Serine/threonine-protein phosphatase PP-Z1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P26570 (PPZ1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 134. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP-Z1
EC=3.1.3.16

Gene names

Name:	PPZ1
Ordered Locus Names:	YML016C
ORF Names:	YM9571.02C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	692 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for the maintenance of cell size and integrity in response to osmotic stress.
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion 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).

Ontologies

Keywords
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein localization Inferred from mutant phenotype PubMed 21237705. Source: SGD cellular sodium ion homeostasis Inferred from genetic interaction PubMed 7768897. Source: SGD protein dephosphorylation Inferred from mutant phenotype PubMed 21237705. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 11914276. Source: SGD extrinsic to plasma membrane Inferred from direct assay PubMed 16166647. Source: SGD nucleus Inferred from direct assay PubMed 11914276 PubMed 8824289. Source: SGD
Molecular_function	cofactor binding Inferred from electronic annotation. Source: InterPro magnesium-dependent protein serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay PubMed 7615085. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CAB3	P36076	6	EBI-13807,EBI-26778
SIS2	P36024	5	EBI-13807,EBI-17250
VHS3	Q08438	4	EBI-13807,EBI-30482

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 692

691

Serine/threonine-protein phosphatase PP-Z1

PRO_0000058891

Regions

Compositional bias

2 – 319

318

Ser-rich

Sites

Active site

480

Proton donor By similarity

Metal binding

419

Iron By similarity

Metal binding

421

Iron By similarity

Metal binding

447

Iron By similarity

Metal binding

447

Manganese By similarity

Metal binding

479

Manganese By similarity

Metal binding

528

Manganese By similarity

Metal binding

603

Manganese By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.10

Modified residue

171

Phosphothreonine Ref.10

Modified residue

249

Phosphoserine Ref.11

Modified residue

261

Phosphothreonine Ref.10

Modified residue

265

Phosphoserine Ref.10

Lipidation

N-myristoyl glycine Potential

Experimental info

Sequence conflict

340

E → G in AAA34898. Ref.1

Sequence conflict

440

S → A no nucleotide entry Ref.5

Sequence conflict

649

E → K no nucleotide entry Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P26570 [UniParc].

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

692

77,491

        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' referencesShow '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. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. Strain: ADR376.
[11]	"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-249, MASS SPECTROMETRY.
+	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.
PIR	PABY12. S55103.
RefSeq	NP_013696.1. NM_001182374.1.
3D structure databases
ProteinModelPortal	P26570.
SMR	P26570. Positions 361-653.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-557N.
IntAct	P26570. 44 interactions.
MINT	MINT-709853.
STRING	4932.YML016C.
Proteomic databases
PaxDb	P26570.
PeptideAtlas	P26570.
PRIDE	P26570.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML016C; YML016C; YML016C.
GeneID	854992.
KEGG	sce:YML016C.
Organism-specific databases
SGD	S000004478. PPZ1.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00700000105101.
HOGENOM	HOG000172697.
KO	K01090.
OMA	YYENALT.
OrthoDB	EOG479JGP.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32620-MONOMER.
Gene expression databases
Genevestigator	P26570.
GermOnline	YML016C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR011159. PPPtase_PPZ. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PIRSF	PIRSF000909. PPPtase_PPZ. 1 hit.
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	978133.

Entry information

Entry name

PPZ1_YEAST

Accession

Primary (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:	May 29, 2013
This is version 134 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents