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DNMT1 as a potential new small ubiquitin-related modifier-(SUMO)-targeted ubiquitin E3 ligase substrate of RNF4, with knockdown of dnmt1 largely restoring primitive and definitive granulopoiesis in rnf4-deficient zebrafish
Study provides an insight into the role of the RNF4 to balance the role of SUMO signaling by directly targeting Ubc9 and SUMO E3 ligases.
High RNF4 expression is associated with adenovirus infections.
Respiratory syncytial virus induces NRF2 degradation through a PML-RNF4 pathway.
Thus, although Rnf4 and Ube2w functionally interact in vitro, these genetic experiments indicate that in response to DNA damage Ube2w and Rnf4 function in distinct pathways.
The E3 ligase RNF4 is required to ubiquitinate FXR in response to SUMOylation.
RNF4-dependent ubiquitylation translates transient phosphorylation signal(s) into long-term protein stabilization, resulting in enhanced oncoprotein activation
These findings indicate that SUMOylation of NDRG2 is necessary for its tumor suppressor function in lung adenocarcinoma and that RNF4 increases the efficiency of this process.
post-translational modification of Nkx3.2 employing HDAC9-PIASy-RNF4 axis plays a crucial role in controlling chondrocyte viability and hypertrophic maturation during skeletal development in vertebrates.
These findings illustrate a novel strategy for viral interference with the SUMO pathway, and identify the EBV miR-BHRF1-1 and the cellular RNF4 as regulators of the productive virus cycle.
These results point to an important role of the affinity between RNF4 and its cognate RAD6B or UBCH5B in governing the multiplicity of substrate ubiquitination.
the opposing activities of RNF4 and ataxin-3 consolidate robust MDC1-dependent signaling and repair ofDNA double-strand break.
Combined effect of dynamic recruitment of RNF4 to KAP1 regulates the relative occupancy of 53BP1 and BRCA1 at double-strand break sites to direct DNA repair in a cell cycle-dependent manner.
c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4
Data show that RNF4 is a SUMO-targeted ubiquitin ligase that targets TRF2 for ubiquitination.
novel insight into cross-talk between ubiquitin and SUMO and uncover USP11 and RNF4 as a balanced SUMO-targeted ubiquitin ligase/protease pair with a role in the DDR.
RNF4 negatively regulates NF-kappaB signaling by down-regulating TAB2
RNF4 enhances Ube2E1 self-ubiquitination.
NMR spectroscopy and biochemical characterization reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer.
RecQ-like helicase BLM subcellular localization is regulated by SUMO-targeted ubiquitin ligase RNF4 in response to DNA damage, presumably to prevent illegitimate recombination events.
These findings suggest that the UBC9/PML/RNF4 axis plays a critical role as an important SUMO pathway in cardiac fibrosis. Modulating the protein levels of the pathway provides an attractive therapeutic target for the treatment of cardiac fibrosis and heart failure.
This paper identifies a nucleosome-targeting motif within the RNF4 RING domain that can bind DNA and thereby enables RNF4 to selectively ubiquitinate nucleosomal histones.
fork collapse in Atr-deleted cells is mediated through the combined effects the sumo targeted E3-ubiquitin ligase RNF4 and activation of the AURKA-PLK1 pathway
Rnf4 controls protein localization at DNA damage sites by integrating SUMOylation and ubiquitylation events.
SUMO interacting motif is dispensable for PML SUMOylation and interaction with RNF4 but is required for efficient PML ubiquitination, recruitment of proteasome components within NBs and proteasome-dependent degradation of PML in response to AsO
Rnf4 deficiency is embryonic lethal with higher levels of methylation in genomic DNA. Mechanistic studies show that RNF4 interacts with and requires the base excision repair enzymes TDG and APE1 for active demethylation.
GC-rich elements flanking the transcription start site govern activation
1.6- and 3.0-kb transcripts originate from the same promoter, encode for the same protein and differ in the 3' UTR.
RNF4 is a negative regulator of TRPS1 activity
results suggest a role for small nuclear ring finger protein(SNURF/RNF4) in fetal germ cell development as well as in oocyte and granulosa cell maturation in an estrogen- and gonadotropin-regulated fashion
Rnf4 possesses ubiquitin E3 ligase activity.
Mammalian RNF4, an active ubiquitin E3 ligase, is an orthologue of Rfp1/Rfp2. Rfp1 and Rfp2 lack E3 activity but recruit Slx8, an active RING-finger ubiquitin ligase, through a RING-RING interaction, to form a functional E3.
The protein encoded by this gene contains a RING finger motif and acts as a transcription regulator. This protein has been shown to interact with, and inhibit the activity of, TRPS1, a transcription suppressor of GATA-mediated transcription. Transcription repressor ZNF278/PATZ is found to interact with this protein, and thus reduce the enhancement of androgen receptor-dependent transcription mediated by this protein. Studies of the mouse and rat counterparts suggested a role of this protein in spermatogenesis. A pseudogene of this gene is found on chromosome 1.
E3 ubiquitin ligase RNF4
, E3 ubiquitin-protein ligase RNF4
, small nuclear RING finger protein
, gene trap ROSA b-geo 8
, small nuclear ring finger protein
, RING finger protein 4