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The protein encoded by RNF31 contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions. Additionally we are shipping RNF31 Antibodies (65) and RNF31 Kits (1) and many more products for this protein.
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RNF31 decreased p53 (show TP53 Proteins) stability. RNF31 depletion caused cell cycle arrest and cisplatin-induced apoptosis in a p53 (show TP53 Proteins)-dependent manner. RNF31 associated with the p53 (show TP53 Proteins)/MDM2 (show MDM2 Proteins) complex, facilitating p53 (show TP53 Proteins) polyubiquitination and degradation by stabilizing MDM2 (show MDM2 Proteins).
This study describes a novel posttranslational regulation of the HOIP-containing linear-ubiquitin-chain assembly complex (LUBAC)-mediated linear ubiquitination that is critical for specifically directing TLR4 (show TLR4 Proteins)-mediated NF-kappaB (show NFKB1 Proteins) activation.
These findings collectively indicated an oncogene (show RAB1A Proteins) role of RNF31 in PCa (show FLVCR1 Proteins) progression which can be regulated by miR (show MLXIP Proteins)-503, suggesting that RNF31 could serve as a potential prognostic biomarker and therapeutic target for PCa (show FLVCR1 Proteins).
we identified BCL10 (show BCL10 Proteins) as a bona fide target of BCR (show BCR Proteins)-induced linear ubiquitylation and demonstrated an important role of the linear ubiquitin ligase HOIP in BCR (show BCR Proteins)-induced phosphorylation
crystal structure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation
human HOIP is essential for the assembly and function of LUBAC, which includes HOIL-1 (show RBCK1 Proteins), and for various processes governing inflammation and immunity in both hematopoietic and nonhematopoietic cells
Two rare germline polymorphisms affecting the LUBAC subunit RNF31 were identified and enriched among patients with activated B cell-like subtype of diffuse large B-cell lymphoma.
RNF31, via stabilizing ESR1 (show ESR1 Proteins) levels, controls the transcription of estrogen-dependent genes linked to breast cancer cell proliferation.
Phosphorylation of OTULIN prevents HOIP binding, whereas unphosphorylated OTULIN is part of the endogenous LUBAC complex.
HOIP binding to OTULIN is required for the recruitment of OTULIN to the TNF (show TNF Proteins) receptor complex.
HOIP's catalytic activity is necessary for preventing TNF (show TNF Proteins)-induced cell death. Hence, LUBAC and its linear-ubiquitin-forming activity are required for maintaining vascular integrity during embryogenesis by preventing TNFR1 (show TNFRSF1A Proteins)-mediated endothelial cell death.
Restoration of HOIP expression reversed the defects in cellular activation and signaling. These results reveal HOIP as a key component of the CD40 (show CD40 Proteins) signaling pathway
The protein encoded by this gene contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions.
ring finger protein 31
, E3 ubiquitin-protein ligase RNF31
, HOIL-1-interacting protein
, zinc in-between-RING-finger ubiquitin-associated domain protein
, RING finger protein 31
, putative Ariadne-like ubiquitin ligase