Function and Biology

Solution Structure of the C-terminal RING from a RING-IBR-RING (TRIAD) motif

Source organism: Homo sapiens
Biochemical function: zinc ion binding
Biological process: protein ubiquitination
Cellular component: not assigned

EC 2.3.2.31: RBR-type E3 ubiquitin transferase

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
Systematic name:
S-ubiquitinyl-[ubiquitin-conjugating E2 enzyme]-L-cysteine:acceptor protein ubiquitin transferase (isopeptide bond-forming; RBR-type)

GO terms

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Sequence family

InterPro InterPro annotations
IPR031127
Domain description: E3 ubiquitin ligase RBR family
Occurring in:
  1. E3 ubiquitin-protein ligase ARIH1
IPR002867
Domain description: IBR domain
Occurring in:
  1. E3 ubiquitin-protein ligase ARIH1
IPR044066
Domain description: TRIAD supradomain
Occurring in:
  1. E3 ubiquitin-protein ligase ARIH1

Structure domain

SCOP SCOP annotation
57851
Class: Small proteins
Fold: RING/U-box
Superfamily: RING/U-box
Occurring in:
  1. E3 ubiquitin-protein ligase ARIH1
The deposited structure of PDB entry 1wd2 contains 1 copy of SCOP domain 57851 (RING finger domain, C3HC4) in E3 ubiquitin-protein ligase ARIH1. Showing 1 copy in chain A.