ID PWP2_YEAST Reviewed; 923 AA.
AC P25635; D6VR63; P25633; P25636;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 01-MAY-2013, entry version 134.
DE RecName: Full=Periodic tryptophan protein 2;
DE AltName: Full=U three protein 1;
DE AltName: Full=U3 small nucleolar RNA-associated protein 1;
DE Short=U3 snoRNA-associated protein 1;
GN Name=PWP2; Synonyms=UTP1; OrderedLocusNames=YCR057C;
GN ORFNames=YCR55C/YCR57C/YCR58C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8804409; DOI=10.1007/s004389670012;
RA Shafaatian R., Payton M.A., Reid J.D.;
RT "PWP2, a member of the WD-repeat family of proteins, is an essential
RT Saccharomyces cerevisiae gene involved in cell separation.";
RL Mol. Gen. Genet. 252:101-114(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
RA Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
RA Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
RA Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
RA Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
RA de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
RA Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
RA Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
RA Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
RA Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
RA Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
RA Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
RA Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
RA van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
RA Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
RA Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION.
RA Gromadka R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
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.,
RA Shabanowitz J., 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 [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.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-651; SER-912
RP AND SER-913, AND MASS SPECTROMETRY.
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-232 AND SER-651, AND
RP MASS SPECTROMETRY.
RX PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT "Proteome-wide identification of in vivo targets of DNA damage
RT checkpoint kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-651; SER-660;
RP SER-664; SER-912 AND SER-913, AND MASS SPECTROMETRY.
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
RT phosphoproteome analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Required for bud-site selection and cell separation.
CC Also involved in nucleolar processing of pre-18S ribosomal RNA.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component
CC of the ribosomal small subunit (SSU) processome composed of at
CC least 40 protein subunits and snoRNA U3.
CC -!- INTERACTION:
CC Q12220:DIP2; NbExp=6; IntAct=EBI-14332, EBI-5896;
CC Q05946:UTP13; NbExp=7; IntAct=EBI-14332, EBI-34702;
CC Q06078:UTP21; NbExp=7; IntAct=EBI-14332, EBI-359;
CC P42942:YGR210C; NbExp=2; IntAct=EBI-14332, EBI-23482;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- MISCELLANEOUS: Present with 16700 molecules/cell in log phase SD
CC medium.
CC -!- SIMILARITY: Belongs to the WD repeat PWP2 family.
CC -!- SIMILARITY: Contains 14 WD repeats.
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DR EMBL; X78964; CAA55558.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42286.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07532.1; -; Genomic_DNA.
DR PIR; S44226; S44226.
DR RefSeq; NP_009984.1; NM_001178769.1.
DR ProteinModelPortal; P25635; -.
DR SMR; P25635; 19-708.
DR DIP; DIP-1868N; -.
DR IntAct; P25635; 116.
DR MINT; MINT-392472; -.
DR PaxDb; P25635; -.
DR PeptideAtlas; P25635; -.
DR EnsemblFungi; YCR057C; YCR057C; YCR057C.
DR GeneID; 850422; -.
DR KEGG; sce:YCR057C; -.
DR CYGD; YCR057c; -.
DR SGD; S000000653; PWP2.
DR eggNOG; COG2319; -.
DR GeneTree; ENSGT00550000074981; -.
DR HOGENOM; HOG000160363; -.
DR KO; K14558; -.
DR OMA; VWQCDTP; -.
DR OrthoDB; EOG4350F7; -.
DR NextBio; 965992; -.
DR Genevestigator; P25635; -.
DR GermOnline; YCR057C; Saccharomyces cerevisiae.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
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:0030515; F:snoRNA binding; IPI:SGD.
DR GO; GO:0000910; P:cytokinesis; IMP: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:0030010; P:establishment of cell polarity; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 4.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR027145; PWP2.
DR InterPro; IPR011047; Quinonprotein_ADH-like_supfam.
DR InterPro; IPR007148; SSU_processome_Utp12.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR PANTHER; PTHR19858; PTHR19858; 1.
DR Pfam; PF04003; Utp12; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 13.
DR SUPFAM; SSF50998; Quin_alc_DH_like; 1.
DR SUPFAM; SSF50978; WD40_like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; Ribosome biogenesis; rRNA processing;
KW WD repeat.
FT CHAIN 1 923 Periodic tryptophan protein 2.
FT /FTId=PRO_0000051179.
FT REPEAT 12 52 WD 1.
FT REPEAT 53 93 WD 2.
FT REPEAT 94 132 WD 3.
FT REPEAT 144 183 WD 4.
FT REPEAT 189 228 WD 5.
FT REPEAT 258 297 WD 6.
FT REPEAT 300 340 WD 7.
FT REPEAT 343 382 WD 8.
FT REPEAT 385 424 WD 9.
FT REPEAT 428 470 WD 10.
FT REPEAT 471 510 WD 11.
FT REPEAT 513 552 WD 12.
FT REPEAT 575 614 WD 13.
FT REPEAT 676 714 WD 14.
FT COMPBIAS 226 240 Asp/Glu-rich (acidic).
FT COMPBIAS 862 923 Asp/Glu-rich (acidic).
FT MOD_RES 232 232 Phosphoserine.
FT MOD_RES 651 651 Phosphoserine.
FT MOD_RES 660 660 Phosphoserine.
FT MOD_RES 664 664 Phosphoserine.
FT MOD_RES 912 912 Phosphoserine.
FT MOD_RES 913 913 Phosphoserine.
SQ SEQUENCE 923 AA; 103983 MW; CBEE4720F81378B6 CRC64;
MKSDFKFSNL LGTVYRQGNI TFSDDGKQLL SPVGNRVSVF DLINNKSFTF EYEHRKNIAA
IDLNKQGTLL ISIDEDGRAI LVNFKARNVL HHFNFKEKCS AVKFSPDGRL FALASGRFLQ
IWKTPDVNKD RQFAPFVRHR VHAGHFQDIT SLTWSQDSRF ILTTSKDLSA KIWSVDSEEK
NLAATTFNGH RDYVMGAFFS HDQEKIYTVS KDGAVFVWEF TKRPSDDDDN ESEDDDKQEE
VDISKYSWRI TKKHFFYANQ AKVKCVTFHP ATRLLAVGFT SGEFRLYDLP DFTLIQQLSM
GQNPVNTVSV NQTGEWLAFG SSKLGQLLVY EWQSESYILK QQGHFDSTNS LAYSPDGSRV
VTASEDGKIK VWDITSGFCL ATFEEHTSSV TAVQFAKRGQ VMFSSSLDGT VRAWDLIRYR
NFRTFTGTER IQFNCLAVDP SGEVVCAGSL DNFDIHVWSV QTGQLLDALS GHEGPVSCLS
FSQENSVLAS ASWDKTIRIW SIFGRSQQVE PIEVYSDVLA LSMRPDGKEV AVSTLKGQIS
IFNIEDAKQV GNIDCRKDII SGRFNQDRFT AKNSERSKFF TTIHYSFDGM AIVAGGNNNS
ICLYDVPNEV LLKRFIVSRN MALNGTLEFL NSKKMTEAGS LDLIDDAGEN SDLEDRIDNS
LPGSQRGGDL STRKMRPEVR VTSVQFSPTA NAFAAASTEG LLIYSTNDTI LFDPFDLDVD
VTPHSTVEAL REKQFLNALV MAFRLNEEYL INKVYEAIPI KEIPLVASNI PAIYLPRILK
FIGDFAIESQ HIEFNLIWIK ALLSASGGYI NEHKYLFSTA MRSIQRFIVR VAKEVVNTTT
DNKYTYRFLV STDGSMEDGA ADDDEVLLKD DADEDNEENE ENDVVMESDD EEGWIGFNGK
DNKLPLSNEN DSSDEEENEK ELP
//
