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P26570 (PPZ1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. 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-Z1

EC=3.1.3.16
Gene names
Name:PPZ1
Ordered Locus Names:YML016C
ORF Names:YM9571.02C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length692 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.

Enzyme regulation

Inhibited by the regulatory subunits VHS3 and SIS2.

Subunit structure

Interacts with SIS2 and VHS3, which regulate its activity. Ref.7 Ref.9

Miscellaneous

Present with 217 molecules/cell in log phase SD medium.

Sequence similarities

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

Caution

Was originally (Ref.5) thought to originate from a rabbit cDNA library and was known as protein phosphatase Z (PP-Z).

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 692691Serine/threonine-protein phosphatase PP-Z1
PRO_0000058891

Regions

Compositional bias2 – 319318Ser-rich

Sites

Active site4801Proton donor By similarity
Metal binding4191Manganese 1 By similarity
Metal binding4211Manganese 1 By similarity
Metal binding4471Manganese 1 By similarity
Metal binding4471Manganese 2 By similarity
Metal binding4791Manganese 2 By similarity
Metal binding5281Manganese 2 By similarity
Metal binding6031Manganese 2 By similarity

Amino acid modifications

Modified residue491Phosphoserine Ref.10
Modified residue1711Phosphothreonine Ref.10
Modified residue2221Phosphoserine Ref.11
Modified residue2611Phosphothreonine Ref.10
Modified residue2651Phosphoserine Ref.10
Modified residue6901Phosphoserine Ref.11
Lipidation21N-myristoyl glycine Potential

Experimental info

Sequence conflict3401E → G in AAA34898. Ref.1
Sequence conflict4401S → A no nucleotide entry Ref.5
Sequence conflict6491E → K no nucleotide entry Ref.5

Sequences

Sequence LengthMass (Da)Tools
P26570 [UniParc].

Last modified October 5, 2010. Version 5.
Checksum: 8B7F009521F72C15

FASTA69277,491
        10         20         30         40         50         60 
MGNSSSKSSK KDSHSNSSSR NPRPQVSRTE TSHSVKSAKS NKSSRSRRSL PSSSTTNTNS 

        70         80         90        100        110        120 
NVPDPSTPSK PNLEVNHQRH SSHTNRYHFP SSSHSHSNSQ NELLTTPSSS STKRPSTSRR 

       130        140        150        160        170        180 
SSYNTKAAAD LPPSMIQMEP KSPILKTNNS STHVSKHKSS YSSTYYENAL TDDDNDDKDN 

       190        200        210        220        230        240 
DISHTKRFSR SSNSRPSSIR SGSVSRRKSD VTHEEPNNGS YSSNNQENYL VQALTRSNSH 

       250        260        270        280        290        300 
ASSLHSRKSS FGSDGNTAYS TPLNSPGLSK LTDHSGEYFT SNSTSSLNHH SSRDIYPSKH 

       310        320        330        340        350        360 
ISNDDDIENS SQLSNIHASM ENVNDKNNNI TDSKKDPNEE FNDIMQSSGN KNAPKKFKKP 

       370        380        390        400        410        420 
IDIDETIQKL LDAGYAAKRT KNVCLKNNEI LQICIKAREI FLSQPSLLEL SPPVKIVGDV 

       430        440        450        460        470        480 
HGQYGDLLRL FTKCGFPPSS NYLFLGDYVD RGKQSLETIL LLFCYKIKYP ENFFLLRGNH 

       490        500        510        520        530        540 
ECANVTRVYG FYDECKRRCN IKIWKTFIDT FNTLPLAAIV AGKIFCVHGG LSPVLNSMDE 

       550        560        570        580        590        600 
IRHVVRPTDV PDFGLINDLL WSDPTDSPNE WEDNERGVSY CYNKVAINKF LNKFGFDLVC 

       610        620        630        640        650        660 
RAHMVVEDGY EFFNDRSLVT VFSAPNYCGE FDNWGAVMSV SEGLLCSFEL LDPLDSAALK 

       670        680        690 
QVMKKGRQER KLANQQQQMM ETSITNDNES QQ 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and analysis of a yeast protein phosphatase with an unusual amino-terminal region."
Posas F., Casamayor A., Morral N., Arino J.
J. Biol. Chem. 267:11734-11740(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: M5.
[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 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] [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 serine/threonine phosphatases; an expanding family."
Cohen P.T.W., Brewis N.D., Hughes V., Mann D.J.
FEBS Lett. 268:355-359(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 345-692.
[6]"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 389-610.
[7]"The yeast halotolerance determinant Hal3p is an inhibitory subunit of the Ppz1p Ser/Thr protein phosphatase."
de Nadal E., Clotet J., Posas F., Serrano R., Gomez N., Arino J.
Proc. Natl. Acad. Sci. U.S.A. 95:7357-7362(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIS2.
[8]"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].
[9]"Functional characterization of the Saccharomyces cerevisiae VHS3 gene. A regulatory subunit of the Ppz1 protein phosphatase with novel, phosphatase-unrelated functions."
Ruiz A., Munoz I., Serrano R., Gonzalez A., Simon E., Arino J.
J. Biol. Chem. 279:34421-34430(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VHS3.
[10]"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-49; THR-171; THR-261 AND SER-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[11]"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-222 AND SER-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86242 Genomic DNA. Translation: AAA34898.1.
X74135 Genomic DNA. Translation: CAA52232.1.
Z49810 Genomic DNA. Translation: CAA89936.1.
BK006946 Genomic DNA. Translation: DAA09882.1.
PIRPABY12. S55103.
RefSeqNP_013696.1. NM_001182374.1.

3D structure databases

ProteinModelPortalP26570.
SMRP26570. Positions 361-653.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35153. 191 interactions.
DIPDIP-557N.
IntActP26570. 43 interactions.
MINTMINT-709853.
STRING4932.YML016C.

Proteomic databases

MaxQBP26570.
PaxDbP26570.
PeptideAtlasP26570.
PRIDEP26570.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML016C; YML016C; YML016C.
GeneID854992.
KEGGsce:YML016C.

Organism-specific databases

SGDS000004478. PPZ1.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00710000107291.
HOGENOMHOG000172697.
KOK06269.
OMAYYENALT.
OrthoDBEOG79KPQ9.

Enzyme and pathway databases

BioCycYEAST:G3O-32620-MONOMER.

Gene expression databases

GenevestigatorP26570.

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

NextBio978133.

Entry information

Entry namePPZ1_YEAST
AccessionPrimary (citable) accession number: P26570
Secondary accession number(s): D6VZF8, Q00979
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 5, 2010
Last modified: June 11, 2014
This is version 145 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families