BUD23_HUMAN
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 03-AUG-2022, entry version 190.
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=5; 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};
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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 PDBsum; 6G4W; -.
DR AlphaFoldDB; O43709; -.
DR SMR; O43709; -.
DR BioGRID; 125277; 35.
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 PeptideAtlas; O43709; -.
DR PRIDE; O43709; -.
DR ProteomicsDB; 12493; -.
DR ProteomicsDB; 49128; -. [O43709-1]
DR ProteomicsDB; 49129; -. [O43709-2]
DR Antibodypedia; 28493; 144 antibodies from 25 providers.
DR DNASU; 114049; -.
DR Ensembl; ENST00000265758.7; ENSP00000265758.3; ENSG00000071462.12. [O43709-1]
DR Ensembl; ENST00000423497.5; ENSP00000401191.1; ENSG00000071462.12. [O43709-3]
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 CTD; 114049; -.
DR DisGeNET; 114049; -.
DR GeneCards; BUD23; -.
DR HGNC; HGNC:16405; BUD23.
DR HPA; ENSG00000071462; Low tissue specificity.
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; QWLCQAD; -.
DR OrthoDB; 1138059at2759; -.
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; 740 hits in 1082 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 209 other tissues.
DR ExpressionAtlas; O43709; baseline and differential.
DR Genevisible; O43709; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
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 Gene3D; 3.40.50.150; -; 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; PTHR12734; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF12589; WBS_methylT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
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"
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
