PHO80_YEAST
ID PHO80_YEAST Reviewed; 293 AA.
AC P20052; D6W266; Q06882; Q06883;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=PHO85 cyclin PHO80;
DE AltName: Full=Aminoglycoside antibiotic sensitivity protein 3;
DE AltName: Full=Phosphate system cyclin PHO80;
GN Name=PHO80; Synonyms=AGS3, TUP7, VAC5; OrderedLocusNames=YOL001W;
GN ORFNames=O2505, UNB293;
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], AND MUTAGENESIS OF LEU-163.
RX PubMed=3283704; DOI=10.1093/nar/16.6.2625;
RA Madden S.L., Creasy C.L., Srinivas V., Fawcett W., Bergman L.W.;
RT "Structure and expression of the PHO80 gene of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 16:2625-2637(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3333302; DOI=10.1002/yea.320020209;
RA Toh-e A., Shimauchi T.;
RT "Cloning and sequencing of the PHO80 gene and CEN15 of Saccharomyces
RT cerevisiae.";
RL Yeast 2:129-139(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 1-36.
RC STRAIN=S288c / GRF88;
RX PubMed=3302947; DOI=10.1093/nar/15.14.5893;
RA Gilliquet V., Legrain M., Hilger F.;
RT "Sequence of the region 5' to the negative regulatory gene PHO80 of
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 15:5893-5893(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-293, AND MUTAGENESIS OF GLY-229.
RX PubMed=2269431; DOI=10.1016/0378-1119(90)90251-l;
RA Gilliquet V., Legrain M., Berben G.H.F., Hilger F.;
RT "Negative regulatory elements of the Saccharomyces cerevisiae PHO system:
RT interaction between PHO80 and PHO85 proteins.";
RL Gene 96:181-188(1990).
RN [8]
RP INTERACTION WITH PHO4.
RX PubMed=8187772; DOI=10.1002/j.1460-2075.1994.tb06496.x;
RA Jayaraman P.-S., Hirst K., Goding C.R.;
RT "The activation domain of a basic helix-loop-helix protein is masked by
RT repressor interaction with domains distinct from that required for
RT transcription regulation.";
RL EMBO J. 13:2192-2199(1994).
RN [9]
RP FUNCTION, AND INTERACTION WITH PHO4 AND PHO81.
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 [10]
RP FUNCTION, INTERACTION WITH PHO85, AND PHOSPHORYLATION OF PHO4.
RX PubMed=8108735; DOI=10.1126/science.8108735;
RA Kaffman A., Herskowitz I., Tjian R., O'Shea E.K.;
RT "Phosphorylation of the transcription factor PHO4 by a cyclin-CDK complex,
RT PHO80-PHO85.";
RL Science 263:1153-1156(1994).
RN [11]
RP ACTIVITY REGULATION, AND INTERACTION WITH PHO81.
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 [12]
RP FUNCTION, AND PHOSPHORYLATION OF PHO4.
RX PubMed=8539622; DOI=10.1126/science.271.5246.209;
RA O'Neill E.M., Kaffman A., Jolly E.R., O'Shea E.K.;
RT "Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK
RT complex.";
RL Science 271:209-212(1996).
RN [13]
RP FUNCTION.
RX PubMed=9732266; DOI=10.1101/gad.12.17.2673;
RA Kaffman A., Rank N.M., O'Shea E.K.;
RT "Phosphorylation regulates association of the transcription factor Pho4
RT with its import receptor Pse1/Kap121.";
RL Genes Dev. 12:2673-2683(1998).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9853758; DOI=10.1038/24898;
RA Kaffman A., Rank N.M., O'Neill E.M., Huang L.S., O'Shea E.K.;
RT "The receptor Msn5 exports the phosphorylated transcription factor Pho4 out
RT of the nucleus.";
RL Nature 396:482-486(1998).
RN [15]
RP PHOSPHORYLATION AT SER-234 AND SER-267, AND PHOSPHORYLATION OF PHO4 AND
RP PHO81.
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 [16]
RP FUNCTION, AND PHOSPHORYLATION OF RIM15.
RX PubMed=16308562; DOI=10.1038/sj.emboj.7600889;
RA Wanke V., Pedruzzi I., Cameroni E., Dubouloz F., De Virgilio C.;
RT "Regulation of G0 entry by the Pho80-Pho85 cyclin-CDK complex.";
RL EMBO J. 24:4271-4278(2005).
RN [17]
RP PHOSPHORYLATION OF CRZ1.
RX PubMed=16455487; DOI=10.1016/j.molcel.2005.12.011;
RA Sopko R., Huang D., Preston N., Chua G., Papp B., Kafadar K., Snyder M.,
RA Oliver S.G., Cyert M., Hughes T.R., Boone C., Andrews B.J.;
RT "Mapping pathways and phenotypes by systematic gene overexpression.";
RL Mol. Cell 21:319-330(2006).
CC -!- FUNCTION: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85.
CC Negatively regulates the expression of phosphate-starvation-responsive
CC genes under phosphate-rich conditions. The PHO80-PHO85 cyclin-CDK
CC holoenzyme phosphorylates and inactivates the transcription factor
CC PHO4, by preventing its association with the transcription factor PHO2
CC and the nuclear import receptor PSE1, and by promoting association with
CC the nuclear export receptor MSN5, excluding PHO4 from the nucleus.
CC PHO80-PHO85 phosphorylates and inactivates protein kinase RIM15 by
CC retaining it in the cytoplasm, antagonizing RIM15-induced entry into
CC stationary phase. PHO80-PHO85 also phosphorylates and inactivates the
CC calcineurin-responsive transcription factor CRZ1, linking PHO85 to
CC calcium signaling. {ECO:0000269|PubMed:16308562,
CC ECO:0000269|PubMed:7957107, ECO:0000269|PubMed:8108735,
CC ECO:0000269|PubMed:8539622, ECO:0000269|PubMed:9732266,
CC ECO:0000269|PubMed:9853758}.
CC -!- ACTIVITY REGULATION: Inhibited by the CDK inhibitor (CKI) PHO81 in
CC response to phosphate starvation. {ECO:0000269|PubMed:7939631}.
CC -!- SUBUNIT: Forms a cyclin-CDK complex with PHO85. PHO80-PHO85 forms a
CC stable complex with its inhibitor PHO81 under both high- and low-
CC phosphate conditions, but PHO81 only inhibits the kinase upon phosphate
CC starvation. Interacts with transcription factor PHO4.
CC {ECO:0000269|PubMed:7939631, ECO:0000269|PubMed:7957107,
CC ECO:0000269|PubMed:8108735, ECO:0000269|PubMed:8187772}.
CC -!- INTERACTION:
CC P20052; P17157: PHO85; NbExp=4; IntAct=EBI-13310, EBI-13327;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9853758}. Nucleus
CC {ECO:0000269|PubMed:9853758}. Note=Localizes predominantly to the
CC cytoplasm under phosphate-rich conditions and concentrates in the
CC nucleus upon phosphate starvation.
CC -!- PTM: Phosphorylation of Ser-267 by PHO85 is required to form an active
CC cyclin-kinase complex and for function. {ECO:0000269|PubMed:15057567,
CC ECO:0000269|PubMed:16308562, ECO:0000269|PubMed:16455487,
CC ECO:0000269|PubMed:8108735, ECO:0000269|PubMed:8539622}.
CC -!- SIMILARITY: Belongs to the cyclin family. PHO80 subfamily.
CC {ECO:0000305}.
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DR EMBL; X07464; CAA30347.1; -; Genomic_DNA.
DR EMBL; U43491; AAC49479.1; -; Genomic_DNA.
DR EMBL; Z74743; CAA99000.1; -; Genomic_DNA.
DR EMBL; Y00382; CAA68454.1; -; Genomic_DNA.
DR EMBL; M60624; AAA34869.1; -; Genomic_DNA.
DR EMBL; M60625; AAA34870.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10782.1; -; Genomic_DNA.
DR PIR; S61983; S61983.
DR RefSeq; NP_014642.1; NM_001183255.1.
DR PDB; 2PK9; X-ray; 2.91 A; B/D=1-293.
DR PDB; 2PMI; X-ray; 2.90 A; B/D=1-293.
DR PDBsum; 2PK9; -.
DR PDBsum; 2PMI; -.
DR AlphaFoldDB; P20052; -.
DR SMR; P20052; -.
DR BioGRID; 34403; 554.
DR ComplexPortal; CPX-1688; PHO80-PHO85 kinase complex.
DR DIP; DIP-2479N; -.
DR IntAct; P20052; 8.
DR MINT; P20052; -.
DR STRING; 4932.YOL001W; -.
DR BindingDB; P20052; -.
DR ChEMBL; CHEMBL2111355; -.
DR ChEMBL; CHEMBL2111410; -.
DR iPTMnet; P20052; -.
DR MaxQB; P20052; -.
DR PaxDb; P20052; -.
DR PRIDE; P20052; -.
DR EnsemblFungi; YOL001W_mRNA; YOL001W; YOL001W.
DR GeneID; 854161; -.
DR KEGG; sce:YOL001W; -.
DR SGD; S000005361; PHO80.
DR VEuPathDB; FungiDB:YOL001W; -.
DR eggNOG; KOG1674; Eukaryota.
DR GeneTree; ENSGT00390000000862; -.
DR HOGENOM; CLU_061246_1_0_1; -.
DR InParanoid; P20052; -.
DR OMA; HINDSMP; -.
DR BioCyc; YEAST:G3O-33418-MON; -.
DR EvolutionaryTrace; P20052; -.
DR PRO; PR:P20052; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P20052; protein.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990860; C:Pho85-Pho80 CDK-cyclin complex; IDA:SGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0006875; P:cellular metal ion homeostasis; IMP:SGD.
DR GO; GO:0050849; P:negative regulation of calcium-mediated signaling; IGI:SGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:ComplexPortal.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:SGD.
DR GO; GO:0045936; P:negative regulation of phosphate metabolic process; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR PANTHER; PTHR15615; PTHR15615; 1.
DR Pfam; PF08613; Cyclin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cyclin; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..293
FT /note="PHO85 cyclin PHO80"
FT /id="PRO_0000080502"
FT REGION 254..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="Phosphoserine; by PHO85"
FT /evidence="ECO:0000269|PubMed:15057567"
FT MOD_RES 267
FT /note="Phosphoserine; by PHO85"
FT /evidence="ECO:0000269|PubMed:15057567"
FT MUTAGEN 163
FT /note="L->S: Temperature-sensitive allele."
FT /evidence="ECO:0000269|PubMed:3283704"
FT MUTAGEN 229
FT /note="G->D: In PHO80-1."
FT /evidence="ECO:0000269|PubMed:2269431"
FT CONFLICT 65
FT /note="T -> S (in Ref. 1; CAA30347)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="P -> S (in Ref. 7; AAA34869/AAA34870)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="E -> K (in Ref. 7; AAA34869/AAA34870)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="P -> A (in Ref. 1; CAA30347 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:2PK9"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2PMI"
FT HELIX 32..51
FT /evidence="ECO:0007829|PDB:2PMI"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:2PMI"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2PMI"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:2PMI"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2PK9"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:2PMI"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:2PMI"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:2PMI"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:2PMI"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:2PMI"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2PMI"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:2PMI"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2PMI"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2PK9"
SQ SEQUENCE 293 AA; 33227 MW; 72918CAF845AE74C CRC64;
MESTSGERSE NIHEDQGIPK VILPADFNKC SRTDLVVLIS RMLVSLIAIN ENSATKKSDD
QITLTRYHSK IPPNISIFNY FIRLTKFSSL EHCVLMTSLY YIDLLQTVYP DFTLNSLTAH
RFLLTATTVA TKGLCDSFST NAHYAKVGGV RCHELNILEN DFLKRVNYRI IPRDHNITLC
SIEQKQKKFV IDKNALGSLD LDSYSYVNRP KSGYNVLDKY YRRIVQLVGS FNASPDKSRK
VDYVLPPNID IVSESGSQTT QLKGSSSPNS HSSQKRYSEA KDAHIYNKRS KPD
