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P53043 (PPT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 T

Short name=PPT
EC=3.1.3.16
Gene names
Name:PPT1
Ordered Locus Names:YGR123C
ORF Names:G6347
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82). Dephosphorylation positively regulates the Hsp90 chaperone machinery. Ref.10

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Enzyme regulation

Stimulated by arachidonic acid and other unsaturated fatty acids, and by arachidoyl coenzyme A. Ref.7

Subunit structure

Interacts (via TPR repeats) with HSP82 (via C-terminal MEEVD pentapeptide). Ref.10

Subcellular location

Nucleus Ref.7 Ref.8.

Induction

Expression peaks in early log phase and decreases dramatically during the stationary phase (at protein level). Ref.7

Domain

The TPR repeats mediate protein-protein interactions with substrate proteins, but also autoinhibit PPT1 phosphatase activity.

Miscellaneous

Present with 6990 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.

Contains 3 TPR repeats.

Biophysicochemical properties

Kinetic parameters:

KM=34 mM for p-nitrophenylphosphate Ref.11

pH dependence:

Optimum pH is 7.8.

Sequence caution

The sequence CAA61596.1 differs from that shown. Reason: Frameshift at position 381.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSC82P151083EBI-13796,EBI-8666
HSP82P028298EBI-13796,EBI-8659

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513Serine/threonine-protein phosphatase T
PRO_0000058898

Regions

Repeat12 – 4534TPR 1
Repeat46 – 7934TPR 2
Repeat80 – 11334TPR 3
Region188 – 513326Catalytic

Sites

Active site3111Proton donor By similarity
Metal binding2491Iron By similarity
Metal binding2511Iron By similarity
Metal binding2781Iron By similarity
Metal binding2781Manganese By similarity
Metal binding3101Manganese By similarity
Metal binding3591Manganese By similarity
Metal binding4341Manganese By similarity

Experimental info

Mutagenesis3111H → A: Loss of phosphatase activity. Ref.10

Secondary structure

.............................................................. 513
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53043 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 6966DA22340A5793

FASTA51357,995
        10         20         30         40         50         60 
MSTPTAADRA KALERKNEGN VFVKEKHFLK AIEKYTEAID LDSTQSIYFS NRAFAHFKVD 

        70         80         90        100        110        120 
NFQSALNDCD EAIKLDPKNI KAYHRRALSC MALLEFKKAR KDLNVLLKAK PNDPAATKAL 

       130        140        150        160        170        180 
LTCDRFIREE RFRKAIGGAE NEAKISLCQT LNLSSFDANA DLANYEGPKL EFEQLYDDKN 

       190        200        210        220        230        240 
AFKGAKIKNM SQEFISKMVN DLFLKGKYLP KKYVAAIISH ADTLFRQEPS MVELENNSTP 

       250        260        270        280        290        300 
DVKISVCGDT HGQFYDVLNL FRKFGKVGPK HTYLFNGDFV DRGSWSCEVA LLFYCLKILH 

       310        320        330        340        350        360 
PNNFFLNRGN HESDNMNKIY GFEDECKYKY SQRIFNMFAQ SFESLPLATL INNDYLVMHG 

       370        380        390        400        410        420 
GLPSDPSATL SDFKNIDRFA QPPRDGAFME LLWADPQEAN GMGPSQRGLG HAFGPDITDR 

       430        440        450        460        470        480 
FLRNNKLRKI FRSHELRMGG VQFEQKGKLM TVFSAPNYCD SQGNLGGVIH VVPGHGILQA 

       490        500        510 
GRNDDQNLII ETFEAVEHPD IKPMAYSNGG FGL 

« Hide

References

« Hide 'large scale' references
[1]"A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus."
Chen M.X., McPartlin A.E., Brown L., Chen Y.H., Barker H.M., Cohen P.T.W.
EMBO J. 13:4278-4290(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown open reading frames, the gene for an Asn synthase, remnants of Ty and three tRNA genes."
van Dyck L., Tettelin H., Purnelle B., Goffeau A.
Yeast 13:171-176(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Polymerase chain reactions using Saccharomyces, Drosophila and human DNA predict a large family of protein serine/threonine phosphatases."
Chen M.X., Chen Y.H., Cohen P.T.W.
FEBS Lett. 306:54-58(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-277.
[7]"Characterization of Saccharomyces cerevisiae protein Ser/Thr phosphatase T1 and comparison to its mammalian homolog PP5."
Jeong J.-Y., Johns J., Sinclair C., Park J.-M., Rossie S.
BMC Cell Biol. 4:3-3(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, ENZYME REGULATION, SUBCELLULAR LOCATION, INDUCTION.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"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].
[10]"The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90."
Wandinger S.K., Suhre M.H., Wegele H., Buchner J.
EMBO J. 25:367-376(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HSP82, MUTAGENESIS OF HIS-311.
[11]"Expression, purification and refolding of the phosphatase domain of protein phosphatase 1 (Ppt1) from Saccharomyces cerevisiae."
Suhre M.H., Wegele H., Wandinger S.K.
Int. J. Biol. Macromol. 39:23-28(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89417 Genomic DNA. Translation: CAA61596.1. Frameshift.
X83099 Genomic DNA. Translation: CAA58158.1.
Z72908 Genomic DNA. Translation: CAA97134.1.
AY558095 Genomic DNA. Translation: AAS56421.1.
S39959 Genomic DNA. Translation: AAB22462.1.
BK006941 Genomic DNA. Translation: DAA08216.1.
PIRS52571.
RefSeqNP_011639.3. NM_001181252.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ICFX-ray2.30A/B179-513[»]
ProteinModelPortalP53043.
SMRP53043. Positions 11-508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33370. 25 interactions.
DIPDIP-1525N.
IntActP53043. 10 interactions.
MINTMINT-406578.
STRING4932.YGR123C.

Proteomic databases

PaxDbP53043.
PeptideAtlasP53043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR123C; YGR123C; YGR123C.
GeneID853023.
KEGGsce:YGR123C.

Organism-specific databases

CYGDYGR123c.
SGDS000003355. PPT1.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000063173.
HOGENOMHOG000172698.
KOK04460.
OMAFKLLYPN.
OrthoDBEOG7Z3FDD.

Enzyme and pathway databases

BioCycYEAST:G3O-30830-MONOMER.

Gene expression databases

GenevestigatorP53043.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR013235. PPP_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR011236. Ser/Thr_PPase_5.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR11668:SF12. PTHR11668:SF12. 1 hit.
PfamPF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
PF00515. TPR_1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PIRSFPIRSF033096. PPPtase_5. 1 hit.
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53043.
NextBio972897.
PROP53043.

Entry information

Entry namePPT1_YEAST
AccessionPrimary (citable) accession number: P53043
Secondary accession number(s): D6VUQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references