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P07270 (PHO4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphate system positive regulatory protein PHO4
Gene names
Name:PHO4
Ordered Locus Names:YFR034C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.9 Ref.10

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly cytoplasmic under high-phosphate conditions and localized to the nucleus upon phosphate starvation. Ref.12

Domain

the 9aaTAD motif (residues 75 to 83) is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.7 Ref.14

Post-translational modification

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. Ref.11 Ref.12 Ref.13

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Phosphate system positive regulatory protein PHO4
PRO_0000127422

Regions

Domain250 – 30657bHLH
Region1 – 3131Interaction with PHO80
Region75 – 9925Transcription activation domain
Region156 – 20045Interaction with PHO80
Region201 – 21818Interaction with PHO2
Region203 – 22725Involved in oligomerization
Motif75 – 8399aaTAD
Motif140 – 16627Nuclear localization signal

Amino acid modifications

Modified residue1001Phosphoserine; by PHO85 Ref.12 Ref.13
Modified residue1141Phosphoserine; by PHO85 Ref.12 Ref.13
Modified residue1281Phosphoserine; by PHO85 Ref.12 Ref.13
Modified residue1521Phosphoserine; by PHO85 Ref.12 Ref.13
Modified residue2041Phosphoserine Ref.17
Modified residue2231Phosphoserine; by PHO85 Ref.12 Ref.13 Ref.15 Ref.18
Modified residue2421Phosphoserine Ref.16
Modified residue2431Phosphoserine Ref.16

Experimental info

Sequence conflict2691A → P in CAA27345. Ref.1
Sequence conflict2691A → P Ref.2
Sequence conflict3101V → G Ref.2

Secondary structure

......... 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07270 [UniParc].

Last modified January 9, 2007. Version 4.
Checksum: 6DB93C0DDDB4D741

FASTA31234,089
        10         20         30         40         50         60 
MGRTTSEGIH GFVDDLEPKS SILDKVGDFI TVNTKRHDGR EDFNEQNDEL NSQENHNSSE 

        70         80         90        100        110        120 
NGNENENEQD SLALDDLDRA FELVEGMDMD WMMPSHAHHS PATTATIKPR LLYSPLIHTQ 

       130        140        150        160        170        180 
SAVPVTISPN LVATATSTTS ANKVTKNKSN SSPYLNKRRG KPGPDSATSL FELPDSVIPT 

       190        200        210        220        230        240 
PKPKPKPKQY PKVILPSNST RRVSPVTAKT SSSAEGVVVA SESPVIAPHG SSHSRSLSKR 

       250        260        270        280        290        300 
RSSGALVDDD KRESHKHAEQ ARRNRLAVAL HELASLIPAE WKQQNVSAAP SKATTVEAAC 

       310 
RYIRHLQQNV ST 

« Hide

References

« Hide 'large scale' references
[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]"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.
Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS56289.
RefSeqNP_116692.1. NM_001179999.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0AX-ray2.80A/B250-312[»]
3W3XX-ray2.90B140-166[»]
ProteinModelPortalP07270.
SMRP07270. Positions 251-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31191. 190 interactions.
DIPDIP-911N.
IntActP07270. 112 interactions.
MINTMINT-2779852.

Proteomic databases

PaxDbP07270.
PRIDEP07270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFR034C; YFR034C; YFR034C.
GeneID850594.
KEGGsce:YFR034C.

Organism-specific databases

CYGDYFR034c.
SGDS000001930. PHO4.

Phylogenomic databases

eggNOGNOG39146.
KOK06658.
OrthoDBEOG7W6X0F.

Enzyme and pathway databases

BioCycYEAST:G3O-30481-MONOMER.

Gene expression databases

GenevestigatorP07270.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07270.
NextBio966449.

Entry information

Entry namePHO4_YEAST
AccessionPrimary (citable) accession number: P07270
Secondary accession number(s): D6VTR7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VI

Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references