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:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Zinc finger, RING-type
- E3 ubiquitin-protein ligase CBL-B, RING finger, HC subclass
- SH2 domain superfamily
- Adaptor protein Cbl, SH2-like domain
- Adaptor protein Cbl, N-terminal domain superfamily
- Zinc finger, RING-type, conserved site
- Zinc finger, RING/FYVE/PHD-type
- Adaptor protein Cbl, EF hand-like
4 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
E3 ubiquitin-protein ligase CBL-B (preferred)
PDBe Complex ID:
PDB-CPX-171596 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase CBL-B
Molecule details ›
Chains: A, B, C
Length: 394 amino acids
Theoretical weight: 45.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 394 amino acids
Theoretical weight: 45.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q13191 (Residues: 39-426; Coverage: 40%)
Sequence domains:
- CBL proto-oncogene N-terminal domain 1
- CBL proto-oncogene N-terminus, EF hand-like domain
- CBL proto-oncogene N-terminus, SH2-like domain
- Zinc finger, C3HC4 type (RING finger)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU MICROMAX-007
Spacegroup:
P31
Expression system: Escherichia coli
