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Reviewed, UniProtKB/Swiss-Prot P25297 (PHO84_YEAST)

Last modified November 24, 2009. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Inorganic phosphate transporter PHO84
Gene names
Name: PHO84
Ordered Locus Names: YML123C
ORF Names: YM7056.03C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

High-affinity transporter for external inorganic phosphate. Is not an essential protein, since a constitutive, low affinity pI transporter exists in yeast.

Subunit structure

May function as a monomer.

Subcellular location

Membrane; Multi-pass membrane protein.

Induction

Under the control of phosphate. It is derepressed by phosphate starvation.

Miscellaneous

Present with 335000 molecules/cell in log phase SD medium. Ref.3

Sequence similarities

Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. [View classification]

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

AGP1P253761EBI-13320,EBI-2357
CAN1P048171EBI-13320,EBI-3993
CBR1P386261EBI-13320,EBI-2048224
CHO1P084561EBI-13320,EBI-14055
COS1P538221EBI-13320,EBI-4959
COS4P435421EBI-13320,EBI-2050225
CPT1P178981EBI-13320,EBI-2050738
EHT1P382951EBI-13320,EBI-20890
ERG11P106141EBI-13320,EBI-5127
ERG25P530451EBI-13320,EBI-6506
ERG26P531991EBI-13320,EBI-6514
ERG3P323531EBI-13320,EBI-6554
ERG5P547811EBI-13320,EBI-6563
ERP1Q053591EBI-13320,EBI-6581
ERV25P548371EBI-13320,EBI-6642
ERV41Q046511EBI-13320,EBI-27850
GAA1P390121EBI-13320,EBI-7252
GAP1P191451EBI-13320,EBI-7314
GPI17Q040801EBI-13320,EBI-7777
GPI8P490181EBI-13320,EBI-7822
HMG2P126841EBI-13320,EBI-8384
HNM1P198071EBI-13320,EBI-8409
ILM1P471551EBI-13320,EBI-2051644
KEX1P096201EBI-13320,EBI-9653
KRE27P405401EBI-13320,EBI-24977
LAC1P284961EBI-13320,EBI-26585
LSP1Q122301EBI-13320,EBI-34978
MCD4P360511EBI-13320,EBI-2070979
NCP1P166031EBI-13320,EBI-11940
NKP2Q061621EBI-13320,EBI-34256
OLE1P211471EBI-13320,EBI-2098
OSH7P387551EBI-13320,EBI-12641
OST1P415431EBI-13320,EBI-12651
PHO86P469561EBI-13320,EBI-13337
PHO88P382641EBI-13320,EBI-13350
PIS1P061971EBI-13320,EBI-13458
PKR1Q038801EBI-13320,EBI-27252
PST2Q123351EBI-13320,EBI-14064
RTN1Q049471EBI-13320,EBI-38020
SAC1P323681EBI-13320,EBI-16210
SCS7Q035291EBI-13320,EBI-16747
SEY1Q992871EBI-13320,EBI-37523
SHR3Q027741EBI-13320,EBI-17099
SLC1P333331EBI-13320,EBI-13494
SOP4P395431EBI-13320,EBI-26193
SPC1P469651EBI-13320,EBI-17823
SPC2Q049691EBI-13320,EBI-27827
SPF1P399861EBI-13320,EBI-3128
SSH1P383531EBI-13320,EBI-18175
STE24P471541EBI-13320,EBI-18298
SUR2P389921EBI-13320,EBI-18574
SWP1Q027951EBI-13320,EBI-12666
TCB3Q036401EBI-13320,EBI-27872
VHS3Q084381EBI-13320,EBI-30482
VMA21P418061EBI-13320,EBI-20323
WBP1P337671EBI-13320,EBI-12658
YOP1Q124021EBI-13320,EBI-37092

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 587587Inorganic phosphate transporter PHO84
PRO_0000050477

Regions

Topological domain1 – 6767Cytoplasmic Potential
Transmembrane68 – 88211 Potential
Topological domain89 – 10820Extracellular Potential
Transmembrane109 – 129212 Potential
Topological domain130 – 1334Cytoplasmic Potential
Transmembrane134 – 154213 Potential
Topological domain155 – 1562Extracellular Potential
Transmembrane157 – 177214 Potential
Topological domain178 – 20124Cytoplasmic Potential
Transmembrane202 – 222215 Potential
Topological domain223 – 25028Extracellular Potential
Transmembrane251 – 271216 Potential
Topological domain272 – 34574Cytoplasmic Potential
Transmembrane346 – 366217 Potential
Topological domain367 – 39529Extracellular Potential
Transmembrane396 – 416218 Potential
Topological domain417 – 4193Cytoplasmic Potential
Transmembrane420 – 440219 Potential
Topological domain441 – 4422Extracellular Potential
Transmembrane443 – 4632110 Potential
Topological domain464 – 48522Cytoplasmic Potential
Transmembrane486 – 5062111 Potential
Topological domain507 – 52216Extracellular Potential
Transmembrane523 – 5432112 Potential
Topological domain544 – 58744Cytoplasmic Potential

Amino acid modifications

Modified residue221Phosphothreonine Ref.7
Modified residue3021Phosphothreonine Ref.7 Ref.4 Ref.5
Modified residue3031Phosphoserine Ref.7 Ref.4 Ref.5
Modified residue3161Phosphoserine Ref.7 Ref.5
Modified residue3171Phosphothreonine Ref.7 Ref.4 Ref.5 Ref.6
Modified residue3211Phosphoserine Ref.7 Ref.4 Ref.5 Ref.6
Modified residue5771Phosphoserine Ref.7 Ref.5
Modified residue5781Phosphoserine Ref.7 Ref.6
Modified residue5791Phosphoserine Ref.7 Ref.4 Ref.5
Modified residue5811Phosphoserine Ref.7 Ref.5
Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4
Cross-link298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4

Experimental info

Sequence conflict1621A → AHSPAINFVA Ref.1
Sequence conflict3531S → Y in BAA14358. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P25297-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: E463954395E8A840

FASTA58764,382
        10         20         30         40         50         60 
MSSVNKDTIH VAERSLHKEH LTEGGNMAFH NHLNDFAHIE DPLERRRLAL ESIDDEGFGW 

        70         80         90        100        110        120 
QQVKTISIAG VGFLTDSYDI FAINLGITMM SYVYWHGSMP GPSQTLLKVS TSVGTVIGQF 

       130        140        150        160        170        180 
GFGTLADIVG RKRIYGMELI IMIVCTILQT TVAHSPAINF VAVLTFYRIV MGIGIGGDYP 

       190        200        210        220        230        240 
LSSIITSEFA TTKWRGAIMG AVFANQAWGQ ISGGIIALIL VAAYKGELEY ANSGAECDAR 

       250        260        270        280        290        300 
CQKACDQMWR ILIGLGTVLG LACLYFRLTI PESPRYQLDV NAKLELAAAA QEQDGEKKIH 

       310        320        330        340        350        360 
DTSDEDMAIN GLERASTAVE SLDNHPPKAS FKDFCRHFGQ WKYGKILLGT AGSWFTLDVA 

       370        380        390        400        410        420 
FYGLSLNSAV ILQTIGYAGS KNVYKKLYDT AVGNLILICA GSLPGYWVSV FTVDIIGRKP 

       430        440        450        460        470        480 
IQLAGFIILT ALFCVIGFAY HKLGDHGLLA LYVICQFFQN FGPNTTTFIV PGECFPTRYR 

       490        500        510        520        530        540 
STAHGISAAS GKVGAIIAQT ALGTLIDHNC ARDGKPTNCW LPHVMEIFAL FMLLGIFTTL 

       550        560        570        580 
LIPETKRKTL EEINELYHDE IDPATLNFRN KNNDIESSSP SQLQHEA

« Hide

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References

« Hide 'large scale' references
[1]"The PHO84 gene of Saccharomyces cerevisiae encodes an inorganic phosphate transporter."
Bun-Ya M., Nishimura M., Harashima S., Oshima Y.
Mol. Cell. Biol. 11:3229-3238(1991) [PubMed: 2038328] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed: 9169872] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302; SER-303; THR-317; SER-321 AND SER-579, UBIQUITINATION AT LYS-6 AND LYS-298, MASS SPECTROMETRY.
[5]"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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302; SER-303; SER-316; THR-317; SER-321; SER-577; SER-579 AND SER-581, MASS SPECTROMETRY.
[6]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-317; SER-321 AND SER-578, MASS SPECTROMETRY.
[7]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22; THR-302; SER-303; SER-316; THR-317; SER-321; SER-577; SER-578; SER-579 AND SER-581, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

D90346 Genomic DNA. Translation: BAA14358.1.
Z49218 Genomic DNA. Translation: CAA89157.1.
PIRS54061.
RefSeqNP_013583.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5072N.
IntActP25297. 78 interactions.
STRINGP25297.

Protein family/group databases

TCDB2.A.1.9.1. major facilitator superfamily (MFS).

Proteomic databases

PeptideAtlasP25297.
PRIDEP25297.

Genome annotation databases

EnsemblYML123C; YML123C; YML123C; Saccharomyces cerevisiae. [Genome view]
GeneID854916.
KEGGsce:YML123C.
NMPDRfig|4932.3.peg.4619.

Organism-specific databases

CYGDYML123c.
SGDS000004592. PHO84.

Phylogenomic databases

HOGENOMP25297.
OMACQFFQNF
OrthoDBEOG9PZKQ9

Gene expression databases

ArrayExpressP25297.
GenevestigatorP25297.
GermOnlineYML123C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR016196. MFS_general_subst_transpt.
IPR004738. Phos_permease.
IPR005828. Sub_transporter.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamPF00083. Sugar_tr. 1 hit.
[Graphical view]
TIGRFAMsTIGR00887. 2A0109. 1 hit.
PROSITEPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
PS00217. SUGAR_TRANSPORT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio977923.

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Entry information

Entry namePHO84_YEAST
AccessionPrimary (citable) accession number: P25297
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: November 24, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIII

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents