Browse our anti-UBR5 (UBR5) Antibodies

Human Ubiquitin Protein Ligase E3 Component N-Recognin 5 (UBR5) interaction partners

1. UBR5 ubiquitylates CSPP1, and that UBR5 is required for cytoplasmic organization of CSPP1-comprising centriolar satellites in centrosomal periphery.

2. UBR5 is a modulator of super-vigilant proteostasis of induced pluripotent stem cells from Huntington's disease patients

3. UBR5 was highly expressed in colon cancer not only at mRNA level but also at protein level; UBR5 promoted the growth of colon cancer cells, and inhibited apoptosis.

4. BMI1 and UBR5 repress the polymerase II (Pol II)-mediated transcription at damaged sites

5. Results found that EDD was consistent with GOLPH3 expression and also promoted the EMT process and activated Wnt/beta-catenin signaling in epithelial ovarian cancer.

6. UBR5 directly binds to the tumor suppressor esophageal cancer-related gene 4, increasing its ubiquitination to reducing the protein stability of ECRG4 to promote colorectal cancer progression.

7. Wnt-dependent inactivation of the Groucho/TLE co-repressor by the HECT E3 ubiquitin ligase Hyd/UBR5 is a key prerequisite that enables Armadillo/beta-catenin to activate transcription.

8. UBR5 downregulates proapoptotic MOAP-1 and suggest that UBR5 can confer cisplatin resistance in ovarian cancer.

9. Data suggest that UBR5 down-regulates levels of TRAF3, a key component of Toll-like receptor signaling, via the miRNA pathway; p90RSK is an upstream regulator of UBR5; p90RSK phosphorylates UBR5 as required for translational repression of TRAF3 mRNA. (UBR5 = ubiquitin protein ligase E3 component n-recognin 5 protein; TRAF3 = TNF receptor-associated factor 3; p90RSK = 90 kDa ribosomal protein S6 kinase)

10. Data show that ubiquitin protein ligase E3 component n-recognin 5 protein (UBR5) bound the tumor suppressor gastrokine 1 (GKN1) and increased its ubiquitination to reduce the protein stability of GKN1.

11. Findings unveil UBR5 as a novel and critical regulator of tumor growth, metastasis, and immune response in triple negative breast cancer.

12. Study highlights many functional biological role of UBR5 especially in cancer where it seems to be a key regulator of cell signaling. [review]

13. Colony-formation assays and soft agar assays show that gain of function of TIP60 or depletion of EDD1 in HPV-positive cervical cancer cells significantly inhibits cell growth in vitro

14. Human herpesvirus-6 U14 induces cell cycle arrest in G2/M phase by associating with a cellular protein, EDD.

15. Elevated metaphase RanGTP levels use Ubr5 to couple overall chromosome congression to SAC silencing.

16. results confirm the role of the MLLE domain of UBR5 in substrate recruitment and suggest a potential role in regulating UBR5 ligase activity.

17. these observations highlight the potential role of EDD in regulating mitotic progression and the cellular response to perturbed mitosis.

18. Utilizing a high throughput RNAi screening approach author identified UBR5, a protein commonly amplified in breast cancer, as a novel regulator of ERalpha protein levels and transcriptional activity.

19. the alpha4 N-terminus binding to endogenous PP2Ac and PABP, and the C-terminus to EDD, is reported.

20. These results identify EDD as a dual regulator of cell survival and cisplatin resistance and suggest that EDD is a therapeutic target for ovarian cancer.

Mouse (Murine) Ubiquitin Protein Ligase E3 Component N-Recognin 5 (UBR5) interaction partners

1. Hence, while loss of UBR5 perturbed Hedgehog signalling in the developing limb, there were no obvious morphological defects.

2. Findings unveil UBR5 as a novel and critical regulator of tumor growth, metastasis, and immune response in triple negative breast cancer.

3. UBR5-mediated ATMIN ubiquitination is a vital event for ATM pathway selection and activation in response to DNA damage

4. a novel function of RIP1 kinase involving its interaction with EDD to regulate JNK activation and TNFalpha production.

5. Silencing Edd1 with shRNA in mouse embryonic stem cells significantly suppressed their growth.

6. The SCF E3 ligase complex containing Fbxo40 directly ubiquitinates IRS1, and this activity is enhanced by increased tyrosine phosphorylation of IRS1.

7. Through the PABC domain, EDD participates in miRNA silencing by recruiting downstream effectors.

8. UBR5 can attenuate myocardin protein degradation resulting in increased myocardin protein expression without affecting myocardin mRNA expression.

9. Results suggest that Edd has an essential role in extraembryonic development.