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Protein

Serine/threonine-protein phosphatase PP-Z2

Gene

PPZ2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi454 – 4541Manganese 1By similarity
Metal bindingi456 – 4561Manganese 1By similarity
Metal bindingi482 – 4821Manganese 1By similarity
Metal bindingi482 – 4821Manganese 2By similarity
Metal bindingi514 – 5141Manganese 2By similarity
Active sitei515 – 5151Proton donorBy similarity
Metal bindingi563 – 5631Manganese 2By similarity
Metal bindingi638 – 6381Manganese 2By similarity

GO - Molecular functioni

  1. cofactor binding Source: InterPro
  2. magnesium-dependent protein serine/threonine phosphatase activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. protein serine/threonine phosphatase activity Source: SGD

GO - Biological processi

  1. cellular sodium ion homeostasis Source: SGD
  2. dephosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YDR436W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP-Z2 (EC:3.1.3.16)
Gene namesi
Name:PPZ2
Ordered Locus Names:YDR436W
ORF Names:D9461.22
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

SGDiS000002844. PPZ2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedSequence Analysis
Chaini2 – 710709Serine/threonine-protein phosphatase PP-Z2PRO_0000058892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence Analysis
Modified residuei55 – 551PhosphoserineBy similarity
Modified residuei71 – 711Phosphoserine1 Publication
Modified residuei161 – 1611PhosphothreonineBy similarity
Modified residuei203 – 2031Phosphoserine1 Publication
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei271 – 2711PhosphothreonineBy similarity
Modified residuei275 – 2751PhosphoserineBy similarity
Modified residuei310 – 3101Phosphoserine1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiP33329.
PaxDbiP33329.
PRIDEiP33329.

Expressioni

Gene expression databases

GenevestigatoriP33329.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CAB3P360764EBI-13815,EBI-26778

Protein-protein interaction databases

BioGridi32492. 51 interactions.
DIPiDIP-6355N.
IntActiP33329. 12 interactions.
MINTiMINT-694847.
STRINGi4932.YDR436W.

Structurei

3D structure databases

SMRiP33329. Positions 396-688.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi346 – 3538Poly-Ser

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00710000107291.
HOGENOMiHOG000172697.
InParanoidiP33329.
KOiK06269.
OMAiYSTPLHS.
OrthoDBiEOG79KPQ9.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR011159. PPPtase_PPZ.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFiPIRSF000909. PPPtase_PPZ. 1 hit.
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33329-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNSGSKQHT KHNSKKDDHD GDRKKTLDLP PLTKSDTTHS LKSSRSLRSL
60 70 80 90 100
RSKRSEASLA SNVQAQTQPL SRRSSTLGNG NRNHRRSNNA PITPPNNHYL
110 120 130 140 150
TSHPSSSRRL SSSSRRSSMG NNNNSELPPS MIQMEPKSPI LKNSTSMHST
160 170 180 190 200
SSFNSYENAL TDDDDDRGDD GGESPSMAKV TRINTSSSAD RGSKRTPLRR
210 220 230 240 250
HNSLQPEKGV TGFSSTSSKL RRRSDNTLPA SYPLNAEAGG NGSDYFSNRS
260 270 280 290 300
NSHASSRKSS FGSTGNTAYS TPLHSPALRK MSSRDNDDSG DNVNGRGTSP
310 320 330 340 350
IPNLNIDKPS PSASSASKRE YLSAYPTLAH RDSSSSLSPR GKGQRSSSSS
360 370 380 390 400
SSSQRIYVSP PSPTGDFVHG SCADGDNGSR TNTMVEMKRK KPVRPVDIDE
410 420 430 440 450
IIQRLLDAGY AAKRTKNVCL KNSEIIQICH KARELFLAQP ALLELSPSVK
460 470 480 490 500
IVGDVHGQYA DLLRLFTKCG FPPMANYLFL GDYVDRGKQS LETILLLLCY
510 520 530 540 550
KIKYPENFFL LRGNHECANV TRVYGFYDEC KRRCNIKIWK TFVDTFNTLP
560 570 580 590 600
LAAIVTGKIF CVHGGLSPVL NSMDEIRHVS RPTDVPDFGL INDLLWSDPT
610 620 630 640 650
DSSNEWEDNE RGVSFCYNKV AINKFLNKFG FDLVCRAHMV VEDGYEFFND
660 670 680 690 700
RSLVTVFSAP NYCGEFDNWG AVMTVSEGLL CSFELLDPLD STALKQVMKK
710
GRQERKLANR
Length:710
Mass (Da):78,492
Last modified:January 23, 2007 - v4
Checksum:i3095F37046489AFB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 2311S → T in AAA34899 (PubMed:8395014).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74136 Genomic DNA. Translation: CAA52233.1.
L10241 Genomic DNA. Translation: AAA34899.1.
U33007 Genomic DNA. Translation: AAB64859.1.
BK006938 Genomic DNA. Translation: DAA12273.1.
PIRiS35674.
RefSeqiNP_010724.1. NM_001180744.1.

Genome annotation databases

EnsemblFungiiYDR436W; YDR436W; YDR436W.
GeneIDi852046.
KEGGisce:YDR436W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74136 Genomic DNA. Translation: CAA52233.1.
L10241 Genomic DNA. Translation: AAA34899.1.
U33007 Genomic DNA. Translation: AAB64859.1.
BK006938 Genomic DNA. Translation: DAA12273.1.
PIRiS35674.
RefSeqiNP_010724.1. NM_001180744.1.

3D structure databases

SMRiP33329. Positions 396-688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32492. 51 interactions.
DIPiDIP-6355N.
IntActiP33329. 12 interactions.
MINTiMINT-694847.
STRINGi4932.YDR436W.

Proteomic databases

MaxQBiP33329.
PaxDbiP33329.
PRIDEiP33329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR436W; YDR436W; YDR436W.
GeneIDi852046.
KEGGisce:YDR436W.

Organism-specific databases

SGDiS000002844. PPZ2.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00710000107291.
HOGENOMiHOG000172697.
InParanoidiP33329.
KOiK06269.
OMAiYSTPLHS.
OrthoDBiEOG79KPQ9.

Enzyme and pathway databases

BioCyciYEAST:YDR436W-MONOMER.

Miscellaneous databases

NextBioi970299.

Gene expression databases

GenevestigatoriP33329.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR011159. PPPtase_PPZ.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFiPIRSF000909. PPPtase_PPZ. 1 hit.
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1992) [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(1992) [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.
    , 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 424-645.
  6. 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(2006) [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(2006) [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(2007) [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(2008) [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].

Entry informationi

Entry nameiPPZ2_YEAST
AccessioniPrimary (citable) accession number: P33329
Secondary accession number(s): D6VT63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 149 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 189 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.