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Reviewed, UniProtKB/Swiss-Prot P11491 (PPB_YEAST)

Last modified January 19, 2010. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Repressible alkaline phosphatase
    EC=3.1.3.1
Gene names
Name: PHO8
Ordered Locus Names: YDR481C
ORF Names: D8035.24
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 length566 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactor

Binds 1 magnesium ion By similarity.

Binds 2 zinc ions By similarity.

Subcellular location

Vacuole membrane; Single-pass membrane protein Potential. Note: Lysosome-like vacuoles. Ref.3

Miscellaneous

Present with 3060 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the alkaline phosphatase family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

RPN3P400161EBI-13762,EBI-15927
SSA1P105911EBI-13762,EBI-8591

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ?Repressible alkaline phosphatasePRO_0000024017
Propeptide? – 566Removed in mature formPRO_0000024018

Regions

Topological domain1 – 3333Cytoplasmic Ref.3
Transmembrane34 – 5926 Potential
Topological domain60 – ?Vacuolar Ref.3

Sites

Active site1231Phosphoserine intermediate By similarity
Metal binding751Magnesium By similarity
Metal binding751Zinc 2 By similarity
Metal binding1741Magnesium By similarity
Metal binding1761Magnesium By similarity
Metal binding3251Magnesium By similarity
Metal binding3301Zinc 1 By similarity
Metal binding3341Zinc 1 By similarity
Metal binding3731Zinc 2 By similarity
Metal binding3741Zinc 2 By similarity
Metal binding4841Zinc 1 By similarity

Amino acid modifications

Modified residue1211Phosphothreonine Ref.6
Modified residue1231Phosphoserine Ref.6 Ref.5
Modified residue1281Phosphothreonine Ref.6
Glycosylation2681N-linked (GlcNAc...)
Glycosylation4011N-linked (GlcNAc...)

Experimental info

Sequence conflict51T → R in AAA34871. Ref.1
Sequence conflict551S → T in AAA34871. Ref.1
Sequence conflict591L → I in AAA34871. Ref.1
Sequence conflict1321C → S in AAA34871. Ref.1
Sequence conflict2711L → F in AAA34871. Ref.1
Sequence conflict4471D → E in AAA34871. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P11491-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 9FA2E87B068FF0DB

FASTA56663,004
        10         20         30         40         50         60 
MMTHTLPSEQ TRLVPGSDSS SRPKKRRISK RSKIIVSTVV CIGLLLVLVQ LAFPSSFALR 

        70         80         90        100        110        120 
SASHKKKNVI FFVTDGMGPA SLSMARSFNQ HVNDLPIDDI LTLDEHFIGS SRTRSSDSLV 

       130        140        150        160        170        180 
TDSAAGATAF ACALKSYNGA IGVDPHHRPC GTVLEAAKLA GYLTGLVVTT RITDATPASF 

       190        200        210        220        230        240 
SSHVDYRWQE DLIATHQLGE YPLGRVVDLL MGGGRSHFYP QGEKASPYGH HGARKDGRDL 

       250        260        270        280        290        300 
IDEAQSNGWQ YVGDRKNFDS LLKSHGENVT LPFLGLFADN DIPFEIDRDE KEYPSLKEQV 

       310        320        330        340        350        360 
KVALGALEKA SNEDKDSNGF FLMVEGSRID HAGHQNDPAS QVREVLAFDE AFQYVLEFAE 

       370        380        390        400        410        420 
NSDTETVLVS TSDHETGGLV TSRQVTASYP QYVWYPQVLA NATHSGEFLK RKLVDFVHEH 

       430        440        450        460        470        480 
KGASSKIENF IKHEILEKDL GIYDYTDSDL ETLIHLDDNA NAIQDKLNDM VSFRAQIGWT 

       490        500        510        520        530        540 
THGHSAVDVN IYAYANKKAT WSYVLNNLQG NHENTEVGQF LENFLELNLN EVTDLIRDTK 

       550        560 
HTSDFDATEI ASEVQHYDEY YHELTN

« Hide

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References

« Hide 'large scale' references
[1]"Structural characteristics of the PHO8 gene encoding repressible alkaline phosphatase in Saccharomyces cerevisiae."
Kaneko Y., Hayashi N., Toh-e A., Banno I., Oshima Y.
Gene 58:137-148(1987) [PubMed: 3319783] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: P-28-24C.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase."
Klionsky D.J., Emr S.D.
EMBO J. 8:2241-2250(1989) [PubMed: 2676517] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, TOPOLOGY, SUBCELLULAR LOCATION.
[4]"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].
[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 SER-123, MASS SPECTROMETRY.
[6]"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-121; SER-123 AND THR-128, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M21134 Genomic DNA. Translation: AAA34871.1.
U33050 Genomic DNA. Translation: AAB64930.1.
PIRS69648.
RefSeqNP_010769.1.

3D structure databases

SMRP11491. Positions 55-528.
ModBaseSearch...

Protein-protein interaction databases

IntActP11491. 4 interactions.
STRINGP11491.

Proteomic databases

PeptideAtlasP11491.

Genome annotation databases

EnsemblYDR481C; YDR481C; YDR481C; Saccharomyces cerevisiae. [Genome view]
GeneID852092.
KEGGsce:YDR481C.
NMPDRfig|4932.3.peg.1542.

Organism-specific databases

CYGDYDR481c.
SGDS000002889. PHO8.

Phylogenomic databases

eggNOGfuNOG04370.
HOGENOMHBG617166.
OMASEITHAT.
OrthoDBEOG9XSN64.
PhylomeDBP11491.

Enzyme and pathway databases

BRENDA3.1.3.1. 250.

Gene expression databases

ArrayExpressP11491.
GenevestigatorP11491.
GermOnlineYDR481C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
Gene3DG3DSA:3.40.720.10. Alk_phosphtse. 1 hit.
PfamPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00113. ALKPHPHTASE.
SMARTSM00098. alkPPc. 1 hit.
[Graphical view]
PROSITEPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio970421.

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Entry information

Entry namePPB_YEAST
AccessionPrimary (citable) accession number: P11491
Secondary accession number(s): Q03374
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 15, 1998
Last modified: January 19, 2010
This is version 102 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

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