ZNF313 antibody - N-terminal region (ARP33164_T100)
- Known as:
- ZNF313 (anti-) - N-terminal region (ARP33164_T100)
- Catalog number:
- arp33164_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ZNF313 antibody - N-terminal region (ARP33164_T100)
Related genes to: ZNF313 antibody - N-terminal region (ARP33164_T100)
- Gene:
- RNF114 NIH gene
- Name:
- ring finger protein 114
- Previous symbol:
- ZNF313
- Synonyms:
- PSORS12
- Chromosome:
- 20q13.13
- Locus Type:
- gene with protein product
- Date approved:
- 2000-07-31
- Date modifiied:
- 2016-10-05
Related products to: ZNF313 antibody - N-terminal region (ARP33164_T100)
Related articles to: ZNF313 antibody - N-terminal region (ARP33164_T100)
- HIV-1 evades host immunity via a number of virally encoded mediators. Here we show that the HIV-1 antisense protein (ASP) evades host immunity by interfering with the type I interferon (IFN-I) response. Mechanistically, host prolyl hydroxylase 3 (PHD3) hydroxylates ASP at Pro47, enabling the recruitment of the RING finger protein 114 (RNF114) to TANK-binding kinase 1 (TBK1). Subsequently, RNF114 mediates K6-linked ubiquitination of TBK1 at Lys236, suppressing TBK1 activation and the downstream IFN-I response. Conversely, mutation of ASP at Pro47 abolishes this inhibitory effect. In humanized mice, either ASP deletion or treatment with the RNF114 inhibitor EN219 or the PHD3 inhibitor Molidustat enhances antiviral immunity and reduces viral replication. Clinically, RNF114 and PHD3 transcript levels exhibit a positive correlation with viral load in treatment-naive patients. Here we show a distinct HIV-1 immune evasion mechanism involving proline hydroxylation and K6-linked ubiquitination, highlighting therapeutic potential. - Source: PubMed
Publication date: 2026/04/13
Lin XinguangZhang WenruiLi ManmanZhang ChuanzhenXun JingnaHan WendongChen JunZhang YihuaYan Dapeng - ADP-ribosylation (ADPr) is a post-translational modification that has regulatory roles in multiple cellular pathways including the DNA damage response and in innate immunity. Recently, it has been uncovered that ADP-ribose can be further modified by a family of ubiquitin E3 ligases, the DELTEXES, which catalyze ubiquitin transfer directly onto ADP-ribose, creating a hybrid ADPr-Ub modification which can be recognized by proteins with dedicated ADPr-Ub binding domains. With this hybrid modification recently been identified in cellular systems, we use a series of in vitro and cellular assays in human cells to investigate the amino acid preference for ADPr-Ub production as well as conditions required for reversal of the modification. We show that ADPr on both serine and glutamate-linked peptides can be ubiquitinated by the RING-DTC domains of DTX2 and DTX3L in vitro and that this can be recognized by RNF114, RNF138 and RNF166 for ubiquitin chain elongation. Finally, we demonstrate that DTX2 rather than DTX3L plays a role in ADPr-Ub production at sites of DNA damage to promote the recruitment of RNF114, RNF138, and RNF166 in an HPF1-independent manner. - Source: PubMed
Publication date: 2026/04/02
Chatrin ChatrinZhu KangSimmons Michael D RMaginn LucySchützenhofer KiraLu YangĐukić NinaWijngaarden SvenKloet Max SKliza Katarzyna WiktoriaHeden van Noort Gerbrand J van derFilippov Dmitri VAhel DraganaSmith RebeccaAhel Ivan - ADP-ribosylation has long been recognised as a key regulator of essential signalling pathways, including the DNA damage response. However, only recent and ongoing technological advances are beginning to make it possible to investigate its distinct forms with molecular precision. Here, we design a 'mono-ADP-ribosylation blocking' strategy to develop sensitive, modular antibodies with high specificity for poly(ADP-ribosyl)ation. During peptide antigen generation, we identify a distinctive mass spectrometric signature that enables accurate mapping of poly(ADP-ribosyl)ation sites and helps prevent site mislocalization. Moreover, we affinity-mature mono-ADP-ribosylation and histone H3 site-specific antibodies. These tools reveal that, upon DNA damage, XRCC1 deficiency dramatically elevates the mono-ADP-ribosylation wave of PARP1 signalling, in addition to increasing poly(ADP-ribosyl)ation. This PARP1 hyperactivation leads to an increase in an unconventional form of ubiquitylation, recently shown to directly target mono-ADP-ribose in the DNA damage response and other signalling pathways. Consequently, XRCC1 loss enhances the recruitment of RNF114, the reader of this composite modification, to DNA lesions. These findings establish mono-ADP-ribosylation - and its ester-linked ubiquitylation - as key modifications induced by XRCC1 deficiency during DNA damage, revealed using tools we developed for precise and sensitive ADP-ribosylation detection. - Source: PubMed
Publication date: 2026/04/02
Dauben HelenMihaljević MihaelaKolvenbach AndreasPalumbieri Maria DiliaKapsali ChrysiHuppertz InaMatić Ivan - [This corrects the article DOI: 10.3389/fnins.2025.1533253.]. - Source: PubMed
Publication date: 2026/02/16
Courraud JeremieQuartier AngéliqueDrouot NathalieZapata-Bodalo IreneGilet JohanBenchoua AlexandraMandel Jean-LouisPiton Amélie - ADP-ribosyl ubiquitination is a unique form of crosstalk between post-translational modifications, where recently RNF114 has been identified as the first dedicated reader of this dual modification. New findings reveal that RNF114 extends the initial hybrid ADPr-Ub modification with K11-linked poly-Ub chains. This highlights the recent advances made in methods and tools to study this hybrid signal and addresses some key questions that remain. - Source: PubMed
Publication date: 2026/02/19
de Vries Max C Mvan der Heden van Noort Gerbrand J