E3 ubiquitin ligase RBR family
IPR031127
Definition
This family of E3 ligases has a distinctive organisation of RING fingers called 'RING-betweenRING-RING' (RBR), characterised by two RING fingers with a cysteine-rich region called the 'in-between-RING' domain that separates them [[cite:PMID:15152079], [cite:PMID:19526189]]. The domains in the RBR E3 ligases have been further named as RING1-BRcat-Rcat according to their structure and function: the C-terminal Rcat (required-for-catalysis) domain is essential for catalytic activity, whereas the central BRcat (benign-catalytic) domain adopts the same fold as the Rcat, but lacks a catalytic cysteine residue and ubiquitination activity PMID:24576094. These ligases have a unique mechanism of elongating ubiquitin chains that distinguishes them from other E3 ligases [[cite:PMID:21532592], [cite:PMID:24469331]]. On the basis of sequence conservation within the RBR segment, RBR proteins are assigned to 15 subfamilies (A-I, P, S, T, U, X, Z). There are two RBR proteins in the yeast Saccharomyces cerevisiae, six in Drosophila melanogaster, 10 in Caenorhabditis elegans, about 40 in Arabidopsis thaliana, around 23 in the zebrafish (Danio rerio), and about 15 in humans PMID:17367545.
9 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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