UTP8_YEAST
ID UTP8_YEAST Reviewed; 713 AA.
AC P53276; D6VUR0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=U3 small nucleolar RNA-associated protein 8;
DE Short=U3 snoRNA-associated protein 8;
DE AltName: Full=U three protein 8;
DE AltName: Full=U3 protein 8 required for transcription;
DE AltName: Full=t-UTP8;
GN Name=UTP8; OrderedLocusNames=YGR128C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
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 [3]
RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12068309; DOI=10.1038/nature00769;
RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT biogenesis.";
RL Nature 417:967-970(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12794079; DOI=10.1074/jbc.m302779200;
RA Steiner-Mosonyi M., Leslie D.M., Dehghani H., Aitchison J.D., Mangroo D.;
RT "Utp8p is an essential intranuclear component of the nuclear tRNA export
RT machinery of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:32236-32245(2003).
RN [5]
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 [6]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH OTHER T-UTPS, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15489292; DOI=10.1101/gad.1226604;
RA Gallagher J.E.G., Dunbar D.A., Granneman S., Mitchell B.M., Osheim Y.,
RA Beyer A.L., Baserga S.J.;
RT "RNA polymerase I transcription and pre-rRNA processing are linked by
RT specific SSU processome components.";
RL Genes Dev. 18:2506-2517(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95 AND SER-150, 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 [10]
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).
CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC Also has a role in nuclear tRNA export. It acts between the steps of
CC tRNA maturation/aminoacylation and its subsequent translocation out of
CC the nucleus. Required for optimal pre-ribosomal RNA transcription by
CC RNA polymerase I together with a subset of U3 proteins required for
CC transcription (t-UTPs). {ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:12794079, ECO:0000269|PubMed:15489292}.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10 and UTP25.
CC Component of the ribosomal small subunit (SSU) processome composed of
CC at least 40 protein subunits and snoRNA U3. In the absence of snoRNA3,
CC forms a complex with other t-UTPs. This complex can associate with pre-
CC 18S ribosomal RNAs. {ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:15489292, ECO:0000269|PubMed:20884785}.
CC -!- INTERACTION:
CC P53276; P47083: MPP10; NbExp=5; IntAct=EBI-23301, EBI-11168;
CC P53276; Q02931: NAN1; NbExp=5; IntAct=EBI-23301, EBI-37773;
CC P53276; P42945: UTP10; NbExp=4; IntAct=EBI-23301, EBI-1884;
CC P53276; Q04305: UTP15; NbExp=9; IntAct=EBI-23301, EBI-28183;
CC P53276; Q06679: UTP4; NbExp=6; IntAct=EBI-23301, EBI-35712;
CC P53276; P38882: UTP9; NbExp=6; IntAct=EBI-23301, EBI-24892;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:12794079, ECO:0000269|PubMed:15489292}.
CC Note=Associated with ribosomal chromatin, even in the absence of
CC transcription.
CC -!- MISCELLANEOUS: Present with 16800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z72913; CAA97140.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08221.1; -; Genomic_DNA.
DR PIR; S64437; S64437.
DR RefSeq; NP_011644.3; NM_001181257.3.
DR PDB; 5WLC; EM; 3.80 A; LI=549-713.
DR PDB; 6KE6; EM; 3.40 A; A8=1-713.
DR PDB; 6LQP; EM; 3.20 A; A8=1-713.
DR PDB; 6LQQ; EM; 4.10 A; A8=1-713.
DR PDB; 6LQR; EM; 8.60 A; A8=1-713.
DR PDB; 6LQS; EM; 3.80 A; A8=1-713.
DR PDB; 6LQU; EM; 3.70 A; A8=1-713.
DR PDB; 6LQV; EM; 4.80 A; A8=1-713.
DR PDB; 6ND4; EM; 4.30 A; I=549-713.
DR PDB; 6ZQA; EM; 4.40 A; UH=1-713.
DR PDB; 6ZQB; EM; 3.90 A; UH=1-713.
DR PDB; 6ZQC; EM; 3.80 A; UH=1-713.
DR PDB; 6ZQD; EM; 3.80 A; UH=1-713.
DR PDB; 6ZQE; EM; 7.10 A; UH=1-713.
DR PDB; 7AJT; EM; 4.60 A; UH=1-713.
DR PDB; 7AJU; EM; 3.80 A; UH=1-713.
DR PDB; 7D4I; EM; 4.00 A; A8=1-713.
DR PDB; 7D5S; EM; 4.60 A; A8=1-713.
DR PDB; 7D63; EM; 12.30 A; A8=1-713.
DR PDBsum; 5WLC; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
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; 7D63; -.
DR AlphaFoldDB; P53276; -.
DR SMR; P53276; -.
DR BioGRID; 33376; 382.
DR ComplexPortal; CPX-1409; UTP-A complex.
DR DIP; DIP-6747N; -.
DR IntAct; P53276; 31.
DR MINT; P53276; -.
DR STRING; 4932.YGR128C; -.
DR TCDB; 9.A.50.1.1; the nuclear t-rna exporter (trna-e) family.
DR iPTMnet; P53276; -.
DR MaxQB; P53276; -.
DR PaxDb; P53276; -.
DR PRIDE; P53276; -.
DR EnsemblFungi; YGR128C_mRNA; YGR128C; YGR128C.
DR GeneID; 853029; -.
DR KEGG; sce:YGR128C; -.
DR SGD; S000003360; UTP8.
DR VEuPathDB; FungiDB:YGR128C; -.
DR eggNOG; ENOG502QQ4S; Eukaryota.
DR HOGENOM; CLU_024075_0_0_1; -.
DR InParanoid; P53276; -.
DR OMA; KQAIVTC; -.
DR BioCyc; YEAST:G3O-30834-MON; -.
DR PRO; PR:P53276; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53276; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0034455; C:t-UTP complex; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR InterPro; IPR018843; Utp8.
DR Pfam; PF10395; Utp8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing; Transcription.
FT CHAIN 1..713
FT /note="U3 small nucleolar RNA-associated protein 8"
FT /id="PRO_0000065743"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 713 AA; 80191 MW; 6F5AE1492F841F49 CRC64;
MPSLSQPFRL ATLPKIASLS NFSLQADYVQ VADGTFNEST NNITLGISGS SISQYIINPT
PKLTFDYPIP STNIITACNA EKGQANIDGN IEASTDDEAN NEKTINTQKK RNVEIWAFGL
MVNKGNYTLN VITKALEDTT DTSNDHLSES DIDNKAYTGS DEFLSQYKIK AKAKVMSIKI
DTKNSLVIAI LQNGLIEIFD FKLTLLHSFD ISYDNLKYAK WFTENGTEYV FVLCPLQDDK
VCYKLLELTD CGSGESSPIK ELSSTIIEGF SFENSKLCYQ FGKLYKLNQG KIYIYSLPHC
QLQQVIEFPM VDKLSPGDDL ISFQPVSVNR VLLTVNNVIY LLDLLHCSTL SQRELTHVKT
FQLLKSAVIN SEKSHNSKTI AIGISTKNGP NPTSSLEIIN IDVGTNTLKD SLGKSFQVGN
NDSSVILKPL FDDKDINDKR VKCNDVSGDS SVPVLHCNEV IEKLSALQDN DITSFDDIFF
KELKIKEEHY TEKDRYISDP GFLNKVLDLI FGKFSGNDYP KTLTFLLTHP LFPLSRTRNL
LSLLRDQPRL FKQAIVTCPN LPLNELLEEL FSIRNRELLL DISFRILQDF TRDSIKQEMK
KLSKLDVQNF IEFITSGGED SSPECFNPSQ STQLFQLLSL VLDSIGLFSL EGALLENLTL
YIDKQVEIAE RNTELWNLID TKGFQHGFAS STFDNGTSQK RALPTYTMEY LDI
