Anti-ARIH2

TRIAD1, also known as ARIH2 (ariadne homolog 2) or ARI2, is a 493 amino acid protein that contains one IBR-type zinc finger and two RING-type zinc fingers and belongs to the ariadne subfamily of RBR proteins. Localized to the nucleus, TRIAD1 interacts with UBE2L3 and is thought to act as an E3 ubiquitin-protein ligase, functioning to accept ubiquitin from E2 ubiquitin-conjugating enzymes and transfer the acquired ubiquitin residue to target substrates. TRIAD1 is subject to post-translational DNA damage-dependent phosphorylation, probably by ATM or ATR. The gene encoding TRIAD1 maps to human chromosome 3, which houses over 1,100 genes, including a chemokine receptor (CKR) gene cluster and a variety of human cancer-related gene loci. Protein function: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3 (PubMed:16118314, PubMed:17646546, PubMed:19340006, PubMed:24076655). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets. The initial ubiquitin is then elongated. E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex (PubMed:24076655). Mediates 'Lys-6', 'Lys-48'-and 'Lys- 63'-linked polyubiquitination (PubMed:16118314, PubMed:17646546, PubMed:19340006). May play a role in myelopoiesis (PubMed:19340006). [The UniProt Consortium]