Function and Biology Details
Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
- not assigned
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185384 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase RING2
Molecule details ›
Chains: A, C, E, G, I, K
Length: 111 amino acids
Theoretical weight: 12.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: RAWUL domain RING finger- and WD40-associated ubiquitin-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 111 amino acids
Theoretical weight: 12.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q99496 (Residues: 223-333; Coverage: 33%)
Sequence domains: RAWUL domain RING finger- and WD40-associated ubiquitin-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
RING1 and YY1-binding protein
Molecule details ›
Chains: B, D, F, H, J, L
Length: 37 amino acids
Theoretical weight: 4.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Yaf2/RYBP C-terminal binding motif
Length: 37 amino acids
Theoretical weight: 4.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q8N488 (Residues: 145-179; Coverage: 15%)
Sequence domains: Yaf2/RYBP C-terminal binding motif
