UTP18_YEAST
ID UTP18_YEAST Reviewed; 594 AA.
AC P40362; D6VWB4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=U3 small nucleolar RNA-associated protein 18;
DE Short=U3 snoRNA-associated protein 18;
DE AltName: Full=U three protein 18;
GN Name=UTP18; OrderedLocusNames=YJL069C; ORFNames=HRE594, J1098;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762302; DOI=10.1002/yea.320110108;
RA Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.;
RT "Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces
RT cerevisiae includes the mitochondrial ribosomal protein L8.";
RL Yeast 11:57-60(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME, AND SUBCELLULAR LOCATION.
RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA Baserga S.J.;
RT "The small-subunit processome is a ribosome assembly intermediate.";
RL Eukaryot. Cell 3:1619-1626(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP INTERACTION WITH UTP25.
RX PubMed=20884785; DOI=10.1261/rna.2359810;
RA Charette J.M., Baserga S.J.;
RT "The DEAD-box RNA helicase-like Utp25 is an SSU processome component.";
RL RNA 16:2156-2169(2010).
RN [10]
RP INTERACTION WITH UTP21.
RX PubMed=24466140; DOI=10.1371/journal.pone.0086540;
RA Zhang C., Lin J., Liu W., Chen X., Chen R., Ye K.;
RT "Structure of Utp21 tandem WD domain provides insight into the organization
RT of the UTPB complex involved in ribosome synthesis.";
RL PLoS ONE 9:E86540-E86540(2014).
CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA and
CC ribosome assembly. {ECO:0000269|PubMed:15590835}.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10, UTP21 and
CC UTP25. Component of the ribosomal small subunit (SSU) processome
CC composed of at least 40 protein subunits and snoRNA U3.
CC {ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:20884785,
CC ECO:0000269|PubMed:24466140}.
CC -!- INTERACTION:
CC P40362; P15790: CKA1; NbExp=3; IntAct=EBI-4534, EBI-9533;
CC P40362; P36009: DHR2; NbExp=2; IntAct=EBI-4534, EBI-5844;
CC P40362; P32899: IMP3; NbExp=2; IntAct=EBI-4534, EBI-9237;
CC P40362; P25586: KRR1; NbExp=2; IntAct=EBI-4534, EBI-21773;
CC P40362; P25635: PWP2; NbExp=14; IntAct=EBI-4534, EBI-14332;
CC P40362; Q06078: UTP21; NbExp=11; IntAct=EBI-4534, EBI-359;
CC P40362; P53254: UTP22; NbExp=4; IntAct=EBI-4534, EBI-1878;
CC P40362; Q06679: UTP4; NbExp=4; IntAct=EBI-4534, EBI-35712;
CC P40362; Q02354: UTP6; NbExp=11; IntAct=EBI-4534, EBI-22119;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15590835}.
CC -!- MISCELLANEOUS: Present with 9570 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat UTP18 family. {ECO:0000305}.
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DR EMBL; Z34288; CAA84053.1; -; Genomic_DNA.
DR EMBL; Z49344; CAA89360.1; -; Genomic_DNA.
DR EMBL; X88851; CAA61308.1; -; Genomic_DNA.
DR EMBL; AY692560; AAT92579.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08730.1; -; Genomic_DNA.
DR PIR; S50802; S50802.
DR RefSeq; NP_012466.1; NM_001181502.1.
DR PDB; 5WLC; EM; 3.80 A; LS=1-594.
DR PDB; 5WYJ; EM; 8.70 A; BD=1-594.
DR PDB; 5WYK; EM; 4.50 A; BD=1-594.
DR PDB; 6KE6; EM; 3.40 A; B8=1-594.
DR PDB; 6LQP; EM; 3.20 A; B8=1-594.
DR PDB; 6LQQ; EM; 4.10 A; B8=1-594.
DR PDB; 6LQR; EM; 8.60 A; B8=1-594.
DR PDB; 6LQS; EM; 3.80 A; B8=1-594.
DR PDB; 6LQT; EM; 4.90 A; B8=1-594.
DR PDB; 6LQU; EM; 3.70 A; B8=1-594.
DR PDB; 6LQV; EM; 4.80 A; B8=1-594.
DR PDB; 6ND4; EM; 4.30 A; S=1-594.
DR PDB; 6ZQA; EM; 4.40 A; UR=1-594.
DR PDB; 6ZQB; EM; 3.90 A; UR=1-594.
DR PDB; 6ZQC; EM; 3.80 A; UR=1-594.
DR PDB; 6ZQD; EM; 3.80 A; UR=1-594.
DR PDB; 6ZQE; EM; 7.10 A; UR=1-594.
DR PDB; 7AJT; EM; 4.60 A; UR=1-594.
DR PDB; 7AJU; EM; 3.80 A; UR=1-594.
DR PDB; 7D4I; EM; 4.00 A; B8=1-594.
DR PDB; 7D5S; EM; 4.60 A; B8=1-594.
DR PDB; 7D5T; EM; 6.00 A; B8=1-594.
DR PDB; 7D63; EM; 12.30 A; B8=1-594.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ND4; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P40362; -.
DR SMR; P40362; -.
DR BioGRID; 33686; 181.
DR ComplexPortal; CPX-1410; UTP-B complex.
DR DIP; DIP-6392N; -.
DR IntAct; P40362; 57.
DR MINT; P40362; -.
DR STRING; 4932.YJL069C; -.
DR iPTMnet; P40362; -.
DR MaxQB; P40362; -.
DR PaxDb; P40362; -.
DR PRIDE; P40362; -.
DR EnsemblFungi; YJL069C_mRNA; YJL069C; YJL069C.
DR GeneID; 853376; -.
DR KEGG; sce:YJL069C; -.
DR SGD; S000003605; UTP18.
DR VEuPathDB; FungiDB:YJL069C; -.
DR eggNOG; KOG2055; Eukaryota.
DR GeneTree; ENSGT00940000165670; -.
DR HOGENOM; CLU_011055_1_0_1; -.
DR InParanoid; P40362; -.
DR OMA; KIRMWEI; -.
DR BioCyc; YEAST:G3O-31528-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P40362; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40362; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000292; P:RNA fragment catabolic process; IMP:CACAO.
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 Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing; WD repeat.
FT CHAIN 1..594
FT /note="U3 small nucleolar RNA-associated protein 18"
FT /id="PRO_0000051330"
FT REPEAT 246..285
FT /note="WD 1"
FT REPEAT 290..334
FT /note="WD 2"
FT REPEAT 463..504
FT /note="WD 3"
FT REPEAT 513..554
FT /note="WD 4"
FT REPEAT 560..593
FT /note="WD 5"
FT REGION 48..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..190
FT /note="Interaction with UTP21"
FT /evidence="ECO:0000269|PubMed:24466140"
FT REGION 176..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..126
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 594 AA; 66424 MW; 0FEBD4540CF039DA CRC64;
MTMATTAMNV SVPPPDEEEQ LLAKFVFGDT TDLQENLAKF NADFIFNEQE MDVEDQEDEG
SESDNSEEDE AQNGELDHVN NDQLFFVDDG GNEDSQDKNE DTMDVDDEDD SSSDDYSEDS
EEAAWIDSDD EKIKVPILVT NKTKKLRTSY NESKINGVHY INRLRSQFEK IYPRPKWVDD
ESDSELDDEE DDEEEGSNNV INGDINALTK ILSTTYNYKD TLSNSKLLPP KKLDIVRLKD
ANASHPSHSA IQSLSFHPSK PLLLTGGYDK TLRIYHIDGK TNHLVTSLHL VGSPIQTCTF
YTSLSNQNQQ NIFTAGRRRY MHSWDLSLEN LTHSQTAKIE KFSRLYGHES TQRSFENFKV
AHLQNSQTNS VHGIVLLQGN NGWINILHST SGLWLMGCKI EGVITDFCID YQPISRGKFR
TILIAVNAYG EVWEFDLNKN GHVIRRWKDQ GGVGITKIQV GGGTTTTCPA LQISKIKQNR
WLAVGSESGF VNLYDRNNAM TSSTPTPVAA LDQLTTTISN LQFSPDGQIL CMASRAVKDA
LRLVHLPSCS VFSNWPTSGT PLGKVTSVAF SPSGGLLAVG NEQGKVRLWK LNHY
