ID TR112_HUMAN Reviewed; 125 AA. AC Q9UI30; B2R539; J3KNG5; Q3MHC7; Q8N2Z4; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 12-AUG-2020, entry version 147. DE RecName: Full=Multifunctional methyltransferase subunit TRM112-like protein; DE AltName: Full=tRNA methyltransferase 112 homolog; GN Name=TRMT112 {ECO:0000303|PubMed:25851604, ECO:0000312|HGNC:HGNC:26940}; GN ORFNames=AD-001, HSPC152, HSPC170; 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] (ISOFORM 1). RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Prostate; 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 [7] RP FUNCTION, AND INTERACTION WITH HEMK2/N6AMT1. RX PubMed=18539146; DOI=10.1016/j.febslet.2008.05.045; RA Figaro S., Scrima N., Buckingham R.H., Heurgue-Hamard V.; RT "HemK2 protein, encoded on human chromosome 21, methylates translation RT termination factor eRF1."; RL FEBS Lett. 582:2352-2356(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP INTERACTION WITH ALKBH8. RX PubMed=20308323; DOI=10.1128/mcb.01604-09; RA Fu D., Brophy J.A., Chan C.T., Atmore K.A., Begley U., Paules R.S., RA Dedon P.C., Begley T.J., Samson L.D.; RT "Human AlkB homolog ABH8 is a tRNA methyltransferase required for wobble RT uridine modification and DNA damage survival."; RL Mol. Cell. Biol. 30:2449-2459(2010). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-125, AND 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 [12] 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 [13] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=25851604; DOI=10.1091/mbc.e15-02-0073; RA Zorbas C., Nicolas E., Wacheul L., Huvelle E., Heurgue-Hamard V., RA Lafontaine D.L.; RT "The human 18S rRNA base methyltransferases DIMT1L and WBSCR22-TRMT112 but RT not rRNA modification are required for ribosome biogenesis."; RL Mol. Biol. Cell 26:2080-2095(2015). RN [14] RP INTERACTION WITH N6AMT1. RX PubMed=31632689; DOI=10.1038/s41421-019-0119-5; RA Woodcock C.B., Yu D., Zhang X., Cheng X.; RT "Human HemK2/KMT9/N6AMT1 is an active protein methyltransferase, but does RT not act on DNA in vitro, in the presence of Trm112."; RL Cell Discov. 5:50-50(2019). RN [15] RP INTERACTION WITH METTL5. RX PubMed=32217665; DOI=10.1101/gad.333369.119; RA Ignatova V.V., Stolz P., Kaiser S., Gustafsson T.H., Lastres P.R., RA Sanz-Moreno A., Cho Y.L., Amarie O.V., Aguilar-Pimentel A., RA Klein-Rodewald T., Calzada-Wack J., Becker L., Marschall S., Kraiger M., RA Garrett L., Seisenberger C., Hoelter S.M., Borland K., Van De Logt E., RA Jansen P.W.T.C., Baltissen M.P., Valenta M., Vermeulen M., Wurst W., RA Gailus-Durner V., Fuchs H., de Angelis M.H., Rando O.J., Kellner S.M., RA Bultmann S., Schneider R.; RT "The rRNA m6A methyltransferase METTL5 is involved in pluripotency and RT developmental programs."; RL Genes Dev. 0:0-0(2020). RN [16] {ECO:0000244|PDB:6H2U, ECO:0000244|PDB:6H2V} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-118 IN COMPLEX WITH METTL5, RP FUNCTION, AND INTERACTION WITH METTL5. RX PubMed=31328227; DOI=10.1093/nar/gkz619; RA van Tran N., Ernst F.G.M., Hawley B.R., Zorbas C., Ulryck N., Hackert P., RA Bohnsack K.E., Bohnsack M.T., Jaffrey S.R., Graille M., Lafontaine D.L.J.; RT "The human 18S rRNA m6A methyltransferase METTL5 is stabilized by RT TRMT112."; RL Nucleic Acids Res. 47:7719-7733(2019). RN [17] {ECO:0000244|PDB:6KMR, ECO:0000244|PDB:6KMS} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS)IN COMPLEX WITH N6AMT1, INTERACTION RP WITH N6AMT1, FUNCTION, AND MUTAGENESIS OF LEU-8; LEU-9 AND ILE-113. RX PubMed=31636962; DOI=10.1038/s41421-019-0121-y; RA Li W., Shi Y., Zhang T., Ye J., Ding J.; RT "Structural insight into human N6amt1-Trm112 complex functioning as a RT protein methyltransferase."; RL Cell Discov. 5:51-51(2019). RN [18] {ECO:0000244|PDB:6H1D, ECO:0000244|PDB:6H1E} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-125 IN COMPLEX WITH N6AMT1, RP FUNCTION, AND INTERACTION WITH N6AMT1. RX PubMed=31061526; DOI=10.1038/s41594-019-0219-9; RA Metzger E., Wang S., Urban S., Willmann D., Schmidt A., Offermann A., RA Allen A., Sum M., Obier N., Cottard F., Ulferts S., Preca B.T., Hermann B., RA Maurer J., Greschik H., Hornung V., Einsle O., Perner S., Imhof A., RA Jung M., Schule R.; RT "KMT9 monomethylates histone H4 lysine 12 and controls proliferation of RT prostate cancer cells."; RL Nat. Struct. Mol. Biol. 26:361-371(2019). CC -!- FUNCTION: Acts as an activator of both rRNA/tRNA and protein CC methyltransferases (PubMed:25851604, PubMed:18539146, PubMed:20308323, CC PubMed:25851604, PubMed:31328227, PubMed:31636962, PubMed:31061526). CC Together with methyltransferase BUD23, methylates the N(7) position of CC a guanine in 18S rRNA (PubMed:25851604). The heterodimer with CC HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on 'Gln-185', using S- CC adenosyl L-methionine as methyl donor (PubMed:18539146, CC PubMed:31636962, PubMed:31061526). The heterodimer with HEMK2/N6AMT1 CC also monomethylates 'Lys-12' of histone H4 (H4K12me1) CC (PubMed:31061526). The heterodimer with ALKBH8 catalyzes the CC methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine CC at the wobble position of the anticodon loop in target tRNA species CC (PubMed:20308323). Involved in the pre-rRNA processing steps leading to CC small-subunit rRNA production (PubMed:25851604). Together with CC methyltransferase METTL5, specifically methylates the 6th position of CC adenine in position 1832 of 18S rRNA (PubMed:31328227). CC {ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:20308323, CC ECO:0000269|PubMed:25851604, ECO:0000269|PubMed:31061526, CC ECO:0000269|PubMed:31328227, ECO:0000269|PubMed:31636962}. CC -!- SUBUNIT: Heterodimer with BUD23; this heterodimerization is necessary CC for the metabolic stability and activity of the catalytic subunit BUD23 CC (PubMed:25851604). Heterodimer with N6AMT1/HEMK2; this CC heterodimerization is necessary for S-adenosyl-L-methionine-binding to CC N6AMT1/HEMK2 (PubMed:20308323, PubMed:25851604, PubMed:31632689, CC PubMed:31636962, PubMed:31061526). Heterodimer with ALKBH8 CC (PubMed:20308323). Heterodimer with METTL5; this heterodimerization is CC necessary for the stability of the catalytic subunit METTL5 CC (PubMed:31328227, PubMed:32217665). {ECO:0000269|PubMed:18539146, CC ECO:0000269|PubMed:20308323, ECO:0000269|PubMed:25851604, CC ECO:0000269|PubMed:31061526, ECO:0000269|PubMed:31328227, CC ECO:0000269|PubMed:31632689, ECO:0000269|PubMed:31636962, CC ECO:0000269|PubMed:32217665}. CC -!- INTERACTION: CC Q9UI30; Q96BT7: ALKBH8; NbExp=5; IntAct=EBI-373326, EBI-10825637; CC Q9UI30; O43709: BUD23; NbExp=4; IntAct=EBI-373326, EBI-1044726; CC Q9UI30; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-373326, EBI-16439278; CC Q9UI30; Q9NRN9: METTL5; NbExp=3; IntAct=EBI-373326, EBI-12360031; CC Q9UI30; Q9BV44: THUMPD3; NbExp=4; IntAct=EBI-373326, EBI-373253; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm CC {ECO:0000269|PubMed:25851604}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:25851604}. Note=Localizes to a polarized CC perinuclear structure, overlapping partially with the Golgi and CC lysosomes (PubMed:25851604). {ECO:0000269|PubMed:25851604}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UI30-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UI30-2; Sequence=VSP_054748; CC -!- SIMILARITY: Belongs to the TRM112 family. {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; AF110774; AAF14857.1; -; mRNA. DR EMBL; AF229068; AAF82266.1; -; mRNA. DR EMBL; AF161501; AAF29116.1; -; mRNA. DR EMBL; AK312050; BAG34986.1; -; mRNA. DR EMBL; AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74251.1; -; Genomic_DNA. DR EMBL; BC017172; AAH17172.1; -; mRNA. DR EMBL; BC029482; AAH29482.1; -; mRNA. DR EMBL; BC105294; AAI05295.1; -; mRNA. DR CCDS; CCDS66113.1; -. [Q9UI30-2] DR CCDS; CCDS8068.1; -. [Q9UI30-1] DR RefSeq; NP_001273011.1; NM_001286082.1. [Q9UI30-2] DR RefSeq; NP_057488.1; NM_016404.2. [Q9UI30-1] DR PDB; 6G4W; EM; 4.50 A; r=1-125. DR PDB; 6H1D; X-ray; 1.94 A; B=2-125. DR PDB; 6H1E; X-ray; 1.90 A; B=2-125. DR PDB; 6H2U; X-ray; 1.60 A; B=1-118. DR PDB; 6H2V; X-ray; 2.49 A; B/D=1-125. DR PDB; 6K0X; X-ray; 2.20 A; B=1-125. DR PDB; 6KMR; X-ray; 2.00 A; A=1-125. DR PDB; 6KMS; X-ray; 3.20 A; A/B=1-125. DR PDB; 6PED; X-ray; 2.30 A; B=1-125. DR PDBsum; 6G4W; -. DR PDBsum; 6H1D; -. DR PDBsum; 6H1E; -. DR PDBsum; 6H2U; -. DR PDBsum; 6H2V; -. DR PDBsum; 6K0X; -. DR PDBsum; 6KMR; -. DR PDBsum; 6KMS; -. DR PDBsum; 6PED; -. DR SMR; Q9UI30; -. DR BioGRID; 119576; 53. DR IntAct; Q9UI30; 28. DR MINT; Q9UI30; -. DR STRING; 9606.ENSP00000438349; -. DR ChEMBL; CHEMBL4295977; -. DR iPTMnet; Q9UI30; -. DR PhosphoSitePlus; Q9UI30; -. DR SwissPalm; Q9UI30; -. DR BioMuta; TRMT112; -. DR DMDM; 47606219; -. DR EPD; Q9UI30; -. DR jPOST; Q9UI30; -. DR MassIVE; Q9UI30; -. DR PaxDb; Q9UI30; -. DR PeptideAtlas; Q9UI30; -. DR PRIDE; Q9UI30; -. DR ProteomicsDB; 84459; -. [Q9UI30-1] DR TopDownProteomics; Q9UI30-1; -. [Q9UI30-1] DR Antibodypedia; 29268; 80 antibodies. DR DNASU; 51504; -. DR Ensembl; ENST00000308774; ENSP00000309433; ENSG00000173113. [Q9UI30-2] DR Ensembl; ENST00000544844; ENSP00000438349; ENSG00000173113. [Q9UI30-1] DR GeneID; 51504; -. DR KEGG; hsa:51504; -. DR UCSC; uc001nzt.5; human. [Q9UI30-1] DR CTD; 51504; -. DR DisGeNET; 51504; -. DR EuPathDB; HostDB:ENSG00000173113.6; -. DR GeneCards; TRMT112; -. DR HGNC; HGNC:26940; TRMT112. DR HPA; ENSG00000173113; Low tissue specificity. DR MIM; 618630; gene. DR neXtProt; NX_Q9UI30; -. DR OpenTargets; ENSG00000173113; -. DR PharmGKB; PA165543757; -. DR eggNOG; KOG1088; Eukaryota. DR GeneTree; ENSGT00390000009268; -. DR HOGENOM; CLU_086140_2_0_1; -. DR InParanoid; Q9UI30; -. DR KO; K15448; -. DR OMA; KVNEVEF; -. DR OrthoDB; 1465773at2759; -. DR PhylomeDB; Q9UI30; -. DR TreeFam; TF313256; -. DR BioCyc; MetaCyc:ENSG00000173113-MONOMER; -. DR PathwayCommons; Q9UI30; -. DR Reactome; R-HSA-156581; Methylation. DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol. DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol. DR Reactome; R-HSA-72764; Eukaryotic Translation Termination. DR BioGRID-ORCS; 51504; 753 hits in 873 CRISPR screens. DR ChiTaRS; TRMT112; human. DR GenomeRNAi; 51504; -. DR Pharos; Q9UI30; Tbio. DR PRO; PR:Q9UI30; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9UI30; protein. DR Bgee; ENSG00000173113; Expressed in oocyte and 240 other tissues. DR ExpressionAtlas; Q9UI30; baseline and differential. DR Genevisible; Q9UI30; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0008276; F:protein methyltransferase activity; IDA:MGI. DR GO; GO:0032259; P:methylation; TAS:Reactome. DR GO; GO:0018364; P:peptidyl-glutamine methylation; IDA:UniProtKB. DR GO; GO:2000234; P:positive regulation of rRNA processing; IMP:UniProtKB. DR GO; GO:0070476; P:rRNA (guanine-N7)-methylation; IMP:UniProtKB. DR GO; GO:0031167; P:rRNA methylation; IDA:UniProtKB. DR GO; GO:0006415; P:translational termination; TAS:Reactome. DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central. DR InterPro; IPR039127; Trm112. DR InterPro; IPR005651; Trm112-like. DR PANTHER; PTHR12773; PTHR12773; 1. DR Pfam; PF03966; Trm112p; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein; KW Reference proteome; rRNA processing. FT CHAIN 1..125 FT /note="Multifunctional methyltransferase subunit TRM112- FT like protein" FT /id="PRO_0000215797" FT DOMAIN 2..119 FT /note="TRM112" FT MOD_RES 119 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231" FT MOD_RES 125 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:20068231" FT VAR_SEQ 61..65 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_054748" FT MUTAGEN 8 FT /note="L->D: Strongly reduced ability to promote N5- FT methylation of ETF1 together with HEMK2/N6AMT1." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 9 FT /note="L->D: Strongly reduced ability to promote N5- FT methylation of ETF1 together with HEMK2/N6AMT1." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 113 FT /note="I->D: Strongly reduced ability to promote N5- FT methylation of ETF1 together with HEMK2/N6AMT1." FT /evidence="ECO:0000269|PubMed:31636962" FT CONFLICT 120 FT /note="E -> G (in Ref. 6; AAH29482)" FT /evidence="ECO:0000305" FT HELIX 3..6 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 17..20 FT /evidence="ECO:0000244|PDB:6KMS" FT STRAND 24..32 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 39..45 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 46..48 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 51..60 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 74..76 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 78..89 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 91..99 FT /evidence="ECO:0000244|PDB:6H1E" FT TURN 101..103 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 106..110 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 113..115 FT /evidence="ECO:0000244|PDB:6H1E" FT TURN 120..122 FT /evidence="ECO:0000244|PDB:6KMR" SQ SEQUENCE 125 AA; 14199 MW; A943569364D4FFEA CRC64; MKLLTHNLLS SHVRGVGSRG FPLRLQATEV RICPVEFNPN FVARMIPKVE WSAFLEAADN LRLIQVPKGP VEGYEENEEF LRTMHHLLLE VEVIEGTLQC PESGRMFPIS RGIPNMLLSE EETES //