PWP1_YEAST
ID PWP1_YEAST Reviewed; 576 AA.
AC P21304; D6VYJ9;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Periodic tryptophan protein 1;
GN Name=PWP1; OrderedLocusNames=YLR196W; ORFNames=L8167.10;
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 204511 / S288c / AB972;
RX PubMed=1594577; DOI=10.1002/prot.340130105;
RA Duronio R.J., Gordon J.I., Boguski M.S.;
RT "Comparative analysis of the beta transducin family with identification of
RT several new members including PWP1, a nonessential gene of Saccharomyces
RT cerevisiae that is divergently transcribed from NMT1.";
RL Proteins 13:41-56(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-131, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-131, 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).
CC -!- INTERACTION:
CC P21304; Q08235: BRX1; NbExp=3; IntAct=EBI-14328, EBI-3775;
CC -!- MISCELLANEOUS: Present with 43800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat PWP1 family. {ECO:0000305}.
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DR EMBL; M37578; AAA34926.1; -; Genomic_DNA.
DR EMBL; U14913; AAB67432.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09515.1; -; Genomic_DNA.
DR PIR; S29367; S29367.
DR RefSeq; NP_013297.1; NM_001182083.1.
DR AlphaFoldDB; P21304; -.
DR SMR; P21304; -.
DR BioGRID; 31466; 297.
DR DIP; DIP-4203N; -.
DR IntAct; P21304; 86.
DR MINT; P21304; -.
DR STRING; 4932.YLR196W; -.
DR iPTMnet; P21304; -.
DR MaxQB; P21304; -.
DR PaxDb; P21304; -.
DR PRIDE; P21304; -.
DR EnsemblFungi; YLR196W_mRNA; YLR196W; YLR196W.
DR GeneID; 850893; -.
DR KEGG; sce:YLR196W; -.
DR SGD; S000004186; PWP1.
DR VEuPathDB; FungiDB:YLR196W; -.
DR eggNOG; KOG0270; Eukaryota.
DR GeneTree; ENSGT00390000017324; -.
DR HOGENOM; CLU_023867_0_1_1; -.
DR InParanoid; P21304; -.
DR OMA; CFVPRGV; -.
DR BioCyc; YEAST:G3O-32317-MON; -.
DR PRO; PR:P21304; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P21304; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR044285; PWP1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR14091; PTHR14091; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..576
FT /note="Periodic tryptophan protein 1"
FT /id="PRO_0000051173"
FT REPEAT 207..252
FT /note="WD 1"
FT REPEAT 284..324
FT /note="WD 2"
FT REPEAT 329..369
FT /note="WD 3"
FT REPEAT 376..414
FT /note="WD 4"
FT REPEAT 420..461
FT /note="WD 5"
FT REPEAT 472..514
FT /note="WD 6"
FT REGION 41..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..92
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..576
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 576 AA; 63803 MW; FC0189B289494AB5 CRC64;
MISATNWVPR GFSSEFPEKY VLDDEEVERI NQLAQLNLDD AKATLEEAEG ESGVEDDAAT
GSSNKLKDQL DIDDDLKEYN LEEYDDEEIA DNEGGKDVSM FPGLSNDSDV KFHEGEKGED
PYISLPNQED SQEEKQELQV YPSDNLVLAA RTEDDVSYLD IYVYDDGAGF HSSDIPVEEG
DEADPDVARG LVRDPALYVH HDLMLPAFPL CVEWLDYKVG SNSEEAANYA AIGTFDPQIE
IWNLDCVDKA FPDMILGEPL DNSMVSLKSK KKKKKSKTGH ITTHHTDAVL SMAHNKYFRS
VLASTSADHT VKLWDLNSGN AARSLASIHS NKNVSSSEWH MLNGSILLTG GYDSRVALTD
VRISDESQMS KYWSAMAGEE IETVTFASEN IILCGTDSGN VYSFDIRNNE NRKPVWTLKA
HDAGISTLCS NKFIPGMMST GAMGEKTVKL WKFPLDDATN TKGPSMVLSR DFDVGNVLTS
SFAPDIEVAG TMVIGGVNKV LKLWDVFTNR SVRKSFKSEL ENVQARAKEE AQKIGKSSRI
ARKYTSNDNP DTVITIDDQG EDEEEREGGD EHDDMA
