P48726 · PP2A1_PARTE

  • Protein
    Serine/threonine-protein phosphatase PP2A catalytic subunit 1
  • Gene
    Ppn1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 manganese ions per subunit.

Features

Showing features for binding site, active site.

131520406080100120140160180200220240260280300
Type
IDPosition(s)Description
Binding site62Mn2+ 1 (UniProtKB | ChEBI)
Binding site64Mn2+ 1 (UniProtKB | ChEBI)
Binding site90Mn2+ 1 (UniProtKB | ChEBI)
Binding site90Mn2+ 2 (UniProtKB | ChEBI)
Binding site122Mn2+ 2 (UniProtKB | ChEBI)
Active site123Proton donor
Binding site172Mn2+ 2 (UniProtKB | ChEBI)
Binding site247Mn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionmyosin phosphatase activity
Molecular Functionprotein serine/threonine phosphatase activity
Biological Processmitotic cell cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein phosphatase PP2A catalytic subunit 1
  • EC number
  • Short names
    PPN 1

Gene names

    • Name
      Ppn1
    • ORF names
      GSPATT00001010001

Organism names

  • Taxonomic identifier
  • Strains
    • Stock 51
    • Stock d4-2
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Ciliophora > Intramacronucleata > Oligohymenophorea > Peniculida > Parameciidae > Paramecium

Accessions

  • Primary accession
    P48726
  • Secondary accessions
    • A0CKH9

Proteomes

    • Identifier
    • Component
      Partially assembled WGS sequence

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00000588671-315Serine/threonine-protein phosphatase PP2A catalytic subunit 1
Modified residue315Leucine 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

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region294-315Disordered

Sequence similarities

Belongs to the PPP phosphatase family. PP-2A subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    315
  • Mass (Da)
    36,134
  • Last updated
    2007-10-23 v2
  • Checksum
    2C67AB335B8C4650
MASLNKLSSNEIGNIDRQIAKLKQGQILSEQEVKSLCIKAKEILQDEPNIIQVRAPLTICGDIHGQFHDLIELFQIGGNLPDTNYLFLGDYVDRGSQSVETFSLMLSLKVRYKDRIVLLRGNHENREINKIYGFYDECFRKYGNEIVWKQFTEVFGYLPLSAIVEQQIFCAHGGLSPAMESVDQIKQLNRVQDIPHEGLMCDLLWSDPEETKNGWGISPRGAGWTWGCDITEKFLHSNKLKQIARAHQLVMEGIQKVHNQKTITIFSAPNYCYRCGNQACIVEVDEQLKMNQTQFEPAPRENEPHTTRRVPDYFL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict34in Ref. 1; AAA68611
Sequence conflict47-49in Ref. 1; AAA68611

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U27497
EMBL· GenBank· DDBJ
AAA68611.1
EMBL· GenBank· DDBJ
Genomic DNA
CT868096
EMBL· GenBank· DDBJ
CAK71296.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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