BUD23_MOUSE
ID BUD23_MOUSE Reviewed; 281 AA.
AC Q9CY21; Q3U915;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable 18S rRNA (guanine-N(7))-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:O43709};
DE AltName: Full=Bud site selection protein 23 homolog;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 22 protein homolog;
DE AltName: Full=rRNA methyltransferase and ribosome maturation factor {ECO:0000250|UniProtKB:O43709};
GN Name=Bud23 {ECO:0000250|UniProtKB:O43709}; Synonyms=Wbscr22;
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 [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryonic liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
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).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the N(7) position of a guanine in 18S rRNA.
CC Requires the methyltransferase adapter protein TRM112 for full rRNA
CC methyltransferase activity. Involved in the pre-rRNA processing steps
CC leading to small-subunit rRNA production independently of its RNA-
CC modifying catalytic activity. Important for biogenesis end export of
CC the 40S ribosomal subunit independent on its methyltransferase
CC activity. Locus-specific steroid receptor coactivator. Potentiates
CC transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2),
CC androgen (AR) and progesterone (PGR) receptors. Required for the
CC maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate
CC NR3C1 loading on the response elements. Required for maintenance of
CC dimethylation on histone H3 'Lys-79' (H3K79me2), although direct
CC histone methyltransferase activity is not observed in vitro.
CC {ECO:0000250|UniProtKB:O43709}.
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:0000250|UniProtKB:O43709};
CC -!- SUBUNIT: Heterodimer with TRMT112; this heterodimerization is necessary
CC for the metabolic stability and activity of the catalytic subunit
CC BUD23. Interacts with GRIP1. {ECO:0000250|UniProtKB:O43709}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43709}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:P25627}. Cytoplasm, perinuclear
CC region {ECO:0000250|UniProtKB:O43709}. Cytoplasm
CC {ECO:0000250|UniProtKB:O43709}. Note=Localized diffusely throughout the
CC nucleus and the cytoplasm. Localizes to a polarized perinuclear
CC structure, overlapping partially with the Golgi and lysosomes.
CC Localization is not affected by glucocorticoid treatment.
CC {ECO:0000250|UniProtKB:O43709}.
CC -!- PTM: May be ubiquitinated and targeted to degradation in response to
CC pro-inflammatory cytokine signaling. {ECO:0000250|UniProtKB:O43709}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. BUD23/WBSCR22 family. {ECO:0000305}.
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DR EMBL; AF412035; AAM62317.1; -; mRNA.
DR EMBL; AK011005; BAB27324.1; -; mRNA.
DR EMBL; AK151986; BAE30852.1; -; mRNA.
DR CCDS; CCDS19732.2; -.
DR RefSeq; NP_079651.2; NM_025375.3.
DR AlphaFoldDB; Q9CY21; -.
DR SMR; Q9CY21; -.
DR BioGRID; 211241; 7.
DR STRING; 10090.ENSMUSP00000083146; -.
DR iPTMnet; Q9CY21; -.
DR PhosphoSitePlus; Q9CY21; -.
DR EPD; Q9CY21; -.
DR MaxQB; Q9CY21; -.
DR PaxDb; Q9CY21; -.
DR PRIDE; Q9CY21; -.
DR ProteomicsDB; 273717; -.
DR Antibodypedia; 28493; 144 antibodies from 25 providers.
DR DNASU; 66138; -.
DR Ensembl; ENSMUST00000085984; ENSMUSP00000083146; ENSMUSG00000005378.
DR GeneID; 66138; -.
DR KEGG; mmu:66138; -.
DR UCSC; uc008zxn.1; mouse.
DR CTD; 114049; -.
DR MGI; MGI:1913388; Bud23.
DR VEuPathDB; HostDB:ENSMUSG00000005378; -.
DR eggNOG; KOG1541; Eukaryota.
DR GeneTree; ENSGT00390000014737; -.
DR InParanoid; Q9CY21; -.
DR OMA; QWLCQAD; -.
DR OrthoDB; 1138059at2759; -.
DR PhylomeDB; Q9CY21; -.
DR TreeFam; TF300750; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 66138; 21 hits in 73 CRISPR screens.
DR ChiTaRS; Wbscr22; mouse.
DR PRO; PR:Q9CY21; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CY21; protein.
DR Bgee; ENSMUSG00000005378; Expressed in epiblast (generic) and 71 other tissues.
DR ExpressionAtlas; Q9CY21; baseline and differential.
DR Genevisible; Q9CY21; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:2000234; P:positive regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0070476; P:rRNA (guanine-N7)-methylation; ISS: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 Chromatin regulator; Cytoplasm; Methyltransferase; Nucleus;
KW Reference proteome; Ribosome biogenesis; rRNA processing;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation.
FT CHAIN 1..281
FT /note="Probable 18S rRNA (guanine-N(7))-methyltransferase"
FT /id="PRO_0000204451"
FT REGION 212..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 31587 MW; 5A71DDB525453FDC CRC64;
MASRSRRPEH SGPPELFYDQ NEARKYVRNS RMIDIQTKMT ERALELLCLP EGQPSYLLDI
GCGSGLSGDY ISEEGHYWVG IDISPAMLDA ALDRDTEGDL LLGDMGQGVP FRPGSFDGCI
SISAVQWLCN ANKKSDVPAR RLYCFFSSLY SALVRGARAV LQLYPENSEQ LELITTQATR
AGFTGGVVVD FPNSAKAKKF YLCLFSGPST SLPKGLTESQ DADQASESMF TSERAPHKKA
RRDLVKKSRE WVLEKKERRR RQGKEVRPDT QYTGRKRKPR F
