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P53043

- PPT1_YEAST

UniProt

P53043 - PPT1_YEAST

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Protein
Serine/threonine-protein phosphatase T
Gene
PPT1, YGR123C, G6347
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

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.

Sites

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

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. protein serine/threonine phosphatase activity Source: SGD
Complete GO annotation...

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 T
PRO_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. 25 interactions.
DIPiDIP-1525N.
IntActiP53043. 10 interactions.
MINTiMINT-406578.
STRINGi4932.YGR123C.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ICFX-ray2.30A/B179-513[»]
ProteinModelPortaliP53043.
SMRiP53043. Positions 11-508.

Miscellaneous databases

EvolutionaryTraceiP53043.

Family & Domainsi

Domains and Repeats

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

Region

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

Domaini

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

Sequence similaritiesi

Contains 3 TPR repeats.

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063173.
HOGENOMiHOG000172698.
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.
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

MSTPTAADRA KALERKNEGN VFVKEKHFLK AIEKYTEAID LDSTQSIYFS    50
NRAFAHFKVD NFQSALNDCD EAIKLDPKNI KAYHRRALSC MALLEFKKAR 100
KDLNVLLKAK PNDPAATKAL LTCDRFIREE RFRKAIGGAE NEAKISLCQT 150
LNLSSFDANA DLANYEGPKL EFEQLYDDKN AFKGAKIKNM SQEFISKMVN 200
DLFLKGKYLP KKYVAAIISH ADTLFRQEPS MVELENNSTP DVKISVCGDT 250
HGQFYDVLNL FRKFGKVGPK HTYLFNGDFV DRGSWSCEVA LLFYCLKILH 300
PNNFFLNRGN HESDNMNKIY GFEDECKYKY SQRIFNMFAQ SFESLPLATL 350
INNDYLVMHG GLPSDPSATL SDFKNIDRFA QPPRDGAFME LLWADPQEAN 400
GMGPSQRGLG HAFGPDITDR FLRNNKLRKI FRSHELRMGG VQFEQKGKLM 450
TVFSAPNYCD SQGNLGGVIH VVPGHGILQA GRNDDQNLII ETFEAVEHPD 500
IKPMAYSNGG FGL 513
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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...

Protein-protein interaction databases

BioGridi 33370. 25 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.
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.
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: June 11, 2014
This is version 139 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.

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

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