ID BUD23_HUMAN Reviewed; 281 AA. AC O43709; A8K501; C9K060; Q96P12; Q9BQ58; Q9HBP9; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 2. DT 27-MAR-2024, entry version 199. DE RecName: Full=Probable 18S rRNA (guanine-N(7))-methyltransferase {ECO:0000305}; DE EC=2.1.1.- {ECO:0000269|PubMed:25851604}; DE AltName: Full=Bud site selection protein 23 homolog; DE AltName: Full=Metastasis-related methyltransferase 1; DE AltName: Full=Williams-Beuren syndrome chromosomal region 22 protein; DE AltName: Full=rRNA methyltransferase and ribosome maturation factor {ECO:0000312|HGNC:HGNC:16405}; GN Name=BUD23 {ECO:0000312|HGNC:HGNC:16405}; Synonyms=MERM1, WBSCR22; GN ORFNames=HUSSY-03, PP3381; 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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=11978965; DOI=10.1159/000057012; RA Doll A., Grzeschik K.-H.; RT "Characterization of two novel genes, WBSCR20 and WBSCR22, deleted in RT Williams-Beuren syndrome."; RL Cytogenet. Cell Genet. 95:20-27(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11124703; RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h; RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., RA Zimbello R., Lanfranchi G., Valle G.; RT "Characterization of 16 novel human genes showing high similarity to yeast RT sequences."; RL Yeast 18:69-80(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=12073013; DOI=10.1007/s00439-002-0710-x; RA Merla G., Ucla C., Guipponi M., Reymond A.; RT "Identification of additional transcripts in the Williams-Beuren syndrome RT critical region."; RL Hum. Genet. 110:429-438(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix, Lung, and Skin; 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 [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-240, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 FUNCTION IN RIBOSOME BIOGENESIS, AND SUBCELLULAR LOCATION. RX PubMed=24086612; DOI=10.1371/journal.pone.0075686; RA Ounap K., Kasper L., Kurg A., Kurg R.; RT "The human WBSCR22 protein is involved in the biogenesis of the 40S RT ribosomal subunits in mammalian cells."; RL PLoS ONE 8:E75686-E75686(2013). RN [12] RP FUNCTION AS NUCLEAR RECEPTOR COACTIVATOR, INTERACTION WITH GRIP1, PROBABLE RP UBIQUITINATION, INDUCTION BY TNF AND IFNG, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF LYS-180 AND LYS-196. RX PubMed=24488492; DOI=10.1074/jbc.m113.540906; RA Jangani M., Poolman T.M., Matthews L., Yang N., Farrow S.N., Berry A., RA Hanley N., Williamson A.J., Whetton A.D., Donn R., Ray D.W.; RT "The methyltransferase WBSCR22/Merm1 enhances glucocorticoid receptor RT function and is regulated in lung inflammation and cancer."; RL J. Biol. Chem. 289:8931-8946(2014). RN [13] RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, 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 TRMT112, AND SUBCELLULAR LOCATION. 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). CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that CC specifically methylates the N(7) position of a guanine in 18S rRNA CC (PubMed:25851604). Requires the methyltransferase adapter protein CC TRM112 for full rRNA methyltransferase activity (PubMed:25851604). CC Involved in the pre-rRNA processing steps leading to small-subunit rRNA CC production independently of its RNA-modifying catalytic activity CC (PubMed:25851604). Important for biogenesis end export of the 40S CC ribosomal subunit independent on its methyltransferase activity CC (PubMed:24086612). Locus-specific steroid receptor coactivator. CC Potentiates transactivation by glucocorticoid (NR3C1), CC mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) CC receptors (PubMed:24488492). Required for the maintenance of open CC chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the CC response elements (PubMed:24488492). Required for maintenance of CC dimethylation on histone H3 'Lys-79' (H3K79me2), although direct CC histone methyltransferase activity is not observed in vitro CC (PubMed:24488492). {ECO:0000250, ECO:0000269|PubMed:24086612, CC ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:25851604}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a guanosine in 18S rRNA + S-adenosyl-L-methionine = an N(7)- CC methylguanosine in 18S rRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:54584, Rhea:RHEA-COMP:13937, Rhea:RHEA-COMP:13938, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:74480; Evidence={ECO:0000269|PubMed:25851604}; CC -!- SUBUNIT: Heterodimer with TRMT112; this heterodimerization is necessary CC for the metabolic stability and activity of the catalytic subunit BUD23 CC (PubMed:25851604, PubMed:34948388). Interacts with GRIP1 CC (PubMed:24488492). {ECO:0000269|PubMed:24488492, CC ECO:0000269|PubMed:25851604, ECO:0000269|PubMed:34948388}. CC -!- INTERACTION: CC O43709; Q9UI30: TRMT112; NbExp=10; IntAct=EBI-1044726, EBI-373326; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24086612, CC ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:34948388}. Nucleus, CC nucleoplasm {ECO:0000269|PubMed:25851604}. Cytoplasm, perinuclear CC region {ECO:0000269|PubMed:25851604}. Cytoplasm CC {ECO:0000269|PubMed:24488492}. Note=Localized diffusely throughout the CC nucleus and the cytoplasm (PubMed:24488492). Localizes to a polarized CC perinuclear structure, overlapping partially with the Golgi and CC lysosomes (PubMed:25851604). Localization is not affected by CC glucocorticoid treatment (PubMed:24488492). CC {ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:25851604}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O43709-1; Sequence=Displayed; CC Name=2; CC IsoId=O43709-2; Sequence=VSP_011511; CC Name=3; CC IsoId=O43709-3; Sequence=VSP_054762; CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in heart, CC skeletal muscle and kidney. Detected at high levels in bronchial CC brushings and in normal lung (at protein level). In fetal lung tissue, CC expressed in the developing bronchial lumen lining cells (at protein CC level). Tends to be down-regulated in lungs affected by inflammatory CC diseases or neoplasia (at protein level). Expressed in immune cells, CC including B and T lymphocytes and macrophages. CC {ECO:0000269|PubMed:11978965, ECO:0000269|PubMed:12073013, CC ECO:0000269|PubMed:24488492}. CC -!- INDUCTION: Up-regulated in CD8+ T lymphocytes by treatment with anti- CC CD3 and in B lymphocytes by treatment with CD40 ligand and anti-B cell CC receptor antibody. In macrophages, no induction following LPS CC treatment. Down-regulated by a combined treatment with TNF and IFNG (at CC protein level). {ECO:0000269|PubMed:24488492}. CC -!- PTM: May be ubiquitinated and targeted to degradation in response to CC pro-inflammatory cytokine signaling. {ECO:0000305}. CC -!- DISEASE: Note=BUD23 is located in the Williams-Beuren syndrome (WBS) CC critical region. WBS results from a hemizygous deletion of several CC genes on chromosome 7q11.23, thought to arise as a consequence of CC unequal crossing over between highly homologous low-copy repeat CC sequences flanking the deleted region. Haploinsufficiency of BUD23 may CC be the cause of certain cardiovascular and musculo-skeletal CC abnormalities observed in the disease. {ECO:0000305|PubMed:11978965}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. BUD23/WBSCR22 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG17249.1; Type=Frameshift; Evidence={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; AF420248; AAL16066.1; -; mRNA. DR EMBL; AJ224442; CAA11944.1; -; mRNA. DR EMBL; AF412034; AAM62316.1; -; mRNA. DR EMBL; AK291116; BAF83805.1; -; mRNA. DR EMBL; AK315032; BAG37517.1; -; mRNA. DR EMBL; AF218007; AAG17249.1; ALT_SEQ; mRNA. DR EMBL; AC073846; AAS07473.1; -; Genomic_DNA. DR EMBL; CH471200; EAW69657.1; -; Genomic_DNA. DR EMBL; BC000169; AAH00169.2; -; mRNA. DR EMBL; BC001780; AAH01780.2; -; mRNA. DR EMBL; BC011696; AAH11696.2; -; mRNA. DR CCDS; CCDS5557.1; -. [O43709-1] DR CCDS; CCDS56490.1; -. [O43709-3] DR RefSeq; NP_001189489.1; NM_001202560.2. [O43709-3] DR RefSeq; NP_059998.2; NM_017528.4. [O43709-1] DR PDB; 6G4W; EM; 4.50 A; q=1-281. DR PDB; 7WTS; EM; 3.20 A; q=1-281. DR PDB; 7WTT; EM; 3.10 A; q=1-281. DR PDB; 7WTU; EM; 3.00 A; q=1-281. DR PDB; 7WTV; EM; 3.50 A; q=1-281. DR PDB; 7WTW; EM; 3.20 A; q=1-207. DR PDBsum; 6G4W; -. DR PDBsum; 7WTS; -. DR PDBsum; 7WTT; -. DR PDBsum; 7WTU; -. DR PDBsum; 7WTV; -. DR PDBsum; 7WTW; -. DR AlphaFoldDB; O43709; -. DR EMDB; EMD-32799; -. DR EMDB; EMD-32800; -. DR EMDB; EMD-32801; -. DR EMDB; EMD-32802; -. DR EMDB; EMD-32803; -. DR EMDB; EMD-4349; -. DR SMR; O43709; -. DR BioGRID; 125277; 46. DR ComplexPortal; CPX-2871; BUD23-TRM112 methyltransferase complex. DR IntAct; O43709; 22. DR MINT; O43709; -. DR STRING; 9606.ENSP00000401191; -. DR GlyGen; O43709; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O43709; -. DR MetOSite; O43709; -. DR PhosphoSitePlus; O43709; -. DR SwissPalm; O43709; -. DR BioMuta; BUD23; -. DR EPD; O43709; -. DR jPOST; O43709; -. DR MassIVE; O43709; -. DR MaxQB; O43709; -. DR PaxDb; 9606-ENSP00000401191; -. DR PeptideAtlas; O43709; -. DR ProteomicsDB; 12493; -. DR ProteomicsDB; 49128; -. [O43709-1] DR ProteomicsDB; 49129; -. [O43709-2] DR Pumba; O43709; -. DR Antibodypedia; 28493; 155 antibodies from 25 providers. DR DNASU; 114049; -. DR Ensembl; ENST00000265758.7; ENSP00000265758.3; ENSG00000071462.13. [O43709-1] DR GeneID; 114049; -. DR KEGG; hsa:114049; -. DR MANE-Select; ENST00000265758.7; ENSP00000265758.3; NM_017528.5; NP_059998.2. DR UCSC; uc003tyt.4; human. [O43709-1] DR AGR; HGNC:16405; -. DR CTD; 114049; -. DR DisGeNET; 114049; -. DR GeneCards; BUD23; -. DR HGNC; HGNC:16405; BUD23. DR HPA; ENSG00000071462; Low tissue specificity. DR MalaCards; BUD23; -. DR MIM; 194050; phenotype. DR MIM; 615733; gene. DR neXtProt; NX_O43709; -. DR OpenTargets; ENSG00000071462; -. DR Orphanet; 904; Williams syndrome. DR PharmGKB; PA38133; -. DR VEuPathDB; HostDB:ENSG00000071462; -. DR eggNOG; KOG1541; Eukaryota. DR GeneTree; ENSGT00390000014737; -. DR HOGENOM; CLU_055194_0_2_1; -. DR InParanoid; O43709; -. DR OMA; FYPKNDE; -. DR OrthoDB; 5486608at2759; -. DR PhylomeDB; O43709; -. DR TreeFam; TF300750; -. DR BRENDA; 2.1.1.309; 2681. DR PathwayCommons; O43709; -. DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR SignaLink; O43709; -. DR BioGRID-ORCS; 114049; 771 hits in 1159 CRISPR screens. DR ChiTaRS; WBSCR22; human. DR GeneWiki; WBSCR22; -. DR GenomeRNAi; 114049; -. DR Pharos; O43709; Tbio. DR PRO; PR:O43709; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; O43709; Protein. DR Bgee; ENSG00000071462; Expressed in right testis and 211 other cell types or tissues. DR ExpressionAtlas; O43709; baseline and differential. 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:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0008168; F:methyltransferase activity; NAS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IMP:UniProtKB. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:2000234; P:positive regulation of rRNA processing; IMP:UniProtKB. DR GO; GO:0070476; P:rRNA (guanine-N7)-methylation; IMP:UniProtKB. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR039769; Bud23-like. DR InterPro; IPR022238; Bud23_C. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR12734:SF0; 18S RRNA (GUANINE-N(7))-METHYLTRANSFERASE-RELATED; 1. DR PANTHER; PTHR12734; METHYLTRANSFERASE-RELATED; 1. DR Pfam; PF08241; Methyltransf_11; 1. DR Pfam; PF12589; WBS_methylT; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR Genevisible; O43709; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; Cytoplasm; KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; KW Ribosome biogenesis; rRNA processing; S-adenosyl-L-methionine; KW Transcription; Transcription regulation; Transferase; Ubl conjugation; KW Williams-Beuren syndrome. FT CHAIN 1..281 FT /note="Probable 18S rRNA (guanine-N(7))-methyltransferase" FT /id="PRO_0000204450" FT REGION 255..281 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 171..281 FT /note="LELITTQATKAGFSGGMVVDYPNSAKAKKFYLCLFSGPSTFIPEGLSENQDE FT VEPRESVFTNERFPLRMSRRGMVRKSRAWVLEKKERHRRQGREVRPDTQYTGRKRKPRF FT -> VSPSATGCAGELGDSTGKLSWGSDKESYADWREKEETCTLVWPLMAHLMT (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:11124703" FT /id="VSP_011511" FT VAR_SEQ 233 FT /note="E -> EREGGAFERRGIRGHQTR (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_054762" FT MUTAGEN 180 FT /note="K->R: Resistant to down-regulation in response to FT TNF and IFNG combined treatment and effective coactivator FT for NR3C1, even in the presence of TNF and IFNG; when FT associated R-196." FT /evidence="ECO:0000269|PubMed:24488492" FT MUTAGEN 196 FT /note="K->R: Resistant to down-regulation in response to FT TNF and IFNG combined treatment and effective coactivator FT for NR3C1, even in the presence of TNF and IFNG; when FT associated R-180." FT /evidence="ECO:0000269|PubMed:24488492" FT HELIX 8..11 FT /evidence="ECO:0007829|PDB:7WTU" FT HELIX 14..17 FT /evidence="ECO:0007829|PDB:7WTU" FT HELIX 20..28 FT /evidence="ECO:0007829|PDB:7WTU" FT HELIX 30..46 FT /evidence="ECO:0007829|PDB:7WTU" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:7WTU" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:7WTU" FT HELIX 66..74 FT /evidence="ECO:0007829|PDB:7WTU" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:7WTU" FT HELIX 85..93 FT /evidence="ECO:0007829|PDB:7WTU" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:7WTU" FT TURN 105..107 FT /evidence="ECO:0007829|PDB:7WTU" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:7WTU" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:7WTU" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:7WTU" FT HELIX 138..152 FT /evidence="ECO:0007829|PDB:7WTU" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:7WTU" FT HELIX 168..179 FT /evidence="ECO:0007829|PDB:7WTU" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:7WTU" FT STRAND 184..193 FT /evidence="ECO:0007829|PDB:7WTU" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:7WTT" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:7WTU" FT HELIX 250..261 FT /evidence="ECO:0007829|PDB:7WTU" SQ SEQUENCE 281 AA; 31880 MW; B090B5F0A156B36A CRC64; MASRGRRPEH GGPPELFYDE TEARKYVRNS RMIDIQTRMA GRALELLYLP ENKPCYLLDI GCGTGLSGSY LSDEGHYWVG LDISPAMLDE AVDREIEGDL LLGDMGQGIP FKPGTFDGCI SISAVQWLCN ANKKSENPAK RLYCFFASLF SVLVRGSRAV LQLYPENSEQ LELITTQATK AGFSGGMVVD YPNSAKAKKF YLCLFSGPST FIPEGLSENQ DEVEPRESVF TNERFPLRMS RRGMVRKSRA WVLEKKERHR RQGREVRPDT QYTGRKRKPR F //