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 10-APR-2019, entry version 121. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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 RT 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 RT factor 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 RT methyltransferase and identification of novel substrates."; RL J. Biol. Chem. 291:6124-6133(2016). CC -!- FUNCTION: Acts as an activator of both rRNA/tRNA and protein CC methyltransferases (PubMed:26797129). Together with CC methyltransferase BUD23, methylates the N(7) position of a guanine CC in 18S rRNA (By similarity). The heterodimer with HEMK2/N6AMT1 CC catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L- CC methionine as methyl donor (PubMed:20606008, PubMed:26797129). The CC heterodimer with ALKBH8 catalyzes the methylation of 5- CC carboxymethyl uridine to 5-methylcarboxymethyl uridine at the CC wobble position of the anticodon loop in target tRNA species (By CC similarity). Involved in the pre-rRNA processing steps leading to CC small-subunit rRNA production (By similarity). CC {ECO:0000250|UniProtKB:Q9UI30, ECO:0000269|PubMed:20606008, CC ECO:0000269|PubMed:26797129}. CC -!- SUBUNIT: Heterodimer with BUD23; this heterodimerization is CC necessary for the metabolic stability and activity of the CC catalytic subunit BUD23 (By similarity). Heterodimer with CC N6AMT1/HEMK2 (PubMed:26797129). Heterodimer with ALKBH8 (By CC 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 -!- 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 UniGene; Mm.318804; -. DR UniGene; Mm.371597; -. DR ProteinModelPortal; Q9DCG9; -. DR SMR; Q9DCG9; -. DR IntAct; Q9DCG9; 1. DR MINT; Q9DCG9; -. 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 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 eggNOG; KOG1088; Eukaryota. DR eggNOG; ENOG4111NTJ; LUCA. DR GeneTree; ENSGT00390000009268; -. DR HOGENOM; HOG000181652; -. DR HOVERGEN; HBG056590; -. DR InParanoid; Q9DCG9; -. DR KO; K15448; -. DR OMA; EEGAMVC; -. DR OrthoDB; 1465773at2759; -. DR PhylomeDB; Q9DCG9; -. DR TreeFam; TF313256; -. DR Reactome; R-MMU-156581; Methylation. DR Reactome; R-MMU-72764; Eukaryotic Translation Termination. DR PRO; PR:Q9DCG9; -. DR Proteomes; UP000000589; Chromosome 19. DR Bgee; ENSMUSG00000038812; Expressed in 84 organ(s), highest expression level in thymus. 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:0016435; F:rRNA (guanine) methyltransferase activity; IEA:Ensembl. 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: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 Complete proteome; Cytoplasm; Nucleus; Reference proteome. FT CHAIN 1 125 Multifunctional methyltransferase subunit FT TRM112-like protein. FT /FTId=PRO_0000215798. FT DOMAIN 2 119 TRM112. FT CONFLICT 85 85 H -> Q (in Ref. 1; BAB22695). FT {ECO:0000305}. FT CONFLICT 122 122 Missing (in Ref. 2; AAH16191). FT {ECO:0000305}. SQ SEQUENCE 125 AA; 14141 MW; A749605B3982A6F6 CRC64; MKLLTHNLLS SHVRGVGTRG FPLRLQATEV RINPVEFNPE FVARMIPKVE WAALVQAADT LNLAEVPKEP TEGYEHDETF LRKMHHVLLE VDVLEGTLQC PESGRLFPIS RGIPNMLLND EETET //