RNF2 Antibody

1. these data indicate that RING1B and EZH2 repress the innate inflammatory cutaneous squamous cell carcinoma function and impair tumor immunosurveillance PMID: 29394319
2. Observations demonstrated that Plk1 directly interacts with RNF2 and degrades RNF2 via the ubiquitindependent degradation pathway. RNF2 may be used as a new target for mitotic regulation and tumorigenesis. PMID: 29565459
3. These data suggest that RNF2 is an important upstream negative regulator of SIK1 and that restoration of SIK1 levels induced by loss of RNF2 inhibited HCC cell growth and promoted apoptosis, which may represent a promising therapeutic strategy for HCC treatment. PMID: 27911266
4. Study found that prostate cancer (PCa) tissues have high RNF2 expression which is positively correlated with tumor grade indicating that RNF2 may have oncogenic function in PCa. PMID: 28029659
5. Our findings identify RING1B as a trait of the cell-of-origin in Ewing sarcoma PMID: 27317769
6. Study detected RNF2 expression to be overexpressed in esophageal carcinoma cell lines and was associated with the poor prognosis of esophageal carcinoma patients. Data also reflect its important role in the growth of esophageal carcinoma cells by shRNA silencing of RNF2 expression. PMID: 26936624
7. overexpression of RNF2, as examined by immunohistochemical analysis, might serve as a novel prognostic biomarker and potential therapeutic target for urothelial carcinoma of the bladder patients. PMID: 26869491
8. Our findings support the notion that epigenetic regulators, such as RNF2, directly and functionally control powerful gene networks that are vital in multiple cancer processes. PMID: 26450788
9. O-GlcNAc modifies and regulates an essential epigenetic tool, RING1B, which may contribute to human embryonic stem cells pluripotency maintenance and differentiation. PMID: 26100231
10. The enzymatic activity of BMI1 and RING1B were evaluated and compared. PMID: 26151332
11. Bmi1 and possibly RNF2 may be attractive biomarkers of gemcitabine resistance in the context of RRM1 expression. PMID: 24614341
12. combinatorial silencing along with Ezh2 depleted epigenetically modified H2- and H3-histones and inhibited pancreatic cancer cell growth in vitro and in vivo (xenograft model) PMID: 25431952
13. BAP1 deficiency causes increased expression of FoxK2 target genes in a Ring1B-Bmi1-dependent manner PMID: 25451922
14. s describe a critical role for the polycomb group protein Ring1b in nonhomologous end-joining (NHEJ)-mediated end-to-end chromosome fusions. PMID: 24813883
15. Ring1B and the SNAG-associated chromatin modifier EZH2 formed distinct protein complexes with Snail and that EZH2 was required for Snail-Ring1A/B recruitment to the target promoter. PMID: 24903147
16. The acidic patch functions within the nucleosome as nucleosomes containing a mutated acidic patch exhibit defective H2A/H2AXub by RNF168 and RING1B/BMI1 in vitro PMID: 24603765
17. Data indicate that RING finger protein 2 (RNF2) knockdown can increase the sensitivity of U87 cells to X ray radiation. PMID: 24796740
18. Expressed the isolated N-terminal region of Ring1B, N-Ring1B, comprising the first 221 residues of the 334-residue-long Ring1B and found that the N-Ring1B is a well-folded, monomeric fragment, with native-like structure which unfolds irreversibly. PMID: 24284202
19. BMI-1 and RING1B expression was enhanced with the development of embryos in early pregnancy. PMID: 23727134
20. knockdown of RNF2 significantly inhibits both cell proliferation and colony formation and induces apoptosis in cancer cells PMID: 23318437
21. Ring2 may effect the DNA repair through other pathways but not through the expressions of NER protein. PMID: 23712474
22. Results indicate that RNF2 is an E3 ligase for p53 degradation in selective cells, implicating RNF2 as a therapeutic target to restore tumor suppression through p53 in certain tumor cells. PMID: 23319651
23. the reduction of LPS-mediated IL-8 promoter activation was not related to de novo X-DING-CD4 protein synthesis, but depended on function of the exogenous X-DING-CD4 protein. PMID: 22031506
24. These data provide evidence that the X-DING-CD4 gene contributes to early cellular protection from HIV infection in some individuals and this protection depends solely on the unique genetic regulation of the host. PMID: 22042911
25. The organism reacts to HIV-infection by an overexpression of DING proteins. PMID: 22427948
26. Crystallography of a complex of the Bmi1/Ring1b RING-RING heterodimer & UbcH5c shows that UbcH5c interacts with Ring1b only. Bmi1/Ring1b interacts with nucleosomal DNA & an acidic patch on histone H4 to achieve specific monoubiquitination of H2A. PMID: 21772249
27. identification of genes regulated by ring finger protein 2 PMID: 21347701
28. Polycomb Group protein targeting to different chromatin locations relies, in part, on binding partners of the C-terminal domain of RING1B that are diverse in sequence and structure. PMID: 20696397
29. Ring1B plays an important role in the induction of T helper (Th)2 cell-driven allergic airway inflammation through the control of Bim-dependent apoptosis of effector T helper (Th)2 cells in vivo. PMID: 20237291
30. polycomb protein Ring1B regulation by self-ubiquitination or by E6-AP may have implications to the pathogenesis of Angelman syndrome PMID: 20351251
31. The human PcG protein dinG interacts with CP2, a mammalian member of the grainyhead-like family of transcription factors, in vitro and in vivo. The functional consequence of this interaction is repression of CP2-dependent transcription. PMID: 11865070
32. The E3 ubiquitin ligase RNF2 might have a dual function: facilitating the ubiquitination of its target substrates and recruiting the substrates to the proteasome. PMID: 15773819
33. Bmi-1-Ring1B complex stabilizes the interaction of the ubiquitin ligase complex. PMID: 16714294
34. Ring1B and Bmi1 are degraded by an exogenous E3, independent of their RING domain. The RING domains of both proteins mediate their association and subsequent stabilization. PMID: 17157253
35. caspases-3 and caspase-9 play novel roles in transcription by regulating polycomb protein function through direct cleaving of Ring1B. PMID: 17379327
36. With prohibitin, regulates the activity of E2F1 transcription factor via dual pathways. PMID: 17873902
37. Results show that a phosphorylated form of Mel-18 targets the Ring1B histone H2A ubiquitin ligase to chromatin. PMID: 17936708
38. Data show that the presence of flexible regions could allow C-terminal region of RING1B to bind a variety of different factors, ultimately recruiting RING1B and its associated PcG proteins to different genomic loci. PMID: 18616292
39. a novel mechanism by which RNF2 and PHB2 modulate the CP2-mediated transcriptional pathway. PMID: 18629613
40. Altered mRNA expression is associated with therapy failure and death in patients with multiple types of cancer. PMID: 15931389

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HGNC: 10061

OMIM: 608985

KEGG: hsa:6045

STRING: 9606.ENSP00000356480

UniGene: Hs.591490