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P33329 (PPZ2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP-Z2

EC=3.1.3.16
Gene names
Name:PPZ2
Ordered Locus Names:YDR436W
ORF Names:D9461.22
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length710 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for the maintenance of cell size and integrity in response to osmotic stress.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Miscellaneous

Present with 189 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PPP phosphatase family. PP-Z subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CAB3P360764EBI-13815,EBI-26778

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 710709Serine/threonine-protein phosphatase PP-Z2
PRO_0000058892

Regions

Compositional bias346 – 3538Poly-Ser

Sites

Active site5151Proton donor By similarity
Metal binding4541Manganese 1 By similarity
Metal binding4561Manganese 1 By similarity
Metal binding4821Manganese 1 By similarity
Metal binding4821Manganese 2 By similarity
Metal binding5141Manganese 2 By similarity
Metal binding5631Manganese 2 By similarity
Metal binding6381Manganese 2 By similarity

Amino acid modifications

Modified residue711Phosphoserine Ref.10
Modified residue2031Phosphoserine Ref.8
Modified residue2241Phosphoserine Ref.10
Modified residue3101Phosphoserine Ref.10
Lipidation21N-myristoyl glycine Potential

Experimental info

Sequence conflict2311S → T in AAA34899. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P33329 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 3095F37046489AFB

FASTA71078,492
        10         20         30         40         50         60 
MGNSGSKQHT KHNSKKDDHD GDRKKTLDLP PLTKSDTTHS LKSSRSLRSL RSKRSEASLA 

        70         80         90        100        110        120 
SNVQAQTQPL SRRSSTLGNG NRNHRRSNNA PITPPNNHYL TSHPSSSRRL SSSSRRSSMG 

       130        140        150        160        170        180 
NNNNSELPPS MIQMEPKSPI LKNSTSMHST SSFNSYENAL TDDDDDRGDD GGESPSMAKV 

       190        200        210        220        230        240 
TRINTSSSAD RGSKRTPLRR HNSLQPEKGV TGFSSTSSKL RRRSDNTLPA SYPLNAEAGG 

       250        260        270        280        290        300 
NGSDYFSNRS NSHASSRKSS FGSTGNTAYS TPLHSPALRK MSSRDNDDSG DNVNGRGTSP 

       310        320        330        340        350        360 
IPNLNIDKPS PSASSASKRE YLSAYPTLAH RDSSSSLSPR GKGQRSSSSS SSSQRIYVSP 

       370        380        390        400        410        420 
PSPTGDFVHG SCADGDNGSR TNTMVEMKRK KPVRPVDIDE IIQRLLDAGY AAKRTKNVCL 

       430        440        450        460        470        480 
KNSEIIQICH KARELFLAQP ALLELSPSVK IVGDVHGQYA DLLRLFTKCG FPPMANYLFL 

       490        500        510        520        530        540 
GDYVDRGKQS LETILLLLCY KIKYPENFFL LRGNHECANV TRVYGFYDEC KRRCNIKIWK 

       550        560        570        580        590        600 
TFVDTFNTLP LAAIVTGKIF CVHGGLSPVL NSMDEIRHVS RPTDVPDFGL INDLLWSDPT 

       610        620        630        640        650        660 
DSSNEWEDNE RGVSFCYNKV AINKFLNKFG FDLVCRAHMV VEDGYEFFND RSLVTVFSAP 

       670        680        690        700        710 
NYCGEFDNWG AVMTVSEGLL CSFELLDPLD STALKQVMKK GRQERKLANR 

« Hide

References

« Hide 'large scale' references
[1]"A pair of functionally redundant yeast genes (PPZ1 and PPZ2) encoding type 1-related protein phosphatases function within the PKC1-mediated pathway."
Lee K.S., Hines L.K., Levin D.E.
Mol. Cell. Biol. 13:5843-5853(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Both isoforms of protein phosphatase Z are essential for the maintenance of cell size and integrity in Saccharomyces cerevisiae in response to osmotic stress."
Hughes V., Mueller A., Stark M.J.R., Cohen P.T.W.
Eur. J. Biochem. 216:269-279(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AY926.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Protein phosphatase 2Bw and protein phosphatase Z are Saccharomyces cerevisiae enzymes."
Da Cruz e Silva E.F., Hughes V., McDonald P., Stark M.J.R., Cohen P.T.W.
Biochim. Biophys. Acta 1089:269-272(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 424-645.
[6]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[8]"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-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-71; SER-224 AND SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74136 Genomic DNA. Translation: CAA52233.1.
L10241 Genomic DNA. Translation: AAA34899.1.
U33007 Genomic DNA. Translation: AAB64859.1.
BK006938 Genomic DNA. Translation: DAA12273.1.
PIRS35674.
RefSeqNP_010724.1. NM_001180744.1.

3D structure databases

ProteinModelPortalP33329.
SMRP33329. Positions 396-688.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32492. 51 interactions.
DIPDIP-6355N.
IntActP33329. 12 interactions.
MINTMINT-694847.
STRING4932.YDR436W.

Proteomic databases

MaxQBP33329.
PaxDbP33329.
PRIDEP33329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR436W; YDR436W; YDR436W.
GeneID852046.
KEGGsce:YDR436W.

Organism-specific databases

SGDS000002844. PPZ2.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00710000107291.
HOGENOMHOG000172697.
KOK06269.
OMAYSTPLHS.
OrthoDBEOG79KPQ9.

Enzyme and pathway databases

BioCycYEAST:YDR436W-MONOMER.

Gene expression databases

GenevestigatorP33329.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR011159. PPPtase_PPZ.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFPIRSF000909. PPPtase_PPZ. 1 hit.
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970299.

Entry information

Entry namePPZ2_YEAST
AccessionPrimary (citable) accession number: P33329
Secondary accession number(s): D6VT63
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 143 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 IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families