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Database: UniProt
Entry: P25635
LinkDB: P25635
Original site: P25635 
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-OCT-2014, entry version 146.
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/BF02173210;
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;
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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-232; SER-651; SER-664;
RP   SER-912 AND SER-913, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-232; SER-651;
RP   SER-912 AND SER-913, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Required for bud-site selection and cell separation.
CC       Also involved in nucleolar processing of pre-18S ribosomal RNA.
CC       {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:8804409}.
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       {ECO:0000269|PubMed:12068309}.
CC   -!- INTERACTION:
CC       Q12220:DIP2; NbExp=6; IntAct=EBI-14332, EBI-5896;
CC       Q06078:UTP21; NbExp=7; IntAct=EBI-14332, EBI-359;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:12068309}.
CC   -!- MISCELLANEOUS: Present with 16700 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the WD repeat PWP2 family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 14 WD repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00221}.
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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; 19-723.
DR   BioGrid; 31035; 118.
DR   DIP; DIP-1868N; -.
DR   IntAct; P25635; 115.
DR   MINT; MINT-392472; -.
DR   MaxQB; P25635; -.
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; IRAWDLI; -.
DR   OrthoDB; EOG7BCNM6; -.
DR   BioCyc; YEAST:G3O-29363-MONOMER; -.
DR   NextBio; 965992; -.
DR   PRO; PR:P25635; -.
DR   Genevestigator; P25635; -.
DR   GO; GO:0030686; C:90S preribosome; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; 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:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0030515; F:snoRNA binding; IPI:SGD.
DR   GO; GO:0007109; P:cytokinesis, completion of separation; 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   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); 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; SSF50978; SSF50978; 3.
DR   SUPFAM; SSF50998; SSF50998; 2.
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     225    225       Phosphoserine.
FT                                {ECO:0000269|PubMed:19779198}.
FT   MOD_RES     232    232       Phosphoserine.
FT                                {ECO:0000269|PubMed:17330950,
FT                                ECO:0000269|PubMed:18407956,
FT                                ECO:0000269|PubMed:19779198}.
FT   MOD_RES     651    651       Phosphoserine.
FT                                {ECO:0000269|PubMed:17330950,
FT                                ECO:0000269|PubMed:18407956,
FT                                ECO:0000269|PubMed:19779198}.
FT   MOD_RES     664    664       Phosphoserine.
FT                                {ECO:0000269|PubMed:18407956}.
FT   MOD_RES     912    912       Phosphoserine.
FT                                {ECO:0000269|PubMed:17330950,
FT                                ECO:0000269|PubMed:18407956,
FT                                ECO:0000269|PubMed:19779198}.
FT   MOD_RES     913    913       Phosphoserine.
FT                                {ECO:0000269|PubMed:17330950,
FT                                ECO:0000269|PubMed:18407956,
FT                                ECO:0000269|PubMed:19779198}.
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
//
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