PHO81_YEAST
ID PHO81_YEAST Reviewed; 1178 AA.
AC P17442; D6VV13; Q06887;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Phosphate system positive regulatory protein PHO81;
DE AltName: Full=CDK inhibitor PHO81;
GN Name=PHO81; OrderedLocusNames=YGR233C; ORFNames=G8567;
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=S288c / GRF88;
RX PubMed=2186378; DOI=10.1093/nar/18.8.2176;
RA Coche T., Prozzi D., Legrain M., Hilger F., Vandenhaute J.;
RT "Nucleotide sequence of the PHO81 gene involved in the regulation of the
RT repressible acid phosphatase gene in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 18:2176-2176(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8492812; DOI=10.1007/bf00292004;
RA Ogawa N., Noguchi K., Yamashita Y., Yasuhara T., Hayashi N., Yoshida K.,
RA Oshima Y.;
RT "Promoter analysis of the PHO81 gene encoding a 134 kDa protein bearing
RT ankyrin repeats in the phosphatase regulon of Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 238:444-454(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8701610;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 12:385-390(1996).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10, AND CHARACTERIZATION.
RX PubMed=8493108; DOI=10.1093/nar/21.8.1975;
RA Creasy C.L., Madden S.L., Bergman L.W.;
RT "Molecular analysis of the PHO81 gene of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 21:1975-1982(1993).
RN [7]
RP FUNCTION, AND INTERACTION WITH PHO4 AND PHO80.
RX PubMed=7957107; DOI=10.1002/j.1460-2075.1994.tb06876.x;
RA Hirst K., Fisher F., McAndrew P.C., Goding C.R.;
RT "The transcription factor, the Cdk, its cyclin and their regulator:
RT directing the transcriptional response to a nutritional signal.";
RL EMBO J. 13:5410-5420(1994).
RN [8]
RP FUNCTION, AND INTERACTION WITH PHO80.
RX PubMed=7939631; DOI=10.1126/science.7939631;
RA Schneider K.R., Smith R.L., O'Shea E.K.;
RT "Phosphate-regulated inactivation of the kinase PHO80-PHO85 by the CDK
RT inhibitor PHO81.";
RL Science 266:122-126(1994).
RN [9]
RP FUNCTION, AND INTERACTION WITH PCL7.
RX PubMed=11069666; DOI=10.1046/j.1365-2958.2000.02140.x;
RA Lee M., O'Regan S., Moreau J.-L., Johnson A.L., Johnston L.H., Goding C.R.;
RT "Regulation of the Pcl7-Pho85 cyclin-cdk complex by Pho81.";
RL Mol. Microbiol. 38:411-422(2000).
RN [10]
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 [11]
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 [12]
RP PHOSPHORYLATION.
RX PubMed=15057567; DOI=10.1007/s00294-004-0501-0;
RA Waters N.C., Knight J.P., Creasy C.L., Bergman L.W.;
RT "The yeast Pho80-Pho85 cyclin-CDK complex has multiple substrates.";
RL Curr. Genet. 46:1-9(2004).
RN [13]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=15127225; DOI=10.1007/s00294-004-0502-z;
RA Knight J.P., Daly T.M., Bergman L.W.;
RT "Regulation by phosphorylation of Pho81p, a cyclin-dependent kinase
RT inhibitor in Saccharomyces cerevisiae.";
RL Curr. Genet. 46:10-19(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-956, 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 [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Inhibits the kinase activity of the cyclin-CDKs PHO80-PHO85
CC and PCL7-PHO85 under low-phosphate conditions.
CC {ECO:0000269|PubMed:11069666, ECO:0000269|PubMed:7939631,
CC ECO:0000269|PubMed:7957107}.
CC -!- SUBUNIT: Associates specifically with the PHO80-PHO85 and PCL7-PHO85
CC cyclin-CDK complexes, and much of this interaction is mediated through
CC the PHO80 and PCL7 cyclin subunits. Interacts with the transcription
CC factor PHO4. {ECO:0000269|PubMed:11069666, ECO:0000269|PubMed:7939631,
CC ECO:0000269|PubMed:7957107}.
CC -!- INTERACTION:
CC P17442; P17157: PHO85; NbExp=6; IntAct=EBI-13314, EBI-13327;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes predominantly
CC to the nucleus in both high- and low-phosphate conditions.
CC -!- PTM: Phosphorylated by the cyclin-CDK PHO80-PHO85. Phosphorylation
CC mediates the formation of a stable interaction with the cyclin-CDK and
CC is required for function as an active inhibitor of the complex under
CC phosphate starvation conditions. {ECO:0000269|PubMed:15057567,
CC ECO:0000269|PubMed:15127225}.
CC -!- MISCELLANEOUS: Present with 2930 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X52482; CAA36726.1; -; Genomic_DNA.
DR EMBL; D13228; BAA02508.1; -; Genomic_DNA.
DR EMBL; X87941; CAA61183.1; -; Genomic_DNA.
DR EMBL; Z73018; CAA97261.1; -; Genomic_DNA.
DR EMBL; S61041; AAD13922.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08324.1; -; Genomic_DNA.
DR PIR; S57698; S57698.
DR RefSeq; NP_011749.3; NM_001181362.3.
DR AlphaFoldDB; P17442; -.
DR SMR; P17442; -.
DR BioGRID; 33485; 70.
DR DIP; DIP-5959N; -.
DR IntAct; P17442; 18.
DR MINT; P17442; -.
DR STRING; 4932.YGR233C; -.
DR BindingDB; P17442; -.
DR ChEMBL; CHEMBL1250353; -.
DR iPTMnet; P17442; -.
DR MaxQB; P17442; -.
DR PaxDb; P17442; -.
DR PRIDE; P17442; -.
DR EnsemblFungi; YGR233C_mRNA; YGR233C; YGR233C.
DR GeneID; 853148; -.
DR KEGG; sce:YGR233C; -.
DR SGD; S000003465; PHO81.
DR VEuPathDB; FungiDB:YGR233C; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1161; Eukaryota.
DR eggNOG; KOG2421; Eukaryota.
DR HOGENOM; CLU_002842_1_0_1; -.
DR InParanoid; P17442; -.
DR OMA; PLRKYGH; -.
DR BioCyc; YEAST:G3O-30911-MON; -.
DR PRO; PR:P17442; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P17442; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IMP:SGD.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IMP:SGD.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR004331; SPX_dom.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF03105; SPX; 2.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS51382; SPX; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1178
FT /note="Phosphate system positive regulatory protein PHO81"
FT /id="PRO_0000067075"
FT DOMAIN 1..169
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT REPEAT 423..452
FT /note="ANK 1"
FT REPEAT 458..487
FT /note="ANK 2"
FT REPEAT 506..535
FT /note="ANK 3"
FT REPEAT 556..586
FT /note="ANK 4"
FT REPEAT 591..620
FT /note="ANK 5"
FT REPEAT 624..653
FT /note="ANK 6"
FT DOMAIN 871..1178
FT /note="GP-PDE"
FT REGION 210..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 956
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 248
FT /note="N -> NN (in Ref. 2; BAA02508)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="T -> I (in Ref. 2; BAA02508)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="S -> F (in Ref. 2; BAA02508)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="D -> H (in Ref. 2; BAA02508)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="N -> K (in Ref. 2; BAA02508)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="Missing (in Ref. 1; CAA36726)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="A -> V (in Ref. 2; BAA02508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1178 AA; 134029 MW; 9314EDB94B3F6B7D CRC64;
MKFGKYLEAR QLELAEYNSH FIDYKALKKL IKQLAIPTLK ASSDLDLHLT LDDIDEKIIH
QRLQENKAAF FFKLERELEK VNGYYLARES DLRIKFNILH SKYKDYKING KLNSNQATSF
KNLYAAFKKF QKDLRNLEQY VELNKTGFSK ALKKWDKRSQ SHDKDFYLAT VVSIQPIFTR
DGPLKLNDET LHILLELNDI DNNNRRADIQ SSTFTNDDDD DNNTSNNNKH NNNNNNNNNN
NNNNNNNNIL HNNYELTTSK ISENQLEHLF QASSSSLDME MEIENWYKEI LNIATVKDVQ
RKHALLRNFR ETKIFTYLLQ NSSESFHKNV FSLLKECLTT LFLLLVASPL DDNSLHIFYK
SNQDHIDLSY CDEDDQVFSR KNVFHEAASC PEKSRLFILD EALTTSKLSK ETVQKLLNAQ
DIHSRVPLHY AAELGKLEFV HSLLITNLLE DVDPIDSDSK TPLVLAITNN HIDVVRDLLT
IGGANASPIE KPILDYSKNV ISSTKVQFDP LNVACKFNNH DAAKLLLEIR SKQNADNAKN
KSSQHLCQPL FKKNSTGLCT LHIVAKIGGD PQLIQLLIRY GADPNEIDGF NKWTPIFYAV
RSGHSEVITE LLKHNARLDI EDDNGHSPLF YALWESHVDV LNALLQRPLN LPSAPLNEIN
SQSSTQRLNT IDLTPNDDKF DLDIQDSIPD FALPPPIIPL RKYGHNFLEK KIFIKLKLRP
GLESIKLTQD NGIIMSSSPG RITLSSNLPE IIPRNVILPV RSGEINNFCK DISETNDEED
DDEISEDHDD GEIIFQVDSI DDFSMDFEIF PSFGTRIIAK TTAMPFLFKK VAINSIATMN
LPLFDTRLNN IGSLTLDYQI IFPYPGNPLK IINYEPYWKS TGSDLMTSSK DGNFVTSSSL
NGSFISVLVC ALNDETIVAA PKPYVEFKGT KILLNDLTKE QLEKVVDYDF GKIDGSFDEV
TLKQYLSSRV VPLRSLLEVI PGSAQLVIRV YFPTDKEIDT IPIKISPFIN INQFIDKLLL
IIFEHERFLR HSGSGSMRQI VFSSCNWEAC SILNWKQPNF PVLLQMKNLL RDSTTGKFVG
DTPNCLKELA VNPQKMSYLN TELINIHTMV QFAMNNNLLG VTLPYEVLKI CPSLARIIKQ
NGLLLIASVG ENDQIPADGG YSGIYYACEL LFENNIDM
