P53043 · PPT1_YEAST
- ProteinSerine/threonine-protein phosphatase T
- GenePPT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids513 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82). Dephosphorylation positively regulates the Hsp90 chaperone machinery.
Miscellaneous
Present with 6990 molecules/cell in log phase SD medium.
Catalytic activity
- H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Cofactor
Note: Binds 2 manganese ions per subunit.
Activity regulation
Stimulated by arachidonic acid and other unsaturated fatty acids, and by arachidoyl coenzyme A.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
34 mM | p-nitrophenylphosphate |
pH Dependence
Optimum pH is 7.8.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 249 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 251 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 278 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 278 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 310 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 311 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 359 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 434 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase T
- EC number
- Short namesPPT
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP53043
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 311 | Loss of phosphatase activity. | ||||
Sequence: H → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000058898 | 1-513 | Serine/threonine-protein phosphatase T | |||
Sequence: MSTPTAADRAKALERKNEGNVFVKEKHFLKAIEKYTEAIDLDSTQSIYFSNRAFAHFKVDNFQSALNDCDEAIKLDPKNIKAYHRRALSCMALLEFKKARKDLNVLLKAKPNDPAATKALLTCDRFIREERFRKAIGGAENEAKISLCQTLNLSSFDANADLANYEGPKLEFEQLYDDKNAFKGAKIKNMSQEFISKMVNDLFLKGKYLPKKYVAAIISHADTLFRQEPSMVELENNSTPDVKISVCGDTHGQFYDVLNLFRKFGKVGPKHTYLFNGDFVDRGSWSCEVALLFYCLKILHPNNFFLNRGNHESDNMNKIYGFEDECKYKYSQRIFNMFAQSFESLPLATLINNDYLVMHGGLPSDPSATLSDFKNIDRFAQPPRDGAFMELLWADPQEANGMGPSQRGLGHAFGPDITDRFLRNNKLRKIFRSHELRMGGVQFEQKGKLMTVFSAPNYCDSQGNLGGVIHVVPGHGILQAGRNDDQNLIIETFEAVEHPDIKPMAYSNGGFGL |
Proteomic databases
PTM databases
Expression
Induction
Expression peaks in early log phase and decreases dramatically during the stationary phase (at protein level).
Interaction
Subunit
Interacts (via TPR repeats) with HSP82 (via C-terminal MEEVD pentapeptide).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P53043 | HSC82 P15108 | 3 | EBI-13796, EBI-8666 | |
BINARY | P53043 | HSP82 P02829 | 9 | EBI-13796, EBI-8659 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 12-45 | TPR 1 | ||||
Sequence: ALERKNEGNVFVKEKHFLKAIEKYTEAIDLDSTQ | ||||||
Repeat | 46-79 | TPR 2 | ||||
Sequence: SIYFSNRAFAHFKVDNFQSALNDCDEAIKLDPKN | ||||||
Repeat | 80-113 | TPR 3 | ||||
Sequence: IKAYHRRALSCMALLEFKKARKDLNVLLKAKPND | ||||||
Region | 188-513 | Catalytic | ||||
Sequence: KNMSQEFISKMVNDLFLKGKYLPKKYVAAIISHADTLFRQEPSMVELENNSTPDVKISVCGDTHGQFYDVLNLFRKFGKVGPKHTYLFNGDFVDRGSWSCEVALLFYCLKILHPNNFFLNRGNHESDNMNKIYGFEDECKYKYSQRIFNMFAQSFESLPLATLINNDYLVMHGGLPSDPSATLSDFKNIDRFAQPPRDGAFMELLWADPQEANGMGPSQRGLGHAFGPDITDRFLRNNKLRKIFRSHELRMGGVQFEQKGKLMTVFSAPNYCDSQGNLGGVIHVVPGHGILQAGRNDDQNLIIETFEAVEHPDIKPMAYSNGGFGL |
Domain
The TPR repeats mediate protein-protein interactions with substrate proteins, but also autoinhibit PPT1 phosphatase activity.
Sequence similarities
Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)57,995
- Last updated1996-10-01 v1
- Checksum6966DA22340A5793
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X89417 EMBL· GenBank· DDBJ | CAA61596.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
X83099 EMBL· GenBank· DDBJ | CAA58158.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z72908 EMBL· GenBank· DDBJ | CAA97134.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY558095 EMBL· GenBank· DDBJ | AAS56421.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S39959 EMBL· GenBank· DDBJ | AAB22462.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006941 EMBL· GenBank· DDBJ | DAA08216.1 EMBL· GenBank· DDBJ | Genomic DNA |