TR112_HUMAN
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 03-AUG-2022, entry version 156.
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 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. 34:715-729(2020).
RN [16]
RP INTERACTION WITH THUMPD3; THUMPD2; BUD23; METTL5; N6AMT1; ALKBH8 AND
RP TRMT11, AND MUTAGENESIS OF THR-5; LEU-8; SER-10; MET-45; LYS-48; GLU-50;
RP GLU-92; PHE-107 AND ILE-113.
RX PubMed=34948388; DOI=10.3390/ijms222413593;
RA Brumele B., Mutso M., Telanne L., Ounap K., Spunde K., Abroi A., Kurg R.;
RT "Human TRMT112-Methyltransferase Network Consists of Seven Partners
RT Interacting with a Common Co-Factor.";
RL Int. J. Mol. Sci. 22:13593-13593(2021).
RN [17]
RP FUNCTION, AND INTERACTION WITH METTL5.
RX PubMed=33428944; DOI=10.1016/j.jbc.2021.100270;
RA Yu D., Kaur G., Blumenthal R.M., Zhang X., Cheng X.;
RT "Enzymatic characterization of three human RNA adenosine methyltransferases
RT reveals diverse substrate affinities and reaction optima.";
RL J. Biol. Chem. 296:100270-100270(2021).
RN [18]
RP FUNCTION, AND INTERACTION WITH THUMPD3.
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).
RN [19]
RP FUNCTION, AND INTERACTION WITH METTL5.
RX PubMed=35033535; DOI=10.1016/j.jbc.2022.101590;
RA Sepich-Poore C., Zheng Z., Schmitt E., Wen K., Zhang Z.S., Cui X.L.,
RA Dai Q., Zhu A.C., Zhang L., Sanchez Castillo A., Tan H., Peng J.,
RA Zhuang X., He C., Nachtergaele S.;
RT "The METTL5-TRMT112 N6-methyladenosine methyltransferase complex regulates
RT mRNA translation via 18S rRNA methylation.";
RL J. Biol. Chem. 298:101590-101590(2022).
RN [20] {ECO:0007744|PDB:6H2U, ECO:0007744|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 [21] {ECO:0007744|PDB:6KMR, ECO:0007744|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 [22] {ECO:0007744|PDB:6H1D, ECO:0007744|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 N6AMT1/HEMK2 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 N6AMT1/HEMK2
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). Together with methyltransferase THUMPD3, catalyzes
CC the formation of N(2)-methylguanosine at position 6 in a broad range of
CC tRNA substrates and at position 7 of tRNA(Trp) (PubMed:34669960).
CC Involved in the pre-rRNA processing steps leading to small-subunit rRNA
CC production (PubMed:25851604). Together with methyltransferase METTL5,
CC specifically methylates the 6th position of adenine in position 1832 of
CC 18S rRNA (PubMed:33428944, PubMed:35033535, 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 ECO:0000269|PubMed:33428944, ECO:0000269|PubMed:34669960}.
CC -!- SUBUNIT: Heterodimer with BUD23/WBSCR22; this heterodimerization is
CC necessary for the metabolic stability and activity of the catalytic
CC subunit BUD23 (PubMed:25851604, PubMed:34948388). Heterodimer with
CC N6AMT1/HEMK2; this heterodimerization is necessary for S-adenosyl-L-
CC methionine-binding to N6AMT1/HEMK2 (PubMed:20308323, PubMed:25851604,
CC PubMed:31632689, PubMed:31636962, PubMed:31061526, PubMed:34948388).
CC Heterodimer with ALKBH8 (PubMed:20308323, PubMed:34948388). Heterodimer
CC with METTL5; this heterodimerization is necessary for the stability of
CC the catalytic subunit METTL5 (PubMed:34948388, PubMed:32217665,
CC PubMed:33428944, PubMed:35033535, PubMed:31328227). Interacts with
CC THUMPD3; the interaction is direct and is required for THUMPD3
CC methyltransferase activity (PubMed:34948388, PubMed:34669960).
CC Interacts with THUMPD2 (PubMed:34948388). Interacts with TRMT11
CC (PubMed:34948388). {ECO:0000269|PubMed:20308323,
CC ECO:0000269|PubMed:25851604, ECO:0000269|PubMed:31061526,
CC ECO:0000269|PubMed:31328227, ECO:0000269|PubMed:31632689,
CC ECO:0000269|PubMed:31636962, ECO:0000269|PubMed:32217665,
CC ECO:0000269|PubMed:33428944, ECO:0000269|PubMed:34669960,
CC ECO:0000269|PubMed:34948388, ECO:0000269|PubMed:35033535}.
CC -!- INTERACTION:
CC Q9UI30; Q96BT7: ALKBH8; NbExp=5; IntAct=EBI-373326, EBI-10825637;
CC Q9UI30; O43709: BUD23; NbExp=5; 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; Q9Y5N5: N6AMT1; NbExp=2; IntAct=EBI-373326, EBI-7966667;
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}.
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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; 6KHS; X-ray; 1.90 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; 6KHS; -.
DR PDBsum; 6KMR; -.
DR PDBsum; 6KMS; -.
DR PDBsum; 6PED; -.
DR AlphaFoldDB; Q9UI30; -.
DR SMR; Q9UI30; -.
DR BioGRID; 119576; 68.
DR IntAct; Q9UI30; 33.
DR MINT; Q9UI30; -.
DR STRING; 9606.ENSP00000438349; -.
DR ChEMBL; CHEMBL4295977; -.
DR GlyGen; Q9UI30; 1 site, 1 O-linked glycan (1 site).
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 MaxQB; Q9UI30; -.
DR PaxDb; Q9UI30; -.
DR PeptideAtlas; Q9UI30; -.
DR PRIDE; Q9UI30; -.
DR ProteomicsDB; 84459; -. [Q9UI30-1]
DR TopDownProteomics; Q9UI30-1; -. [Q9UI30-1]
DR Antibodypedia; 29268; 88 antibodies from 18 providers.
DR DNASU; 51504; -.
DR Ensembl; ENST00000308774.6; ENSP00000309433.2; ENSG00000173113.7. [Q9UI30-2]
DR Ensembl; ENST00000544844.6; ENSP00000438349.2; ENSG00000173113.7. [Q9UI30-1]
DR GeneID; 51504; -.
DR KEGG; hsa:51504; -.
DR MANE-Select; ENST00000544844.6; ENSP00000438349.2; NM_016404.3; NP_057488.1.
DR UCSC; uc001nzt.5; human. [Q9UI30-1]
DR CTD; 51504; -.
DR DisGeNET; 51504; -.
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 VEuPathDB; HostDB:ENSG00000173113; -.
DR eggNOG; KOG1088; Eukaryota.
DR GeneTree; ENSGT00390000009268; -.
DR HOGENOM; CLU_086140_2_0_1; -.
DR InParanoid; Q9UI30; -.
DR OMA; NMLTSKC; -.
DR OrthoDB; 1465773at2759; -.
DR PhylomeDB; Q9UI30; -.
DR TreeFam; TF313256; -.
DR BioCyc; MetaCyc:ENSG00000173113-MON; -.
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 SignaLink; Q9UI30; -.
DR BioGRID-ORCS; 51504; 803 hits in 1054 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 203 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:0034968; P:histone lysine methylation; IDA:UniProtKB.
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:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002940; P:tRNA N2-guanine methylation; IMP: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 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:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 61..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054748"
FT MUTAGEN 5
FT /note="T->A: Abolishes interaction with N6AMT1, METTL5,
FT TRMT11, THUMPD3 and THUMPD2. Reduces interaction with BUD23
FT and ALKBH8. Reduces expression of exogenous TRMT112."
FT /evidence="ECO:0000269|PubMed:34948388"
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 8
FT /note="L->W: Abolishes interaction with METTL5 and THUMPD3.
FT Reduces interaction with ALKBH8, THUMPD2 and TRMT11. No
FT effect on interaction with N6AMT1 and BUD23. No effect on
FT expression of exogenous TRMT112."
FT /evidence="ECO:0000269|PubMed:34948388"
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 10
FT /note="S->F: Abolishes interaction with THUMPD2. Increases
FT expression of exogenous TRMT112. No effect on interaction
FT with N6AMT1, BUD23, METTL5, TRMT11, ALKBH8 and THUMPD3."
FT /evidence="ECO:0000269|PubMed:34948388"
FT MUTAGEN 45
FT /note="M->A: Abolishes interaction with METTL5 and THUMPD3.
FT Reduces interaction with ALKBH8 and THUMPD2. No effect on
FT interaction with N6AMT1, BUD23 and TRMT11. Reduces
FT expression of exogenous TRMT112."
FT /evidence="ECO:0000269|PubMed:34948388"
FT MUTAGEN 48
FT /note="K->A: Abolishes interaction with THUMPD2 and
FT THUMPD3. Reduces interaction with TRMT11, ALKBH8 and
FT N6AMT1. No effect on interaction with BUD23 and METTL5. No
FT effect on expression of exogenous TRMT112."
FT /evidence="ECO:0000269|PubMed:34948388"
FT MUTAGEN 50
FT /note="E->A: Increases interaction with METTL5. No effect
FT on interaction with TRMT11, THUMPD2, THUMPD3, N6AMT1, BUD23
FT and ALKBH8. No effect on expression of exogenous TRMT112."
FT /evidence="ECO:0000269|PubMed:34948388"
FT MUTAGEN 92
FT /note="E->A: Reduces interaction with THUMPD2, THUMPD3,
FT ALKBH8, TRMT11, N6AMT1 and BUD23. Increases interaction
FT with METTL5. Reduces expression of exogenous TRMT112."
FT /evidence="ECO:0000269|PubMed:34948388"
FT MUTAGEN 107
FT /note="F->A: Abolishes interaction with BUD23, THUMPD2 and
FT THUMPD3. Reduces interaction with TRMT11, N6AMT1, METTL5
FT and ALKBH8. Reduces expression of exogenous TRMT112."
FT /evidence="ECO:0000269|PubMed:34948388"
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 MUTAGEN 113
FT /note="I->F: Abolishes interaction with THUMPD2 and
FT THUMPD3. Reduces interaction with N6AMT1, BUD23, TRMT11 and
FT ALKBH8. Reduces expression of exogenous TRMT112. Increases
FT interaction with METTL5."
FT /evidence="ECO:0000269|PubMed:34948388"
FT CONFLICT 120
FT /note="E -> G (in Ref. 6; AAH29482)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:6KHS"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:6KMS"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:6KHS"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:6KHS"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6KHS"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:6KHS"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6KHS"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:6KHS"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:6KHS"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6KHS"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6KHS"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6KHS"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6KHS"
SQ SEQUENCE 125 AA; 14199 MW; A943569364D4FFEA CRC64;
MKLLTHNLLS SHVRGVGSRG FPLRLQATEV RICPVEFNPN FVARMIPKVE WSAFLEAADN
LRLIQVPKGP VEGYEENEEF LRTMHHLLLE VEVIEGTLQC PESGRMFPIS RGIPNMLLSE
EETES
