Function and Biology

E3 ligase Cbl-b in complex with a triazolone core inhibitor (compound 1)

Source organism: Homo sapiens
Biochemical function: metal ion binding
Biological process: regulation of signaling
Cellular component: not assigned

EC 2.3.2.27: RING-type E3 ubiquitin transferase

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
Systematic name:
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein]-L-lysine ubiquitin transferase (isopeptide bond-forming; RING-type)
Alternative Name(s):
  • RING E3 ligase
  • Ubiquitin transferase RING E3

Sequence families

Pfam Protein families (Pfam)
PF00097
Domain description: Zinc finger, C3HC4 type (RING finger)
Occurring in:
  1. E3 ubiquitin-protein ligase CBL-B
The deposited structure of PDB entry 9fqh contains 1 copy of Pfam domain PF00097 (Zinc finger, C3HC4 type (RING finger)) in E3 ubiquitin-protein ligase CBL-B. Showing 1 copy in chain A.

PF02762
Domain description: CBL proto-oncogene N-terminus, SH2-like domain
Occurring in:
  1. E3 ubiquitin-protein ligase CBL-B
The deposited structure of PDB entry 9fqh contains 1 copy of Pfam domain PF02762 (CBL proto-oncogene N-terminus, SH2-like domain) in E3 ubiquitin-protein ligase CBL-B. Showing 1 copy in chain A.

PF02761
Domain description: CBL proto-oncogene N-terminus, EF hand-like domain
Occurring in:
  1. E3 ubiquitin-protein ligase CBL-B
The deposited structure of PDB entry 9fqh contains 1 copy of Pfam domain PF02761 (CBL proto-oncogene N-terminus, EF hand-like domain) in E3 ubiquitin-protein ligase CBL-B. Showing 1 copy in chain A.

PF02262
Domain description: CBL proto-oncogene N-terminal domain 1
Occurring in:
  1. E3 ubiquitin-protein ligase CBL-B
The deposited structure of PDB entry 9fqh contains 1 copy of Pfam domain PF02262 (CBL proto-oncogene N-terminal domain 1) in E3 ubiquitin-protein ligase CBL-B. Showing 1 copy in chain A.