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P53043

- PPT1_YEAST

UniProt

P53043 - PPT1_YEAST

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Protein

Serine/threonine-protein phosphatase T

Gene

PPT1

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

Functioni

Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82). Dephosphorylation positively regulates the Hsp90 chaperone machinery.1 Publication

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

Enzyme regulationi

Stimulated by arachidonic acid and other unsaturated fatty acids, and by arachidoyl coenzyme A.1 Publication

Kineticsi

  1. KM=34 mM for p-nitrophenylphosphate1 Publication

pH dependencei

Optimum pH is 7.8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi249 – 2491Manganese 1By similarity
Metal bindingi251 – 2511Manganese 1By similarity
Metal bindingi278 – 2781Manganese 1By similarity
Metal bindingi278 – 2781Manganese 2By similarity
Metal bindingi310 – 3101Manganese 2By similarity
Active sitei311 – 3111Proton donorBy similarity
Metal bindingi359 – 3591Manganese 2By similarity
Metal bindingi434 – 4341Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: SGD

GO - Biological processi

  1. protein dephosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30830-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase T (EC:3.1.3.16)
Short name:
PPT
Gene namesi
Name:PPT1
Ordered Locus Names:YGR123C
ORF Names:G6347
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR123c.
SGDiS000003355. PPT1.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi311 – 3111H → A: Loss of phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Serine/threonine-protein phosphatase TPRO_0000058898Add
BLAST

Proteomic databases

MaxQBiP53043.
PaxDbiP53043.
PeptideAtlasiP53043.

Expressioni

Inductioni

Expression peaks in early log phase and decreases dramatically during the stationary phase (at protein level).1 Publication

Gene expression databases

GenevestigatoriP53043.

Interactioni

Subunit structurei

Interacts (via TPR repeats) with HSP82 (via C-terminal MEEVD pentapeptide).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HSC82P151083EBI-13796,EBI-8666
HSP82P028298EBI-13796,EBI-8659

Protein-protein interaction databases

BioGridi33370. 30 interactions.
DIPiDIP-1525N.
IntActiP53043. 10 interactions.
MINTiMINT-406578.
STRINGi4932.YGR123C.

Structurei

Secondary structure

1
513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi192 – 20110Combined sources
Helixi203 – 2053Combined sources
Helixi211 – 22616Combined sources
Beta strandi230 – 2345Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi243 – 2475Combined sources
Helixi254 – 26411Combined sources
Beta strandi271 – 2755Combined sources
Beta strandi280 – 2834Combined sources
Helixi286 – 29914Combined sources
Turni301 – 3033Combined sources
Beta strandi304 – 3063Combined sources
Helixi314 – 3207Combined sources
Helixi322 – 3298Combined sources
Helixi332 – 34211Combined sources
Beta strandi347 – 3515Combined sources
Turni352 – 3543Combined sources
Beta strandi355 – 3573Combined sources
Helixi370 – 3745Combined sources
Beta strandi384 – 3863Combined sources
Helixi387 – 3937Combined sources
Beta strandi398 – 4047Combined sources
Beta strandi411 – 4133Combined sources
Helixi415 – 42410Combined sources
Beta strandi428 – 4325Combined sources
Beta strandi439 – 4446Combined sources
Helixi445 – 4473Combined sources
Beta strandi449 – 4524Combined sources
Helixi458 – 4603Combined sources
Beta strandi465 – 4717Combined sources
Turni480 – 4823Combined sources
Beta strandi488 – 4936Combined sources
Turni503 – 5064Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ICFX-ray2.30A/B179-513[»]
ProteinModelPortaliP53043.
SMRiP53043. Positions 11-508.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati12 – 4534TPR 1Add
BLAST
Repeati46 – 7934TPR 2Add
BLAST
Repeati80 – 11334TPR 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 513326CatalyticAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063173.
HOGENOMiHOG000172698.
InParanoidiP53043.
KOiK04460.
OMAiFKLLYPN.
OrthoDBiEOG7Z3FDD.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR013235. PPP_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR011236. Ser/Thr_PPase_5.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11668:SF12. PTHR11668:SF12. 1 hit.
PfamiPF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
PF00515. TPR_1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PIRSFiPIRSF033096. PPPtase_5. 1 hit.
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53043-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTPTAADRA KALERKNEGN VFVKEKHFLK AIEKYTEAID LDSTQSIYFS
60 70 80 90 100
NRAFAHFKVD NFQSALNDCD EAIKLDPKNI KAYHRRALSC MALLEFKKAR
110 120 130 140 150
KDLNVLLKAK PNDPAATKAL LTCDRFIREE RFRKAIGGAE NEAKISLCQT
160 170 180 190 200
LNLSSFDANA DLANYEGPKL EFEQLYDDKN AFKGAKIKNM SQEFISKMVN
210 220 230 240 250
DLFLKGKYLP KKYVAAIISH ADTLFRQEPS MVELENNSTP DVKISVCGDT
260 270 280 290 300
HGQFYDVLNL FRKFGKVGPK HTYLFNGDFV DRGSWSCEVA LLFYCLKILH
310 320 330 340 350
PNNFFLNRGN HESDNMNKIY GFEDECKYKY SQRIFNMFAQ SFESLPLATL
360 370 380 390 400
INNDYLVMHG GLPSDPSATL SDFKNIDRFA QPPRDGAFME LLWADPQEAN
410 420 430 440 450
GMGPSQRGLG HAFGPDITDR FLRNNKLRKI FRSHELRMGG VQFEQKGKLM
460 470 480 490 500
TVFSAPNYCD SQGNLGGVIH VVPGHGILQA GRNDDQNLII ETFEAVEHPD
510
IKPMAYSNGG FGL
Length:513
Mass (Da):57,995
Last modified:October 1, 1996 - v1
Checksum:i6966DA22340A5793
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS52571.
RefSeqiNP_011639.3. NM_001181252.3.

Genome annotation databases

EnsemblFungiiYGR123C; YGR123C; YGR123C.
GeneIDi853023.
KEGGisce:YGR123C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi S52571.
RefSeqi NP_011639.3. NM_001181252.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ICF X-ray 2.30 A/B 179-513 [» ]
ProteinModelPortali P53043.
SMRi P53043. Positions 11-508.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33370. 30 interactions.
DIPi DIP-1525N.
IntActi P53043. 10 interactions.
MINTi MINT-406578.
STRINGi 4932.YGR123C.

Proteomic databases

MaxQBi P53043.
PaxDbi P53043.
PeptideAtlasi P53043.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR123C ; YGR123C ; YGR123C .
GeneIDi 853023.
KEGGi sce:YGR123C.

Organism-specific databases

CYGDi YGR123c.
SGDi S000003355. PPT1.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000063173.
HOGENOMi HOG000172698.
InParanoidi P53043.
KOi K04460.
OMAi FKLLYPN.
OrthoDBi EOG7Z3FDD.

Enzyme and pathway databases

BioCyci YEAST:G3O-30830-MONOMER.

Miscellaneous databases

EvolutionaryTracei P53043.
NextBioi 972897.
PROi P53043.

Gene expression databases

Genevestigatori P53043.

Family and domain databases

Gene3Di 1.25.40.10. 1 hit.
3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR013235. PPP_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR011236. Ser/Thr_PPase_5.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view ]
PANTHERi PTHR11668:SF12. PTHR11668:SF12. 1 hit.
Pfami PF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
PF00515. TPR_1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF033096. PPPtase_5. 1 hit.
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. 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.
  12. "Structure of protein serine/threonine phosphatase from Saccharomyces cerevisiae with similarity to human phosphatase PP5."
    Midwest center for structural genomics (MCSG)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 179-513.

Entry informationi

Entry nameiPPT1_YEAST
AccessioniPrimary (citable) accession number: P53043
Secondary accession number(s): D6VUQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6990 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3