Function and Biology Details
Reaction catalysed:
(1) O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- HEAT, type 2
- Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
- HEAT repeat
- Metallo-dependent phosphatase-like
- Calcineurin-like, phosphoesterase domain
- Serine/Threonine protein phosphatase PP2A-like
- Phosphatase PP2A regulatory subunit A/Splicing factor 3B subunit 1-like, HEAT repeat
- Armadillo-type fold
2 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151655 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Molecule details ›
Chain: A
Length: 589 amino acids
Theoretical weight: 65.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: HEAT repeat
Structure domains: Leucine-rich Repeat Variant
Length: 589 amino acids
Theoretical weight: 65.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P30153 (Residues: 1-589; Coverage: 100%)
Sequence domains: HEAT repeat
Structure domains: Leucine-rich Repeat Variant
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Molecule details ›
Chain: C
Length: 309 amino acids
Theoretical weight: 35.64 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 309 amino acids
Theoretical weight: 35.64 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
- Canonical: P67775 (Residues: 1-309; Coverage: 100%)
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2
