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Protein

Phosphate system positive regulatory protein PHO81

Gene

PHO81

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits the kinase activity of the cyclin-CDKs PHO80-PHO85 and PCL7-PHO85 under low-phosphate conditions.3 Publications

GO - Molecular functioni

  • cyclin-dependent protein serine/threonine kinase inhibitor activity Source: SGD
  • phosphoric diester hydrolase activity Source: InterPro

GO - Biological processi

  • lipid metabolic process Source: InterPro
  • phosphate-containing compound metabolic process Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-30911-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphate system positive regulatory protein PHO81
Alternative name(s):
CDK inhibitor PHO81
Gene namesi
Name:PHO81
Ordered Locus Names:YGR233C
ORF Names:G8567
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR233C.
SGDiS000003465. PHO81.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Localizes predominantly to the nucleus in both high- and low-phosphate conditions.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2111410.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11781178Phosphate system positive regulatory protein PHO81PRO_0000067075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei956 – 9561PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by the cyclin-CDK PHO80-PHO85. Phosphorylation mediates the formation of a stable interaction with the cyclin-CDK and is required for function as an active inhibitor of the complex under phosphate starvation conditions.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP17442.

PTM databases

iPTMnetiP17442.

Interactioni

Subunit structurei

Associates specifically with the PHO80-PHO85 and PCL7-PHO85 cyclin-CDK complexes, and much of this interaction is mediated through the PHO80 and PCL7 cyclin subunits. Interacts with the transcription factor PHO4.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PHO85P171575EBI-13314,EBI-13327

Protein-protein interaction databases

BioGridi33485. 39 interactions.
DIPiDIP-5959N.
IntActiP17442. 14 interactions.
MINTiMINT-667561.

Chemistry

BindingDBiP17442.

Structurei

3D structure databases

ProteinModelPortaliP17442.
SMRiP17442. Positions 413-711.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 169169SPXPROSITE-ProRule annotationAdd
BLAST
Repeati423 – 45230ANK 1Add
BLAST
Repeati458 – 48730ANK 2Add
BLAST
Repeati506 – 53530ANK 3Add
BLAST
Repeati556 – 58631ANK 4Add
BLAST
Repeati591 – 62030ANK 5Add
BLAST
Repeati624 – 65330ANK 6Add
BLAST
Domaini871 – 1178308GP-PDEAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi198 – 25356Asn/Asp-richAdd
BLAST
Compositional biasi231 – 24818Poly-AsnAdd
BLAST

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation
Contains 1 GP-PDE domain.Curated
Contains 1 SPX domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

HOGENOMiHOG000187674.
InParanoidiP17442.
KOiK06653.
OMAiERNCLHQ.
OrthoDBiEOG7JDR7K.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR030395. GP_PDE_dom.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR004331. SPX_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF03105. SPX. 2 hits.
[Graphical view]
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS51704. GP_PDE. 1 hit.
PS51382. SPX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFGKYLEAR QLELAEYNSH FIDYKALKKL IKQLAIPTLK ASSDLDLHLT
60 70 80 90 100
LDDIDEKIIH QRLQENKAAF FFKLERELEK VNGYYLARES DLRIKFNILH
110 120 130 140 150
SKYKDYKING KLNSNQATSF KNLYAAFKKF QKDLRNLEQY VELNKTGFSK
160 170 180 190 200
ALKKWDKRSQ SHDKDFYLAT VVSIQPIFTR DGPLKLNDET LHILLELNDI
210 220 230 240 250
DNNNRRADIQ SSTFTNDDDD DNNTSNNNKH NNNNNNNNNN NNNNNNNNIL
260 270 280 290 300
HNNYELTTSK ISENQLEHLF QASSSSLDME MEIENWYKEI LNIATVKDVQ
310 320 330 340 350
RKHALLRNFR ETKIFTYLLQ NSSESFHKNV FSLLKECLTT LFLLLVASPL
360 370 380 390 400
DDNSLHIFYK SNQDHIDLSY CDEDDQVFSR KNVFHEAASC PEKSRLFILD
410 420 430 440 450
EALTTSKLSK ETVQKLLNAQ DIHSRVPLHY AAELGKLEFV HSLLITNLLE
460 470 480 490 500
DVDPIDSDSK TPLVLAITNN HIDVVRDLLT IGGANASPIE KPILDYSKNV
510 520 530 540 550
ISSTKVQFDP LNVACKFNNH DAAKLLLEIR SKQNADNAKN KSSQHLCQPL
560 570 580 590 600
FKKNSTGLCT LHIVAKIGGD PQLIQLLIRY GADPNEIDGF NKWTPIFYAV
610 620 630 640 650
RSGHSEVITE LLKHNARLDI EDDNGHSPLF YALWESHVDV LNALLQRPLN
660 670 680 690 700
LPSAPLNEIN SQSSTQRLNT IDLTPNDDKF DLDIQDSIPD FALPPPIIPL
710 720 730 740 750
RKYGHNFLEK KIFIKLKLRP GLESIKLTQD NGIIMSSSPG RITLSSNLPE
760 770 780 790 800
IIPRNVILPV RSGEINNFCK DISETNDEED DDEISEDHDD GEIIFQVDSI
810 820 830 840 850
DDFSMDFEIF PSFGTRIIAK TTAMPFLFKK VAINSIATMN LPLFDTRLNN
860 870 880 890 900
IGSLTLDYQI IFPYPGNPLK IINYEPYWKS TGSDLMTSSK DGNFVTSSSL
910 920 930 940 950
NGSFISVLVC ALNDETIVAA PKPYVEFKGT KILLNDLTKE QLEKVVDYDF
960 970 980 990 1000
GKIDGSFDEV TLKQYLSSRV VPLRSLLEVI PGSAQLVIRV YFPTDKEIDT
1010 1020 1030 1040 1050
IPIKISPFIN INQFIDKLLL IIFEHERFLR HSGSGSMRQI VFSSCNWEAC
1060 1070 1080 1090 1100
SILNWKQPNF PVLLQMKNLL RDSTTGKFVG DTPNCLKELA VNPQKMSYLN
1110 1120 1130 1140 1150
TELINIHTMV QFAMNNNLLG VTLPYEVLKI CPSLARIIKQ NGLLLIASVG
1160 1170
ENDQIPADGG YSGIYYACEL LFENNIDM
Length:1,178
Mass (Da):134,029
Last modified:October 1, 1996 - v2
Checksum:i9314EDB94B3F6B7D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481N → NN in BAA02508 (PubMed:8492812).Curated
Sequence conflicti728 – 7281T → I in BAA02508 (PubMed:8492812).Curated
Sequence conflicti762 – 7621S → F in BAA02508 (PubMed:8492812).Curated
Sequence conflicti845 – 8451D → H in BAA02508 (PubMed:8492812).Curated
Sequence conflicti873 – 8731N → K in BAA02508 (PubMed:8492812).Curated
Sequence conflicti920 – 9201Missing in CAA36726 (PubMed:2186378).Curated
Sequence conflicti984 – 9841A → V in BAA02508 (PubMed:8492812).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52482 Genomic DNA. Translation: CAA36726.1.
D13228 Genomic DNA. Translation: BAA02508.1.
X87941 Genomic DNA. Translation: CAA61183.1.
Z73018 Genomic DNA. Translation: CAA97261.1.
S61041 Genomic DNA. Translation: AAD13922.1.
BK006941 Genomic DNA. Translation: DAA08324.1.
PIRiS57698.
RefSeqiNP_011749.3. NM_001181362.3.

Genome annotation databases

EnsemblFungiiYGR233C; YGR233C; YGR233C.
GeneIDi853148.
KEGGisce:YGR233C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52482 Genomic DNA. Translation: CAA36726.1.
D13228 Genomic DNA. Translation: BAA02508.1.
X87941 Genomic DNA. Translation: CAA61183.1.
Z73018 Genomic DNA. Translation: CAA97261.1.
S61041 Genomic DNA. Translation: AAD13922.1.
BK006941 Genomic DNA. Translation: DAA08324.1.
PIRiS57698.
RefSeqiNP_011749.3. NM_001181362.3.

3D structure databases

ProteinModelPortaliP17442.
SMRiP17442. Positions 413-711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33485. 39 interactions.
DIPiDIP-5959N.
IntActiP17442. 14 interactions.
MINTiMINT-667561.

Chemistry

BindingDBiP17442.
ChEMBLiCHEMBL2111410.

PTM databases

iPTMnetiP17442.

Proteomic databases

MaxQBiP17442.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR233C; YGR233C; YGR233C.
GeneIDi853148.
KEGGisce:YGR233C.

Organism-specific databases

EuPathDBiFungiDB:YGR233C.
SGDiS000003465. PHO81.

Phylogenomic databases

HOGENOMiHOG000187674.
InParanoidiP17442.
KOiK06653.
OMAiERNCLHQ.
OrthoDBiEOG7JDR7K.

Enzyme and pathway databases

BioCyciYEAST:G3O-30911-MONOMER.

Miscellaneous databases

PROiP17442.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR030395. GP_PDE_dom.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR004331. SPX_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF03105. SPX. 2 hits.
[Graphical view]
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS51704. GP_PDE. 1 hit.
PS51382. SPX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the PHO81 gene involved in the regulation of the repressible acid phosphatase gene in Saccharomyces cerevisiae."
    Coche T., Prozzi D., Legrain M., Hilger F., Vandenhaute J.
    Nucleic Acids Res. 18:2176-2176(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / GRF88.
  2. "Promoter analysis of the PHO81 gene encoding a 134 kDa protein bearing ankyrin repeats in the phosphatase regulon of Saccharomyces cerevisiae."
    Ogawa N., Noguchi K., Yamashita Y., Yasuhara T., Hayashi N., Yoshida K., Oshima Y.
    Mol. Gen. Genet. 238:444-454(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the right arm of Saccharomyces cerevisiae chromosome VII."
    van der Aart Q.J.M., Kleine K., Steensma H.Y.
    Yeast 12:385-390(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Molecular analysis of the PHO81 gene of Saccharomyces cerevisiae."
    Creasy C.L., Madden S.L., Bergman L.W.
    Nucleic Acids Res. 21:1975-1982(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10, CHARACTERIZATION.
  7. "The transcription factor, the Cdk, its cyclin and their regulator: directing the transcriptional response to a nutritional signal."
    Hirst K., Fisher F., McAndrew P.C., Goding C.R.
    EMBO J. 13:5410-5420(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHO4 AND PHO80.
  8. "Phosphate-regulated inactivation of the kinase PHO80-PHO85 by the CDK inhibitor PHO81."
    Schneider K.R., Smith R.L., O'Shea E.K.
    Science 266:122-126(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHO80.
  9. Cited for: FUNCTION, INTERACTION WITH PCL7.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "The yeast Pho80-Pho85 cyclin-CDK complex has multiple substrates."
    Waters N.C., Knight J.P., Creasy C.L., Bergman L.W.
    Curr. Genet. 46:1-9(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  13. "Regulation by phosphorylation of Pho81p, a cyclin-dependent kinase inhibitor in Saccharomyces cerevisiae."
    Knight J.P., Daly T.M., Bergman L.W.
    Curr. Genet. 46:10-19(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
  14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPHO81_YEAST
AccessioniPrimary (citable) accession number: P17442
Secondary accession number(s): D6VV13, Q06887
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2930 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.