Aliases for RING1 Gene
External Ids for RING1 Gene
Previous GeneCards Identifiers for RING1 Gene
This gene belongs to the RING finger family, members of which encode proteins characterized by a RING domain, a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is associated with the multimeric polycomb group protein complex. The gene product interacts with the polycomb group proteins BMI1, EDR1, and CBX4, and colocalizes with these proteins in large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is contiguous with the RING finger genes FABGL and HKE4. [provided by RefSeq, Jul 2008]
GeneCards Summary for RING1 Gene
RING1 (Ring Finger Protein 1) is a Protein Coding gene. Diseases associated with RING1 include Granulomatosis With Polyangiitis and Juvenile-Onset Parkinson's Disease. Among its related pathways are Notch Signaling Pathway (WikiPathways) and SUMOylation. Gene Ontology (GO) annotations related to this gene include chromatin binding and ubiquitin-protein transferase activity. An important paralog of this gene is RNF2.
UniProtKB/Swiss-Prot Summary for RING1 Gene
Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity.