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The protein encoded by RNF20 shares similarity with BRE1 of S. Additionally we are shipping RNF20 Antibodies (66) and many more products for this protein.
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RNF20 plays a critical role in the regulation of hepatic lipid metabolism by modulating the protein stability and transcriptional activity of SREBP1c (show SREBF1 Proteins) during hormonal changes.
results suggested that RNF20 may play roles in adipocyte differentiation by stimulating ubiquitin-proteasome-dependent degradation of AP-2alpha (show TFAP2A Proteins).
Bre1a-negative cells in the ventricular zone of early embryonic brains remain undifferentiated and are selected as self-renewing neural stem cells
model whereby cotranscriptional recruitment of Rnf20 at MLL (show MLL Proteins)-fusion target genes leads to amplification of Dot1l (show DOT1L Proteins)-mediated H3K79 methylation, thereby rendering leukemia cells dependent on Rnf20 to maintain their oncogenic transcriptional program
Loss of Bre1 (RNF20) disrupts gene silencing at telomeric chromatin. Most of the genomic instability in the Bre1-deficient cells is attributed to the formation of R-loops.
We show that Bre1 (human BRE1A/B (RNF20/40) and mouse Bre1a/b (Rnf20/40)) acts as an important suppressor of chromosomal instability
the observed defects in the radiation response of Bre1a/b-deficient cells
It was observed that RE-IIBP induces MEIS1 (show MEIS1 Proteins)-mediated apoptosis, which was dependent on H2BK120 ubiquitination by RNF20.
A primary role for FACT in RNF20 recruitment chromatin remodeling for initiation of homologous recombination repair.
Together, these results indicate that human adenovirus E1A (show BCKDHA Proteins) uses hBre1 to recruit the hPaf1 (show PAF1 Proteins) complex in order to optimally activate viral early transcription by enhancing transcriptional elongation.
The ability of E1A (show BCKDHA Proteins) to target hBre1 to simultaneously repress cellular IFN dependent transcription while activating viral transcription
our results suggest that RNF20 and RNF40, either via ubiquitylation of H2B or other targets, are coupled to the proliferation of prostate cancer cells.
Studies indicate that H2B monoubiquitylation is driven primarily by an E3 ubiquitin ligase (show MUL1 Proteins) composed of the two RING finger (show PCGF1 Proteins) proteins RNF20 and RNF40 (show RNF40 Proteins).
RNF20, presumably via H2Bub, selectively represses oncogenic genes by interfering with chromatin recruitment of TFIIS (show TCEA1 Proteins), a factor capable of relieving stalled RNA polymerase II. RNF20 inhibits the interaction between TFIIS (show TCEA1 Proteins) and the PAF1 (show PEX2 Proteins) complex.
RNF20-mediated H2B ubiquitination at DSBs plays a critical role in HRR through chromatin remodeling
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).
, E3 ubiquitin-protein ligase BRE1A
, BRE1 E3 ubiquitin ligase homolog
, homolog of S. cerevisiae BRE1