UTP18_MOUSE
ID UTP18_MOUSE Reviewed; 552 AA.
AC Q5SSI6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=U3 small nucleolar RNA-associated protein 18 homolog;
DE AltName: Full=WD repeat-containing protein 50;
GN Name=Utp18; Synonyms=Wdr50;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-115 AND SER-206, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-115; SER-118;
RP SER-201; SER-202 AND SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-115 AND SER-118, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-115; SER-118;
RP SER-202 AND SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat UTP18 family. {ECO:0000305}.
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DR EMBL; AL663078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25245.1; -.
DR RefSeq; NP_001013393.1; NM_001013375.1.
DR AlphaFoldDB; Q5SSI6; -.
DR SMR; Q5SSI6; -.
DR BioGRID; 229843; 25.
DR STRING; 10090.ENSMUSP00000068103; -.
DR iPTMnet; Q5SSI6; -.
DR PhosphoSitePlus; Q5SSI6; -.
DR SwissPalm; Q5SSI6; -.
DR EPD; Q5SSI6; -.
DR jPOST; Q5SSI6; -.
DR MaxQB; Q5SSI6; -.
DR PaxDb; Q5SSI6; -.
DR PRIDE; Q5SSI6; -.
DR ProteomicsDB; 299665; -.
DR Antibodypedia; 30799; 75 antibodies from 19 providers.
DR DNASU; 217109; -.
DR Ensembl; ENSMUST00000066888; ENSMUSP00000068103; ENSMUSG00000054079.
DR GeneID; 217109; -.
DR KEGG; mmu:217109; -.
DR UCSC; uc007kxk.1; mouse.
DR CTD; 51096; -.
DR MGI; MGI:1923402; Utp18.
DR VEuPathDB; HostDB:ENSMUSG00000054079; -.
DR eggNOG; KOG2055; Eukaryota.
DR GeneTree; ENSGT00440000033919; -.
DR HOGENOM; CLU_011055_3_1_1; -.
DR InParanoid; Q5SSI6; -.
DR OMA; QFHPTST; -.
DR OrthoDB; 462558at2759; -.
DR PhylomeDB; Q5SSI6; -.
DR TreeFam; TF313426; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 217109; 30 hits in 75 CRISPR screens.
DR ChiTaRS; Utp18; mouse.
DR PRO; PR:Q5SSI6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SSI6; protein.
DR Bgee; ENSMUSG00000054079; Expressed in primitive streak and 252 other tissues.
DR ExpressionAtlas; Q5SSI6; baseline and differential.
DR Genevisible; Q5SSI6; MM.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045161; Utp18.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR18359; PTHR18359; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW rRNA processing; Ubl conjugation; WD repeat.
FT CHAIN 1..552
FT /note="U3 small nucleolar RNA-associated protein 18
FT homolog"
FT /id="PRO_0000051406"
FT REPEAT 245..284
FT /note="WD 1"
FT REPEAT 289..329
FT /note="WD 2"
FT REPEAT 376..415
FT /note="WD 3"
FT REPEAT 417..458
FT /note="WD 4"
FT REPEAT 467..508
FT /note="WD 5"
FT REPEAT 515..551
FT /note="WD 6"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5J1"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5J1"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5J1"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5J1"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5J1"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5J1"
SQ SEQUENCE 552 AA; 61218 MW; 770648B0A19103E1 CRC64;
MPPERKSRTR RDRRAGATPG RKARPGSGST PAKAARSSQR TQPAEPRAAP SAGSAAAAAE
EEESRLRQRN RLTLEDDKPA AERCLEQLVF GDVEDDEDAL LQRLRSSRGQ LHGSSDESEV
ENEAKDIFSQ KKKQPVWVDE DDEDEEIVDM SNNRFRKDIM KNASESKLSK DKLQKRLKEE
FQHAMGGVPD WAEAGSKRRT SSDDESEEDE DDLLQRTGNF ISTSTSLPRG ILKMKNCRPA
NAERPTTARI SSVQFHPGAQ VVMVSGVDNA ISLFQVDGKT NPKIQSIYLE KFPIFKACFS
ANGEEVLATS MHSKVLYVYD MLAGKLIPVH QVRGLKEKTV KQFEVSPDGS FLLISGIAGF
SHLLSMKTKE LIGSMKINGR IAASTFSSDS KRIYTYSENG EVYVWDVNSR KCMNRFLDEG
SLCGLSIAAS KNGQYVACGS KSGVVNIYNQ DSCLQQTNPK PIKAIMNLVT GVTSLAFNPT
TEILAVASRK MKEAVRLVHL PSCTVFSNFP VFKKSTLSRV QTMDFSPRGG YFALGNEKGR
ALMYRLHHYS DF
