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Ring finger protein 125

RNF125, TRAC-1, ring finger protein 125
This gene encodes a novel E3 ubiquitin ligase that contains a RING finger domain in the N-terminus and three zinc-binding and one ubiquitin-interacting motif in the C-terminus. As a result of myristoylation, this protein associates with membranes and is primarily localized to intracellular membrane systems. The encoded protein may function as a positive regulator in the T-cell receptor signaling pathway. [provided by RefSeq, Mar 2012] (from NCBI)
Top mentioned proteins: Ubiquitin, RIG-I, MDA5, V1a, SMRT
Papers on RNF125
A non-canonical role of the p97 complex in RIG-I antiviral signaling.
Zhou et al., Shanghai, China. In Embo J, Jan 2016
The p97 complex is able to directly bind both non-ubiquitinated RIG-I and the E3 ligase RNF125, promoting K48-linked ubiquitination of RIG-I at residue K181.
MicroRNA-15b Modulates Japanese Encephalitis Virus-Mediated Inflammation via Targeting RNF125.
Cao et al., Wuhan, China. In J Immunol, Oct 2015
Mechanistically, ring finger protein 125 (RNF125), a negative regulator of RIG-I signaling, is identified as a direct target of miR-15b in the context of JEV infection.
Downregulation of the Ubiquitin Ligase RNF125 Underlies Resistance of Melanoma Cells to BRAF Inhibitors via JAK1 Deregulation.
Ronai et al., Los Angeles, United States. In Cell Rep, Jul 2015
Here, we identified the downregulation of the ubiquitin ligase RNF125 in BRAFi-resistant melanomas and demonstrated its role in intrinsic and adaptive resistance to BRAFi in cultures as well as its association with resistance in tumor specimens.
RNF125 is a ubiquitin-protein ligase that promotes p53 degradation.
Miao et al., Xinxiang, China. In Cell Physiol Biochem, 2014
Here, we investigated the role of RNF125, a non-Mdm2 ubiquitin-protein ligase, in the regulation of p53.
A new overgrowth syndrome is due to mutations in RNF125.
Lapunzina et al., Madrid, Spain. In Hum Mutat, 2014
We identified one de novo deletion and three missense mutations in RNF125 in six patients from four families with overgrowth, macrocephaly, intellectual disability, mild hydrocephaly, hypoglycemia, and inflammatory diseases resembling Sjögren syndrome.
Ring finger protein 166 potentiates RNA virus-induced interferon-β production via enhancing the ubiquitination of TRAF3 and TRAF6.
Chen et al., Beijing, China. In Sci Rep, 2014
Overexpression of RNF166 rather than its homologous proteins RNF114, RNF125, and RNF138, enhanced Sendai virus (SeV)-induced activation of the IFN-β promoter.
Expression levels of the innate response gene RIG-I and its regulators RNF125 and TRIM25 in HIV-1-infected adult and pediatric individuals.
Giannini et al., Rio de Janeiro, Brazil. In Aids, 2013
As the ubiquitin ligases RNF125 and TRIM25 are involved in regulating RIG-I function, our aim was to assess whether the levels of these three genes vary between healthy and HIV-infected individuals and whether these levels are related to disease progression.
Association between hepatic steatosis and hepatic expression of genes involved in innate immunity in patients with chronic hepatitis C.
Murakami et al., Ōgaki, Japan. In Cytokine, 2013
The levels of mRNA of innate immunity genes (RIG-I, MDA5, LGP2, Cardif, RNF125, ISG15, and USP18) were measured by real-time polymerase chain reaction in RNA extracted from biopsied liver tissue and compared between patients with and without hepatic steatosis.
Human bocavirus VP2 upregulates IFN-β pathway by inhibiting ring finger protein 125-mediated ubiquitination of retinoic acid-inducible gene-I.
Wang et al., Wuhan, China. In J Immunol, 2013
In this study, we report that the structural protein VP2 of human Bocavirus modulates IFN pathway by targeting the ring finger protein 125 (RNF125), a negative regulator of type I IFN signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I (RIG-I) and subsequently leads to the proteasome-dependent degradation of RIG-I.
Ubiquitin-mediated modulation of the cytoplasmic viral RNA sensor RIG-I.
Seya et al., Sapporo, Japan. In J Biochem, 2012
RNF125, another ubiquitin ligase, is a negative regulator of RIG-I and mediates K48-linked polyubiquitination of RIG-I, leading to the degradation of the RIG-I protein by proteasomes.
Association of gene expression involving innate immunity and genetic variation in interleukin 28B with antiviral response.
Izumi et al., Musashino, Japan. In Hepatology, 2012
We genotyped IL28B SNPs (rs8099917 and rs12979860) in 88 chronic hepatitis C patients treated with PEG-IFNα-2b/RBV and quantified expressions of viral sensors (RIG-I, MDA5, and LGP2), adaptor molecule (IPS-1), related ubiquitin E3-ligase (RNF125), modulators (ISG15 and USP18), and IL28 (IFNλ).
Functional analysis of the RNF114 psoriasis susceptibility gene implicates innate immune responses to double-stranded RNA in disease pathogenesis.
Capon et al., London, United Kingdom. In Hum Mol Genet, 2011
Although the function of RNF114 is unknown, its paralogue RNF125 has been shown to regulate the RIG-I/MDA5 innate antiviral response.
The ubiquitin ligase Riplet is essential for RIG-I-dependent innate immune responses to RNA virus infection.
Seya et al., Sapporo, Japan. In Cell Host Microbe, 2011
RIG-I is regulated by Lys63-linked polyubiquitination, and three E3 ubiquitin ligases, RNF125, TRIM25, and Riplet, are reported to target RIG-I for ubiquitination.
Identification of genes with differential expression in chemoresistant epithelial ovarian cancer using high-density oligonucleotide microarrays.
Lee et al., Seoul, South Korea. In Oncol Res, 2008
Upregulated genes in chemoresistant tumors included cell cycle regulating genes (TOP2A, BCAT1, CDCA8, CCNA2, CENPE), and genes with previously known mechanisms in tumorigenesis (S100A9, APOA1, RNF125, IFI16).
Potential relevance of cytoplasmic viral sensors and related regulators involving innate immunity in antiviral response.
Miyake et al., Musashino, Japan. In Gastroenterology, 2008
Cardif and RNF125 were negatively correlated with RIG-I and significantly suppressed in NVR.
T-cell regulator RNF125/TRAC-1 belongs to a novel family of ubiquitin ligases with zinc fingers and a ubiquitin-binding domain.
Bijlmakers et al., London, United Kingdom. In Biochem J, 2008
TRAC-1 associates with membranes and is excluded from the nucleus through myristoylation
The RING finger ubiquitin ligase RNF125/TRAC-1 down-modulates HIV-1 replication in primary human peripheral blood mononuclear cells.
Ikuta et al., Suita, Japan. In Virology, 2007
These results suggest that RNF125/TRAC-1 could function to recruit host factor(s) controlling HIV-1 transcription to the ubiquitin-proteasome pathway.
Negative regulation of the RIG-I signaling by the ubiquitin ligase RNF125.
Shimotohno et al., Kyoto, Japan. In Proc Natl Acad Sci U S A, 2007
RNF125 is enhanced by IFN, these functions constitute a negative regulatory loop circuit for IFN production
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