Ariadne Homolog 2 (ARIH2)

Zinc-binding cysteine and histidine residues that form a 3-dimensional structure, stabilized by zinc, are found in protein-interacting motifs in LIM , RING, or LAP finger-containing proteins. TRIAD1, a 493-amino acid nuclear protein upregulated during retinoic acid-induced granulocytic differentiation of acute promyelocytic leukemia cells. ARIH2 contains 2 RING fingers flanking a conserved cysteine-rich (C6HC) domain the authors designated DRIL (double RING finger-linked domain); 2 C-terminal coiled-coil domains; and an acidic N-terminal region. The DRIL domain with its 2 flanking RING fingers, collectively referred to by the authors as the TRIAD (2 RING fingers and DRIL) domain, spans approximately 200 amino acids and was identified, with a preserved order and distance, in more than 20 eukaryotic proteins.