ID TR112_MOUSE Reviewed; 125 AA. AC Q9DCG9; Q91YP8; Q9D1N6; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 03-AUG-2022, entry version 137. DE RecName: Full=Multifunctional methyltransferase subunit TRM112-like protein; DE AltName: Full=tRNA methyltransferase 112 homolog; GN Name=Trmt112; 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; TISSUE=Embryo, and Kidney; 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]. 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Kidney, Lung, Pancreas, 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). RN [4] RP FUNCTION. RX PubMed=20606008; DOI=10.1128/mcb.00218-10; RA Liu P., Nie S., Li B., Yang Z.Q., Xu Z.M., Fei J., Lin C., Zeng R., RA Xu G.L.; RT "Deficiency in a glutamine-specific methyltransferase for release factor RT causes mouse embryonic lethality."; RL Mol. Cell. Biol. 30:4245-4253(2010). RN [5] RP FUNCTION, AND INTERACTION WITH N6AMT1. RX PubMed=26797129; DOI=10.1074/jbc.m115.711952; RA Kusevic D., Kudithipudi S., Jeltsch A.; RT "Substrate specificity of the HEMK2 protein glutamine methyltransferase and RT identification of novel substrates."; RL J. Biol. Chem. 291:6124-6133(2016). RN [6] RP TISSUE SPECIFICITY. RX PubMed=34669960; DOI=10.1093/nar/gkab927; RA Yang W.Q., Xiong Q.P., Ge J.Y., Li H., Zhu W.Y., Nie Y., Lin X., Lv D., RA Li J., Lin H., Liu R.J.; RT "THUMPD3-TRMT112 is a m2G methyltransferase working on a broad range of RT tRNA substrates."; RL Nucleic Acids Res. 49:11900-11919(2021). CC -!- FUNCTION: Acts as an activator of both rRNA/tRNA and protein CC methyltransferases (PubMed:20606008, PubMed:26797129). Together with CC methyltransferase BUD23, methylates the N(7) position of a guanine in CC 18S rRNA (By similarity). The heterodimer with HEMK2/N6AMT1 catalyzes CC N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as CC methyl donor (PubMed:20606008, PubMed:26797129). The heterodimer with CC ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5- CC methylcarboxymethyl uridine at the wobble position of the anticodon CC loop in target tRNA species (By similarity). Together with CC methyltransferase THUMPD3, catalyzes the formation of N(2)- CC methylguanosine at position 6 in a broad range of tRNA substrates and CC at position 7 of tRNA(Trp) (By similarity). Involved in the pre-rRNA CC processing steps leading to small-subunit rRNA production (By CC similarity). Together with methyltransferase METTL5, specifically CC methylates the 6th position of adenine in position 1832 of 18S rRNA (By CC similarity). {ECO:0000250|UniProtKB:Q9UI30, CC ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129}. CC -!- SUBUNIT: Heterodimer with BUD23/WBSCR22; this heterodimerization is CC necessary for the metabolic stability and activity of the catalytic CC subunit BUD23 (By similarity). Heterodimer with N6AMT1/HEMK2; this CC heterodimerization is necessary for S-adenosyl-L-methionine-binding to CC N6AMT1/HEMK2 (PubMed:26797129). Heterodimer with ALKBH8 (By CC similarity). Heterodimer with METTL5; this heterodimerization is CC necessary for the stability of the catalytic subunit METTL5 (By CC similarity). Interacts with THUMPD3; the interaction is direct and is CC required for THUMPD3 methyltransferase activity (By similarity). CC Interacts with THUMPD2 (By similarity). {ECO:0000250|UniProtKB:Q9UI30, CC ECO:0000269|PubMed:26797129}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm CC {ECO:0000250|UniProtKB:Q9UI30}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:Q9UI30}. Note=Localizes to a polarized CC perinuclear structure, overlapping partially with the Golgi and CC lysosomes. {ECO:0000250|UniProtKB:Q9UI30}. CC -!- TISSUE SPECIFICITY: Abundantly expressed in the testis, also expressed CC in the brain, heart, kidney, liver, lung, muscle and spleen. CC {ECO:0000269|PubMed:34669960}. 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; AK002791; BAB22361.1; -; mRNA. DR EMBL; AK003292; BAB22695.1; -; mRNA. DR EMBL; BC016191; AAH16191.1; -; mRNA. DR CCDS; CCDS29508.1; -. DR RefSeq; NP_001159842.1; NM_001166370.1. DR RefSeq; NP_080582.3; NM_026306.3. DR AlphaFoldDB; Q9DCG9; -. DR SMR; Q9DCG9; -. DR BioGRID; 212357; 10. DR STRING; 10090.ENSMUSP00000112250; -. DR iPTMnet; Q9DCG9; -. DR PhosphoSitePlus; Q9DCG9; -. DR SwissPalm; Q9DCG9; -. DR EPD; Q9DCG9; -. DR jPOST; Q9DCG9; -. DR MaxQB; Q9DCG9; -. DR PaxDb; Q9DCG9; -. DR PRIDE; Q9DCG9; -. DR ProteomicsDB; 259173; -. DR Antibodypedia; 29268; 88 antibodies from 18 providers. DR Ensembl; ENSMUST00000088257; ENSMUSP00000085591; ENSMUSG00000038812. DR Ensembl; ENSMUST00000116551; ENSMUSP00000112250; ENSMUSG00000038812. DR GeneID; 67674; -. DR KEGG; mmu:67674; -. DR UCSC; uc008gjd.2; mouse. DR CTD; 51504; -. DR MGI; MGI:1914924; Trmt112. DR VEuPathDB; HostDB:ENSMUSG00000038812; -. DR eggNOG; KOG1088; Eukaryota. DR GeneTree; ENSGT00390000009268; -. DR HOGENOM; CLU_086140_2_0_1; -. DR InParanoid; Q9DCG9; -. DR OMA; NMLTSKC; -. DR OrthoDB; 1465773at2759; -. DR PhylomeDB; Q9DCG9; -. DR TreeFam; TF313256; -. DR Reactome; R-MMU-156581; Methylation. DR Reactome; R-MMU-72764; Eukaryotic Translation Termination. DR BioGRID-ORCS; 67674; 25 hits in 73 CRISPR screens. DR ChiTaRS; Trmt112; mouse. DR PRO; PR:Q9DCG9; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q9DCG9; protein. DR Bgee; ENSMUSG00000038812; Expressed in embryonic brain and 103 other tissues. DR ExpressionAtlas; Q9DCG9; baseline and differential. DR Genevisible; Q9DCG9; MM. DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0008276; F:protein methyltransferase activity; ISO:MGI. DR GO; GO:0034968; P:histone lysine methylation; ISS:UniProtKB. DR GO; GO:0018364; P:peptidyl-glutamine methylation; IDA:UniProtKB. DR GO; GO:2000234; P:positive regulation of rRNA processing; ISS:UniProtKB. DR GO; GO:0070476; P:rRNA (guanine-N7)-methylation; ISS:UniProtKB. DR GO; GO:0031167; P:rRNA methylation; ISS:UniProtKB. DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central. DR GO; GO:0002940; P:tRNA N2-guanine methylation; ISS:UniProtKB. 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 Cytoplasm; Nucleus; Reference proteome. FT CHAIN 1..125 FT /note="Multifunctional methyltransferase subunit TRM112- FT like protein" FT /id="PRO_0000215798" FT DOMAIN 2..119 FT /note="TRM112" FT CONFLICT 85 FT /note="H -> Q (in Ref. 1; BAB22695)" FT /evidence="ECO:0000305" FT CONFLICT 122 FT /note="Missing (in Ref. 2; AAH16191)" FT /evidence="ECO:0000305" SQ SEQUENCE 125 AA; 14141 MW; A749605B3982A6F6 CRC64; MKLLTHNLLS SHVRGVGTRG FPLRLQATEV RINPVEFNPE FVARMIPKVE WAALVQAADT LNLAEVPKEP TEGYEHDETF LRKMHHVLLE VDVLEGTLQC PESGRLFPIS RGIPNMLLND EETET //