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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 (show MYC ELISA Kits) is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1 (show PIAS1 ELISA Kits), SENP7 (show SENP7 ELISA Kits) and RNF4
Data show that RNF4 is a SUMO-targeted ubiquitin ligase that targets TRF2 (show TERF2 ELISA Kits) for ubiquitination.
novel insight into cross-talk between ubiquitin and SUMO and uncover USP11 (show USP11 ELISA Kits) and RNF4 as a balanced SUMO-targeted ubiquitin ligase/protease pair with a role in the DDR (show DDR1 ELISA Kits).
RNF4 negatively regulates NF-kappaB (show NFKB1 ELISA Kits) signaling by down-regulating TAB2 (show TAB2 ELISA Kits)
RNF4 enhances Ube2E1 (show UBE2E1 ELISA Kits) 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.
Cells lacking RNF4 exhibited interstrand cross-linker hypersensitivity. The gene encoding RNF4 was epistatic with the other genes encoding members of the FA/BRCA pathway.
RNF4 mediates ubiquitination and turnover of MeCP2 (show MECP2 ELISA Kits) and thus derepresses transcription from DNA methylation (show HELLS ELISA Kits).
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 (show ATR ELISA Kits)-deleted cells is mediated through the combined effects the sumo targeted E3-ubiquitin ligase RNF4 and activation of the AURKA (show AURKA ELISA Kits)-PLK1 (show PLK1 ELISA Kits) pathway
Rnf4 controls protein localization at DNA damage sites by integrating SUMOylation and ubiquitylation events.
SUMO interacting motif is dispensable for PML (show PML ELISA Kits) SUMOylation and interaction with RNF4 but is required for efficient PML (show PML ELISA Kits) ubiquitination, recruitment of proteasome components within NBs (show NLRP2 ELISA Kits) and proteasome-dependent degradation of PML (show PML ELISA Kits) 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 ELISA Kits) and APE1 (show APEX1 ELISA Kits) for active demethylation.
GC-rich (show RELB ELISA Kits) 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 (show UTS2R ELISA Kits).
RNF4 is a negative regulator of TRPS1 (show TRPS1 ELISA Kits) 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.
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