Function and Biology Details
Reaction catalysed:
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Proteasome complex (preferred)
PDBe Complex ID:
PDB-CPX-155094 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
26S proteasome regulatory subunit RPN8
Molecule details ›
Chain: A
Length: 338 amino acids
Theoretical weight: 38.37 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Cytidine Deaminase, domain 2
Length: 338 amino acids
Theoretical weight: 38.37 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical:
Q08723 (Residues: 1-338; Coverage: 100%)
Sequence domains:
Structure domains: Cytidine Deaminase, domain 2
Ubiquitin carboxyl-terminal hydrolase RPN11
Molecule details ›
Chain: B
Length: 222 amino acids
Theoretical weight: 24.88 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: JAB1/Mov34/MPN/PAD-1 ubiquitin protease
Length: 222 amino acids
Theoretical weight: 24.88 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical: P43588 (Residues: 1-222; Coverage: 73%)
Sequence domains: JAB1/Mov34/MPN/PAD-1 ubiquitin protease
