Aliases for RNF20 Gene
External Ids for RNF20 Gene
Previous GeneCards Identifiers for RNF20 Gene
The protein encoded by this gene shares similarity with BRE1 of S. cerevisiae. The protein encoded by this human gene is an E3 ubiquitin ligase that regulates chromosome structure by monoubiquitinating histone H2B. This protein acts as a putative tumor suppressor and positively regulates the p53 tumor suppressor as well as numerous histone H2A and H2B genes. In contrast, this protein also suppresses the expression of several protooncogenes and growth-related genes, including many genes that are induced by epidermal growth factor. This gene selectively suppresses the expression of some genes by interfering with chromatin recruitment of transcription elongation factor SII (TFIIS). [provided by RefSeq, Feb 2012]
GeneCards Summary for RNF20 Gene
RNF20 (Ring Finger Protein 20, E3 Ubiquitin Protein Ligase) is a Protein Coding gene. Among its related pathways are Chromatin Regulation / Acetylation. GO annotations related to this gene include transcription factor activity, sequence-specific DNA binding and ligase activity. An important paralog of this gene is RNF40.
UniProtKB/Swiss-Prot for RNF20 Gene
Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of Lys-120 of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 Lys-4 and Lys-79 methylation (H3K4me and H3K79me, respectively). It thereby plays a central role inb histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of isoform 2 of PA2G4 in cancer cells leading to its proteasome-mediated degradation.