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BUD23_BOVIN
ID   BUD23_BOVIN             Reviewed;         281 AA.
AC   Q58DP0; Q2TBN2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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, 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:O43709}. 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; BT021557; AAX46404.1; -; mRNA.
DR   EMBL; BC109889; AAI09890.1; -; mRNA.
DR   RefSeq; NP_001029629.2; NM_001034457.2.
DR   AlphaFoldDB; Q58DP0; -.
DR   SMR; Q58DP0; -.
DR   STRING; 9913.ENSBTAP00000022697; -.
DR   PaxDb; Q58DP0; -.
DR   PRIDE; Q58DP0; -.
DR   GeneID; 513878; -.
DR   KEGG; bta:513878; -.
DR   CTD; 114049; -.
DR   eggNOG; KOG1541; Eukaryota.
DR   HOGENOM; CLU_055194_0_2_1; -.
DR   InParanoid; Q58DP0; -.
DR   OrthoDB; 1138059at2759; -.
DR   TreeFam; TF300750; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
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   2: Evidence at transcript 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_0000247014"
FT   REGION          256..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        3
FT                   /note="F -> I (in Ref. 2; AAI09890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="P -> S (in Ref. 2; AAI09890)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  31687 MW;  F45ACE99A6B46D9D CRC64;
     MAFRGRRPEL RGPPELYYDK NEARKYVRNS RMIDVQIKMT GRALELLCVP EDKPCYVLDI
     GCGTGLSGDY LSDEGHYWVG IDISPAMLDE ALDRETQGDV ILGDMGQGIP FKPGTFDACI
     SISAVQWLCN ANKKSDIPAK RLYCFFSSLY SVLVRGGRAV LQLYPENSEQ LELITTQATR
     AGFTGGVVVD YPNSAKAKKF YLCLFSGPST SLPEGLSEDT EEEKPAESTF TADRIPYRIA
     RRGVVRKSRE WVLEKKARRR RQGKEVCPDT QYTGRKRKPR F
 
 
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