Function and Biology Details
Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Cyclic nucleotide-binding domain
- DnaJ domain
- Cyclic nucleotide-binding, conserved site
- Cyclic nucleotide-binding domain superfamily
- RmlC-like jelly roll fold
- cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain
- Chaperone J-domain superfamily
- cAMP-dependent protein kinase regulatory subunit
7 more domains
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
cAMP-dependent protein kinase (preferred)
PDBe Complex ID:
PDB-CPX-146156 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DnaJ homolog subfamily B member 1; cAMP-dependent protein kinase catalytic subunit alpha
Molecule details ›
Chains: A, B
Length: 405 amino acids
Theoretical weight: 47.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 405 amino acids
Theoretical weight: 47.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P25685 (Residues: 2-70; Coverage: 20%) - Canonical: P17612 (Residues: 16-351; Coverage: 96%)
Sequence domains:
cAMP-dependent protein kinase type II-beta regulatory subunit
Molecule details ›
Chains: C, D
Length: 416 amino acids
Theoretical weight: 46.18 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 416 amino acids
Theoretical weight: 46.18 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
- Canonical: P12369 (Residues: 1-416; Coverage: 100%)
Sequence domains:
