Transformation/transcription Domain-Associated Protein (TRRAP) Kits ELISA

Human Transformation/transcription Domain-Associated Protein (TRRAP) interaction partners

1. TRRAP silencing attenuated p53 accumulation in lymphoma and colon cancer models, whereas TRRAP overexpression increased mutp53 levels, suggesting a role for TRRAP across cancer entities and p53 mutations.

2. TRRAP, an essential component of multiple histone acetyltransferase complexes, was identified as a central regulator of multiciliated cell formation.

3. TRRAP plays an important role in the regulation of the proliferation and stemness of ovarian cancer stem cells.

4. Data suggest that ubiquitin thioesterase 7 (HAUSP) may act as an oncogenic protein that can modulate c-MYC protein expression via transformation-transcription domain-associated protein (TRRAP).

5. study defined eight additional recurrently mutated genes in SMZL; these genes are CREBBP, CBFA2T3, AMOTL1, FAT4, FBXO11, PLA2G4D, TRRAP and USH2A.

6. MYC associates with STAGA through extended interactions of the TAD with both TRRAP and GCN5.

7. Findings establish Trrap as a critical part of the mechanism that restricts differentiation and promotes the maintenance of key features of ESCs.

8. TRRAP is targeted for destruction in a cell cycle-dependent fashion.

9. The over-expression of TRA1 in hepatocirrhosis and hepatocellular carcinoma is correlated with the formation and development of HCC.

10. TRRAP harbors a recurrent mutation that clustered in one position (p. Ser722Phe) in 6 out of 167 melanoma samples (approx. 4%). The nature, pattern and functional evaluation of the TRRAP recurrent mutation suggest that TRRAP functions as an oncogene.

11. knockdown of the adaptor protein TRRAP significantly increased differentiation of cultured brain tumor-initiating cells, sensitized the cells to apoptotic stimuli, and negatively affected cell cycle progression.

12. TRRAP binding and the recruitment of histone H3 and H4 acetyltransferase activities are required for the transactivation of a silent TERT gene in exponentially growing human fibroblasts by c-Myc or N-Myc protein.

13. Data suggest a model in which p53 directly recruits a TRRAP/acetyltransferase complex to the mdm2 gene to activate transcription. In addition, this study defines a novel mechanism utilized by the p53 tumor suppressor to regulate gene expression.

14. requirement in transcription activation via c-myc transformation domain

15. Results identify YL1 as a subunit of the TRRAP/TIP60 HAT complex, and also as a component of a novel mammalian multiprotein complex that includes the SNF2-related helicase SRCAP.

16. HAT cofactor Trrap and Tip60 HAT bind to the chromatin surrounding sites of DNA double-strand breaks (DSBs). Cells may use the same basic mechanism involving HAT complexes to regulate distinct cellular processes, such as transcription and DNA repair.

17. NPAT recruits the TRRAP-Tip60 complex to histone gene promoters to coordinate the transcriptional activation of multiple histone genes during the G(1)/S-phase transition

18. Loss of Transduction; transformation-transcription domain-associated protein leads to a reduced level of beta-catenin ubiquitination, accumulation of beta-catenin protein and concomitant hyperactivation of the Wnt Proteins pathway.

19. Several function of TRRAP during cellular process like: DNA repair, cell cycle, transcription etc...

Mouse (Murine) Transformation/transcription Domain-Associated Protein (TRRAP) interaction partners

1. TRRAP deficiency impairs B-cell development but does not directly affect class switch recombination (CSR. Instead, cells induced to proliferate undergo apoptosis. Our findings demonstrate a central and general role of TRRAP in cell proliferation.

2. expression profiles of Trrap-responsive genes, using cDNA microarray in mitotic cells

3. Data show that the loss of Trrap leads to chromosome missegregation, mitotic exit failure and compromised mitotic checkpoints, which are caused by defective Trrap-mediated transcription of the mitotic checkpoint proteins Mad1 and Mad2.

4. HAT cofactor Trrap and Tip60 HAT bind to the chromatin surrounding sites of DNA double-strand breaks (DSBs). Cells may use the same basic mechanism involving HAT complexes to regulate distinct cellular processes, such as transcription and DNA repair.

5. Fe65 and its interaction with APP play an important role in the response to DNA damage by assisting the recruitment

6. this study has identified a critical role for Trrap in the mechanism that maintains hematopoietic stem cells and hematopoietic system, and underscores the importance of Trrap and histone modifications in tissue homeostasis.