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P07270

- PHO4_YEAST

UniProt

P07270 - PHO4_YEAST

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Protein

Phosphate system positive regulatory protein PHO4

Gene

PHO4

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

Functioni

Transcriptional activator that regulates the expression of repressible phosphatase under phosphate starvation conditions. Binds to the upstream activating sequence (UAS) of several phosphatase encoding PHO genes. Inhibited by the cyclin-CDK PHO80-PHO85 under high-phosphate conditions.

GO - Molecular functioni

  1. sequence-specific DNA binding Source: SGD
  2. sequence-specific DNA binding transcription factor activity Source: SGD

GO - Biological processi

  1. cellular response to phosphate starvation Source: SGD
  2. chromatin remodeling Source: SGD
  3. positive regulation of phosphate metabolic process Source: SGD
  4. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30481-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphate system positive regulatory protein PHO4
Gene namesi
Name:PHO4
Ordered Locus Names:YFR034C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VI

Organism-specific databases

CYGDiYFR034c.
SGDiS000001930. PHO4.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 PublicationPROSITE-ProRule annotation
Note: Predominantly cytoplasmic under high-phosphate conditions and localized to the nucleus upon phosphate starvation.

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Phosphate system positive regulatory protein PHO4PRO_0000127422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001Phosphoserine; by PHO852 Publications
Modified residuei114 – 1141Phosphoserine; by PHO852 Publications
Modified residuei128 – 1281Phosphoserine; by PHO852 Publications
Modified residuei152 – 1521Phosphoserine; by PHO852 Publications
Modified residuei204 – 2041Phosphoserine1 Publication
Modified residuei223 – 2231Phosphoserine; by PHO854 Publications
Modified residuei242 – 2421Phosphoserine1 Publication
Modified residuei243 – 2431Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by the cyclin-CDK PHO80-PHO85 at five residues under high-phosphate conditions, preventing PHO4 from activating the structural PHO genes. Phosphorylation of Ser-114 and Ser-128 promotes nuclear export. Phosphorylation of Ser-152 decreases nuclear import. Phosphorylation of Ser-223 decreases the binding affinity for PHO2.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07270.
PaxDbiP07270.
PRIDEiP07270.

Expressioni

Gene expression databases

GenevestigatoriP07270.

Interactioni

Subunit structurei

Binds DNA as a homodimer. Interacts with transcription factor PHO2 and binds cooperatively to PHO5 UAS. Interacts with the cyclin-CDK PHO80-PHO85 and the CDK inhibitor (CKI) PHO81.2 Publications

Protein-protein interaction databases

BioGridi31191. 191 interactions.
DIPiDIP-911N.
IntActiP07270. 112 interactions.
MINTiMINT-2779852.

Structurei

Secondary structure

1
312
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi254 – 2585
Helixi260 – 27516
Helixi279 – 2824
Helixi294 – 30613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0AX-ray2.80A/B251-312[»]
3W3XX-ray2.90B140-166[»]
ProteinModelPortaliP07270.
SMRiP07270. Positions 251-312.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07270.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini250 – 30657bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3131Interaction with PHO80Add
BLAST
Regioni75 – 9925Transcription activation domainAdd
BLAST
Regioni156 – 20045Interaction with PHO80Add
BLAST
Regioni201 – 21818Interaction with PHO2Add
BLAST
Regioni203 – 22725Involved in oligomerizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi75 – 8399aaTAD
Motifi140 – 16627Nuclear localization signalAdd
BLAST

Domaini

the 9aaTAD motif (residues 75 to 83) is a transactivation domain present in a large number of yeast and animal transcription factors.2 Publications

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG39146.
InParanoidiP07270.
KOiK06658.
OrthoDBiEOG7W6X0F.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07270-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRTTSEGIH GFVDDLEPKS SILDKVGDFI TVNTKRHDGR EDFNEQNDEL
60 70 80 90 100
NSQENHNSSE NGNENENEQD SLALDDLDRA FELVEGMDMD WMMPSHAHHS
110 120 130 140 150
PATTATIKPR LLYSPLIHTQ SAVPVTISPN LVATATSTTS ANKVTKNKSN
160 170 180 190 200
SSPYLNKRRG KPGPDSATSL FELPDSVIPT PKPKPKPKQY PKVILPSNST
210 220 230 240 250
RRVSPVTAKT SSSAEGVVVA SESPVIAPHG SSHSRSLSKR RSSGALVDDD
260 270 280 290 300
KRESHKHAEQ ARRNRLAVAL HELASLIPAE WKQQNVSAAP SKATTVEAAC
310
RYIRHLQQNV ST
Length:312
Mass (Da):34,089
Last modified:January 9, 2007 - v4
Checksum:i6DB93C0DDDB4D741
GO

Sequence cautioni

The sequence CAA27345.1 differs from that shown. Reason: Frameshift at position 290.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691A → P in CAA27345. (PubMed:3008105)Curated
Sequence conflicti269 – 2691A → P(PubMed:2505053)Curated
Sequence conflicti310 – 3101V → G(PubMed:2505053)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03719 Genomic DNA. Translation: CAA27345.1. Frameshift.
D50617 Genomic DNA. Translation: BAA09273.1.
AY692776 Genomic DNA. Translation: AAT92795.1.
BK006940 Genomic DNA. Translation: DAA12477.1.
PIRiS56289.
RefSeqiNP_116692.1. NM_001179999.1.

Genome annotation databases

EnsemblFungiiYFR034C; YFR034C; YFR034C.
GeneIDi850594.
KEGGisce:YFR034C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03719 Genomic DNA. Translation: CAA27345.1 . Frameshift.
D50617 Genomic DNA. Translation: BAA09273.1 .
AY692776 Genomic DNA. Translation: AAT92795.1 .
BK006940 Genomic DNA. Translation: DAA12477.1 .
PIRi S56289.
RefSeqi NP_116692.1. NM_001179999.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A0A X-ray 2.80 A/B 251-312 [» ]
3W3X X-ray 2.90 B 140-166 [» ]
ProteinModelPortali P07270.
SMRi P07270. Positions 251-312.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31191. 191 interactions.
DIPi DIP-911N.
IntActi P07270. 112 interactions.
MINTi MINT-2779852.

Proteomic databases

MaxQBi P07270.
PaxDbi P07270.
PRIDEi P07270.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YFR034C ; YFR034C ; YFR034C .
GeneIDi 850594.
KEGGi sce:YFR034C.

Organism-specific databases

CYGDi YFR034c.
SGDi S000001930. PHO4.

Phylogenomic databases

eggNOGi NOG39146.
InParanoidi P07270.
KOi K06658.
OrthoDBi EOG7W6X0F.

Enzyme and pathway databases

BioCyci YEAST:G3O-30481-MONOMER.

Miscellaneous databases

EvolutionaryTracei P07270.
NextBioi 966449.

Gene expression databases

Genevestigatori P07270.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR011598. bHLH_dom.
[Graphical view ]
Pfami PF00010. HLH. 1 hit.
[Graphical view ]
SMARTi SM00353. HLH. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, physical characterization and expression analysis of the Saccharomyces cerevisiae positive regulatory gene PHO4."
    Legrain M., de Wilde M., Hilger F.
    Nucleic Acids Res. 14:3059-3073(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Mode of expression of the positive regulatory genes PHO2 and PHO4 of the phosphatase regulon in Saccharomyces cerevisiae."
    Yoshida K., Kuromitsu Z., Ogawa N., Oshima Y.
    Mol. Gen. Genet. 217:31-39(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Fifteen open reading frames in a 30.8 kb region of the right arm of chromosome VI from Saccharomyces cerevisiae."
    Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H., Hanaoka F., Murakami Y.
    Yeast 12:177-190(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. "Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae."
    Ogawa N., Oshima Y.
    Mol. Cell. Biol. 10:2224-2236(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  8. "The yeast regulatory gene PHO4 encodes a helix-loop-helix motif."
    Berben G.H.F., Legrain M., Gilliquet V., Hilger F.
    Yeast 6:451-454(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: HELIX-LOOP-HELIX MOTIF.
  9. "The activation domain of a basic helix-loop-helix protein is masked by repressor interaction with domains distinct from that required for transcription regulation."
    Jayaraman P.-S., Hirst K., Goding C.R.
    EMBO J. 13:2192-2199(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHO80.
  10. "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: INTERACTION WITH PHO2; PHO80 AND PHO81.
  11. "Phosphorylation of the transcription factor PHO4 by a cyclin-CDK complex, PHO80-PHO85."
    Kaffman A., Herskowitz I., Tjian R., O'Shea E.K.
    Science 263:1153-1156(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  12. "Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex."
    O'Neill E.M., Kaffman A., Jolly E.R., O'Shea E.K.
    Science 271:209-212(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-100; SER-114; SER-128; SER-152 AND SER-223, SUBCELLULAR LOCATION.
  13. "Roles of phosphorylation sites in regulating activity of the transcription factor Pho4."
    Komeili A., O'Shea E.K.
    Science 284:977-980(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-100; SER-114; SER-128; SER-152 AND SER-223.
  14. "Nine-amino-acid transactivation domain: establishment and prediction utilities."
    Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
    Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  15. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  16. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition."
    Shimizu T., Toumoto A., Ihara K., Shimizu M., Kyogoku Y., Ogawa N., Oshima Y., Hakoshima T.
    EMBO J. 16:4689-4697(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 251-312.

Entry informationi

Entry nameiPHO4_YEAST
AccessioniPrimary (citable) accession number: P07270
Secondary accession number(s): D6VTR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 9, 2007
Last modified: October 29, 2014
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3