Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable 18S rRNA (guanine-N(7))-methyltransferase

Gene

Bud23

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N7 position of a guanine in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors. Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements. Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro.By similarity

Catalytic activityi

S-adenosyl-L-methionine + guanine in 18S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine in 18S rRNA.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, Methyltransferase, Transferase
Biological processRibosome biogenesis, rRNA processing, Transcription, Transcription regulation
LigandS-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 18S rRNA (guanine-N(7))-methyltransferaseCurated (EC:2.1.1.-By similarity)
Alternative name(s):
Bud site selection protein 23 homolog
Williams-Beuren syndrome chromosomal region 22 protein homolog
rRNA methyltransferase and ribosome maturation factorBy similarity
Gene namesi
Name:Bud23By similarity
Synonyms:Wbscr22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1913388 Bud23

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002044511 – 281Probable 18S rRNA (guanine-N(7))-methyltransferaseAdd BLAST281

Post-translational modificationi

May be ubiquitinated and targeted to degradation in response to proinflammatory cytokine signaling.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ9CY21
MaxQBiQ9CY21
PaxDbiQ9CY21
PRIDEiQ9CY21

PTM databases

iPTMnetiQ9CY21
PhosphoSitePlusiQ9CY21

Expressioni

Gene expression databases

BgeeiENSMUSG00000005378
CleanExiMM_WBSCR22
ExpressionAtlasiQ9CY21 baseline and differential
GenevisibleiQ9CY21 MM

Interactioni

Subunit structurei

Heterodimer with TRMT112; this heterodimerization is necessary for the metabolic stability and activity of the catalytic subunit BUD23. Interacts with GRIP1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9CY21, 1 interactor
MINTiQ9CY21
STRINGi10090.ENSMUSP00000083146

Structurei

3D structure databases

ProteinModelPortaliQ9CY21
SMRiQ9CY21
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1541 Eukaryota
COG0500 LUCA
GeneTreeiENSGT00390000014737
HOGENOMiHOG000111527
HOVERGENiHBG054765
InParanoidiQ9CY21
KOiK19306
OMAiQMERKGK
OrthoDBiEOG091G0EVK
PhylomeDBiQ9CY21
TreeFamiTF300750

Family and domain databases

InterProiView protein in InterPro
IPR022238 Bud23
IPR013216 Methyltransf_11
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF08241 Methyltransf_11, 1 hit
PF12589 WBS_methylT, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit

Sequencei

Sequence statusi: Complete.

Q9CY21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRSRRPEH SGPPELFYDQ NEARKYVRNS RMIDIQTKMT ERALELLCLP
60 70 80 90 100
EGQPSYLLDI GCGSGLSGDY ISEEGHYWVG IDISPAMLDA ALDRDTEGDL
110 120 130 140 150
LLGDMGQGVP FRPGSFDGCI SISAVQWLCN ANKKSDVPAR RLYCFFSSLY
160 170 180 190 200
SALVRGARAV LQLYPENSEQ LELITTQATR AGFTGGVVVD FPNSAKAKKF
210 220 230 240 250
YLCLFSGPST SLPKGLTESQ DADQASESMF TSERAPHKKA RRDLVKKSRE
260 270 280
WVLEKKERRR RQGKEVRPDT QYTGRKRKPR F
Length:281
Mass (Da):31,587
Last modified:June 1, 2001 - v1
Checksum:i5A71DDB525453FDC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF412035 mRNA Translation: AAM62317.1
AK011005 mRNA Translation: BAB27324.1
AK151986 mRNA Translation: BAE30852.1
CCDSiCCDS19732.2
RefSeqiNP_079651.2, NM_025375.3
UniGeneiMm.439878

Genome annotation databases

EnsembliENSMUST00000085984; ENSMUSP00000083146; ENSMUSG00000005378
GeneIDi66138
KEGGimmu:66138
UCSCiuc008zxn.1 mouse

Similar proteinsi

Entry informationi

Entry nameiBUD23_MOUSE
AccessioniPrimary (citable) accession number: Q9CY21
Secondary accession number(s): Q3U915
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2001
Last modified: April 25, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health