Function and Biology Details
Reactions catalysed:
ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- SH2 domain
- Phosphatidylinositol 3-/4-kinase, catalytic domain
- Phosphoinositide 3-kinase, accessory (PIK) domain
- C2 phosphatidylinositol 3-kinase-type domain
- Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain
- Phosphatidylinositol 3-kinase, adaptor-binding domain
- SH2 domain superfamily
- Phosphatidylinositol 3/4-kinase, conserved site
11 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151133 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
Molecule details ›
Chain: A
Length: 1096 amino acids
Theoretical weight: 128.06 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains:
Length: 1096 amino acids
Theoretical weight: 128.06 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
- Canonical:
P42336 (Residues: 1-1068; Coverage: 100%)
Sequence domains:
Phosphatidylinositol 3-kinase regulatory subunit alpha
Molecule details ›
Chain: B
Length: 279 amino acids
Theoretical weight: 33.67 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains:
Structure domains: Helix Hairpins
Length: 279 amino acids
Theoretical weight: 33.67 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
- Canonical: P27986 (Residues: 322-600; Coverage: 39%)
Sequence domains:
Structure domains: Helix Hairpins
