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P07270

- PHO4_YEAST

UniProt

P07270 - PHO4_YEAST

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
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (09 Jan 2007)
      Previous versions | rss
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    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

    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

    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 PHO853 Publications
    Modified residuei114 – 1141Phosphoserine; by PHO853 Publications
    Modified residuei128 – 1281Phosphoserine; by PHO853 Publications
    Modified residuei152 – 1521Phosphoserine; by PHO853 Publications
    Modified residuei204 – 2041Phosphoserine2 Publications
    Modified residuei223 – 2231Phosphoserine; by PHO855 Publications
    Modified residuei242 – 2421Phosphoserine2 Publications
    Modified residuei243 – 2431Phosphoserine2 Publications

    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.
    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

    MGRTTSEGIH GFVDDLEPKS SILDKVGDFI TVNTKRHDGR EDFNEQNDEL    50
    NSQENHNSSE NGNENENEQD SLALDDLDRA FELVEGMDMD WMMPSHAHHS 100
    PATTATIKPR LLYSPLIHTQ SAVPVTISPN LVATATSTTS ANKVTKNKSN 150
    SSPYLNKRRG KPGPDSATSL FELPDSVIPT PKPKPKPKQY PKVILPSNST 200
    RRVSPVTAKT SSSAEGVVVA SESPVIAPHG SSHSRSLSKR RSSGALVDDD 250
    KRESHKHAEQ ARRNRLAVAL HELASLIPAE WKQQNVSAAP SKATTVEAAC 300
    RYIRHLQQNV ST 312
    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.
    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

    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 1, 2014
    This is version 152 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