RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in really interesting new gene proteins RING1, RING2 and similar proteins
RING1, also termed polycomb complex protein RING1, or RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), has been identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also termed huntingtin-interacting protein 2-interacting protein 3, or HIP2-interacting protein 3, or protein DinG, or RING finger protein 1B (RING1B), or RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both, RING1 and RING2, are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members in this family contain a C3HC4-type RING-HC finger, and a RAWUL domain.
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