P48726 · PP2A1_PARTE
- ProteinSerine/threonine-protein phosphatase PP2A catalytic subunit 1
- GenePpn1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids315 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
Cofactor
Note: Binds 2 manganese ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 62 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 64 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 90 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 90 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 122 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 123 | Proton donor | |||
Binding site | 172 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 247 | Mn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity | |
Biological Process | mitotic cell cycle |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase PP2A catalytic subunit 1
- EC number
- Short namesPPN 1
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Sar > Alveolata > Ciliophora > Intramacronucleata > Oligohymenophorea > Peniculida > Parameciidae > Paramecium
Accessions
- Primary accessionP48726
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000058867 | 1-315 | Serine/threonine-protein phosphatase PP2A catalytic subunit 1 | ||
Modified residue | 315 | Leucine methyl ester | |||
Post-translational modification
Reversibly methyl esterified on Leu-315 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length315
- Mass (Da)36,134
- Last updated2007-10-23 v2
- Checksum2C67AB335B8C4650
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 34 | in Ref. 1; AAA68611 | |||
Sequence conflict | 47-49 | in Ref. 1; AAA68611 | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U27497 EMBL· GenBank· DDBJ | AAA68611.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CT868096 EMBL· GenBank· DDBJ | CAK71296.1 EMBL· GenBank· DDBJ | Genomic DNA |