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15861136,
CC ECO:0000269|PubMed:26751069}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBP6-2; Sequence=VSP_044671, VSP_044672;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10329009}.
CC -!- PTM: Phosphorylation at Ser-27 inactivates its catalytic activity but
CC does not affect the interaction with WDR4. {ECO:0000255|HAMAP-
CC Rule:MF_03055, ECO:0000269|PubMed:15861136}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_03055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA65470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y18643; CAA77239.1; -; mRNA.
DR EMBL; Y18642; CAA77238.1; -; Genomic_DNA.
DR EMBL; X96698; CAA65470.1; ALT_INIT; mRNA.
DR EMBL; AK314851; BAG37368.1; -; mRNA.
DR EMBL; AK223202; BAD96922.1; -; mRNA.
DR EMBL; AC025165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000550; AAH00550.1; -; mRNA.
DR CCDS; CCDS8955.3; -. [Q9UBP6-1]
DR CCDS; CCDS8956.1; -. [Q9UBP6-2]
DR RefSeq; NP_005362.3; NM_005371.5. [Q9UBP6-1]
DR RefSeq; NP_075422.3; NM_023033.3. [Q9UBP6-2]
DR PDB; 3CKK; X-ray; 1.55 A; A=32-265.
DR PDB; 7OGJ; X-ray; 1.59 A; A/B=32-265.
DR PDB; 7PL1; X-ray; 1.85 A; A=32-265.
DR PDBsum; 3CKK; -.
DR PDBsum; 7OGJ; -.
DR PDBsum; 7PL1; -.
DR AlphaFoldDB; Q9UBP6; -.
DR SMR; Q9UBP6; -.
DR BioGRID; 110392; 43.
DR DIP; DIP-61920N; -.
DR IntAct; Q9UBP6; 3.
DR MINT; Q9UBP6; -.
DR STRING; 9606.ENSP00000314441; -.
DR iPTMnet; Q9UBP6; -.
DR PhosphoSitePlus; Q9UBP6; -.
DR BioMuta; METTL1; -.
DR DMDM; 32171926; -.
DR EPD; Q9UBP6; -.
DR jPOST; Q9UBP6; -.
DR MassIVE; Q9UBP6; -.
DR MaxQB; Q9UBP6; -.
DR PaxDb; Q9UBP6; -.
DR PeptideAtlas; Q9UBP6; -.
DR PRIDE; Q9UBP6; -.
DR ProteomicsDB; 43260; -.
DR ProteomicsDB; 84026; -. [Q9UBP6-1]
DR Antibodypedia; 16399; 177 antibodies from 29 providers.
DR DNASU; 4234; -.
DR Ensembl; ENST00000257848.7; ENSP00000257848.7; ENSG00000037897.17. [Q9UBP6-2]
DR Ensembl; ENST00000324871.12; ENSP00000314441.7; ENSG00000037897.17. [Q9UBP6-1]
DR GeneID; 4234; -.
DR KEGG; hsa:4234; -.
DR MANE-Select; ENST00000324871.12; ENSP00000314441.7; NM_005371.6; NP_005362.3.
DR UCSC; uc009zqc.4; human. [Q9UBP6-1]
DR CTD; 4234; -.
DR DisGeNET; 4234; -.
DR GeneCards; METTL1; -.
DR HGNC; HGNC:7030; METTL1.
DR HPA; ENSG00000037897; Low tissue specificity.
DR MIM; 604466; gene.
DR neXtProt; NX_Q9UBP6; -.
DR OpenTargets; ENSG00000037897; -.
DR PharmGKB; PA30766; -.
DR VEuPathDB; HostDB:ENSG00000037897; -.
DR eggNOG; KOG3115; Eukaryota.
DR GeneTree; ENSGT00390000017840; -.
DR HOGENOM; CLU_050910_3_0_1; -.
DR InParanoid; Q9UBP6; -.
DR OMA; DLHNWMV; -.
DR OrthoDB; 1417652at2759; -.
DR PhylomeDB; Q9UBP6; -.
DR TreeFam; TF314083; -.
DR PathwayCommons; Q9UBP6; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q9UBP6; -.
DR SIGNOR; Q9UBP6; -.
DR UniPathway; UPA00989; -.
DR BioGRID-ORCS; 4234; 326 hits in 1097 CRISPR screens.
DR ChiTaRS; METTL1; human.
DR EvolutionaryTrace; Q9UBP6; -.
DR GeneWiki; METTL1; -.
DR GenomeRNAi; 4234; -.
DR Pharos; Q9UBP6; Tbio.
DR PRO; PR:Q9UBP6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UBP6; protein.
DR Bgee; ENSG00000037897; Expressed in cervix squamous epithelium and 143 other tissues.
DR ExpressionAtlas; Q9UBP6; baseline and differential.
DR Genevisible; Q9UBP6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025763; Trm8_euk.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR23417; PTHR23417; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00091; TIGR00091; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Methyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..276
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171431"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055,
FT ECO:0000269|Ref.15, ECO:0007744|PDB:3CKK"
FT BINDING 107..109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.15, ECO:0007744|PDB:3CKK"
FT BINDING 140..141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.15, ECO:0007744|PDB:3CKK"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055,
FT ECO:0000269|Ref.15, ECO:0007744|PDB:3CKK"
FT BINDING 238..240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.15, ECO:0007744|PDB:3CKK"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 27
FT /note="Phosphoserine; by PKB and RPS6KA3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055,
FT ECO:0000269|PubMed:15861136, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 92..155
FT /note="VELSPLFPDTLILGLEIRVKVSDYVQDRIRALRAAPAGGFQNIACLRSNAMK
FT HLPNFFYKGQLT -> ADKDVLPLPRPTFQADKAQVANHQSHPASRICLRAKSWGAGVY
FT HNRCAGATRLDVHSFRRAPTV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044671"
FT VAR_SEQ 156..276
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044672"
FT MUTAGEN 27
FT /note="S->A: Able to complement a trm8-delta mutant yeast."
FT /evidence="ECO:0000269|PubMed:15861136"
FT MUTAGEN 27
FT /note="S->D,E: Abolishes ability to complement a trm8-delta
FT mutant yeast."
FT /evidence="ECO:0000269|PubMed:15861136"
FT MUTAGEN 107..109
FT /note="EIR->AAA: Abolished RNA methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31031083"
FT CONFLICT 18
FT /note="K -> R (in Ref. 3; BAD96922)"
FT /evidence="ECO:0000305"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3CKK"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3CKK"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:7OGJ"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3CKK"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:3CKK"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3CKK"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:3CKK"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:3CKK"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3CKK"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:3CKK"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:3CKK"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:3CKK"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:7OGJ"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:7OGJ"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:3CKK"
FT STRAND 188..199
FT /evidence="ECO:0007829|PDB:3CKK"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:3CKK"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3CKK"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:3CKK"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3CKK"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3CKK"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:3CKK"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:3CKK"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3CKK"
SQ SEQUENCE 276 AA; 31471 MW; 715AE85A18632892 CRC64;
MAAETRNVAG AEAPPPQKRY YRQRAHSNPM ADHTLRYPVK PEEMDWSELY PEFFAPLTQN
QSHDDPKDKK EKRAQAQVEF ADIGCGYGGL LVELSPLFPD TLILGLEIRV KVSDYVQDRI
RALRAAPAGG FQNIACLRSN AMKHLPNFFY KGQLTKMFFL FPDPHFKRTK HKWRIISPTL
LAEYAYVLRV GGLVYTITDV LELHDWMCTH FEEHPLFERV PLEDLSEDPV VGHLGTSTEE
GKKVLRNGGK NFPAIFRRIQ DPVLQAVTSQ TSLPGH
