Function and Biology Details
Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Leucine-rich repeat
- Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
- Leucine-rich repeat, typical subtype
- Leucine-rich repeat domain superfamily
- Metallo-dependent phosphatase-like
- U2A'/phosphoprotein 32 family A, C-terminal
- Calcineurin-like phosphoesterase domain, ApaH type
- Serine-threonine protein phosphatase, N-terminal
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158558 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Molecule details ›
Chain: A
Length: 305 amino acids
Theoretical weight: 34.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 305 amino acids
Theoretical weight: 34.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P62136 (Residues: 1-300; Coverage: 91%)
Sequence domains:
Protein phosphatase 1 regulatory subunit 7
Molecule details ›
Chain: C
Length: 310 amino acids
Theoretical weight: 36.09 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
Sequence domains:
Length: 310 amino acids
Theoretical weight: 36.09 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
- Canonical: Q15435 (Residues: 56-360; Coverage: 85%)
Sequence domains:
