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RING1 belongs to the RING finger family, members of which encode proteins characterized by a RING domain, a zinc-binding motif related to the zinc finger domain. Zusätzlich bieten wir Ihnen Ring Finger Protein 1 Antikörper (97) und und viele weitere Produktgruppen zu diesem Protein an.
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High RING1 expression is associated with hepatocellular carcinoma.
Mutation of RING1 is associated with neurodevelopmental abnormalities
study identified novel interactions between CD147 and RING1, recovered CD147 nuclear envelope distribution in melanoma cells, and suggested a new mechanism underlying how cytoplasmic CD147 promotes melanoma development
The release of epigenetic repression by nitrosylation of RING1A is critical for effective cell transdifferentiation.
The polycomb complex proteins BMI1 and RING1A regulate the ubiquitination of chromatin associated proteins bound to promoters.
On the basis of these results, we proposed that the expression of Ring1 protein may be a novel indicator of hepatocellular carcinoma prognosis.
High RING1 expression is associated with non-small cell lung cancer.
HSCARG interacts with RING1 and inhibits RING1 ubiquitination.
Overexpression of the EZH2, RING1, and BMI1 genes is common in MDS and indicate poor prognosis. The products of these genes might participate in epigenetic regulation of Myelodysplastic syndromes.
USP7 was identified as a deubiquitinating enzyme that regulates the ubiquitination state of RING1B.
PcG protein RING1 is associated with adverse pathological features and clinical PSA recurrence in prostate cancer.
Studies in mammalian cells have found a multiplicity of protein complexes containing Ring1A and Ring1B, suggesting an expanded regulatory role for Ring1A, Ring1B proteins in the epigenetic regulation of gene expression.
Data suggest that the RING1-MEIS1/2 axis is regulated by early PD signals and contributes to the initiation or maintenance of the distal signal circuitry.
identification of gene-dosage-dependent roles in primordial germ cell development for Ring1 and Rnf2, two central components of the Polycomb repressive complex 1 (PRC1)
loss of Ring1a/b postnatally results in defective cervical loops and disturbances of enamel and dentin formation in continuously growing incisors
Ring/Sce interacts directly with PcG proteins
Data show that Bmi-1 and Ring1A positively regulate histone H2A ubiquitylation.
Study shows anterior homeotic transformations of the axial skeleton of YY1 mutant mice and reduced phenotypes in mice that are deficient in the class II Polycomb group genes Ring1/Ring1A, indicating a genetic interaction between those two genes.
muscle RING finger 1 and muscle RING finger 3 as key E3 ubiquitin ligases for the ubiquitin proteasome system-dependent turnover of sarcomeric proteins and reveal a potential basis for myosin storage myopathies
poised RNAP configuration is enforced by Polycomb Repressor Complex-mediated ubiquitination of H2A, conditional deletion of Ring1A and Ring1B leads to loss of ubiquitination of H2A, release of poised RNAP, and subsequent gene de-repression.
Ring1A/B-mediated Polycomb silencing functions downstream of the core transcriptional regulatory circuitry to maintain ES cell identity
This gene belongs to the RING finger family, members of which encode proteins characterized by a RING domain, a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is associated with the multimeric polycomb group protein complex. The gene product interacts with the polycomb group proteins BMI1, EDR1, and CBX4, and colocalizes with these proteins in large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is contiguous with the RING finger genes FABGL and HKE4.
E3 ubiquitin-protein ligase RING1
, polycomb complex protein RING1
, really interesting new gene 1 protein
, transcription repressor Ring1A