Function and Biology Details
Reaction catalysed:
(1a) [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [RBR-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine
Biochemical function:
Biological process:
- not assigned
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
E3 ubiquitin-protein ligase RNF31 and Sharpin (preferred)
PDBe Complex ID:
PDB-CPX-188463 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase RNF31
Molecule details ›
Chains: A, C, E, G
Length: 166 amino acids
Theoretical weight: 18.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: HOIP UBA domain pair
Length: 166 amino acids
Theoretical weight: 18.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q96EP0 (Residues: 480-639; Coverage: 15%)
Sequence domains: HOIP UBA domain pair
Sharpin
Molecule details ›
Chains: B, D, F, H
Length: 108 amino acids
Theoretical weight: 11.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 108 amino acids
Theoretical weight: 11.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q9H0F6 (Residues: 206-309; Coverage: 27%)
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
