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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 (show GABPA Proteins) degradation through a PML (show PML Proteins)-RNF4 pathway.
Thus, although Rnf4 and Ube2w (show UBE2W Proteins) functionally interact in vitro, these genetic experiments indicate that in response to DNA damage Ube2w (show UBE2W Proteins) and Rnf4 function in distinct pathways.
The E3 ligase RNF4 is required to ubiquitinate FXR (show NR1H4 Proteins) 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 (show NDRG2 Proteins) 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 (show NKX3-2 Proteins) employing HDAC9 (show HDAC9 Proteins)-PIASy (show PIAS4 Proteins)-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 (show MLXIP Proteins)-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 (show UBE2B Proteins) or UBCH5B (show UBE2D2 Proteins) in governing the multiplicity of substrate ubiquitination.
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 (show PML Proteins) SUMOylation and interaction with RNF4 but is required for efficient PML (show PML Proteins) ubiquitination, recruitment of proteasome components within NBs (show NLRP2 Proteins) and proteasome-dependent degradation of PML (show PML Proteins) 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 (show TDG Proteins) and APE1 (show APEX1 Proteins) for active demethylation.
GC-rich (show RELB Proteins) 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
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