Function and Biology Details
Reactions catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Protein-tyrosine phosphatase-like
- Serine/threonine-protein kinase, active site
- Protein kinase, ATP binding site
- Protein kinase domain
- Protein kinase-like domain superfamily
- Tyrosine-specific protein phosphatases domain
- Protein-tyrosine phosphatase, catalytic
- Dual specificity protein phosphatase domain
2 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150323 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cyclin-dependent kinase inhibitor 3
Molecule details ›
Chain: A
Length: 212 amino acids
Theoretical weight: 23.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Cyclin-dependent kinase inhibitor 3 (CDKN3)
Structure domains: Protein tyrosine phosphatase superfamily
Length: 212 amino acids
Theoretical weight: 23.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q16667 (Residues: 1-212; Coverage: 100%)
Sequence domains: Cyclin-dependent kinase inhibitor 3 (CDKN3)
Structure domains: Protein tyrosine phosphatase superfamily
Cyclin-dependent kinase 2
Molecule details ›
Chain: B
Length: 298 amino acids
Theoretical weight: 34.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein kinase domain
Structure domains:
Length: 298 amino acids
Theoretical weight: 34.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P24941 (Residues: 1-298; Coverage: 100%)
Sequence domains: Protein kinase domain
Structure domains:
