TRRAP: A Potential Drug Target and Biomarker for Transformational Genomics

Target Name: TRRAP

NCBI ID: G8295

TRRAP

TRRAP: A Potential Drug Target and Biomarker for Transformational Genomics

Transformation/transcription domain-associated proteins (TRRAPs) are a class of non-coding RNAs that play crucial roles in various cellular processes. These proteins have been identified as potential drug targets and biomarkers due to their unique structure, function, and involvement in various cellular pathways. In this article, we will explore the TRRAP protein and its potential as a drug target and biomarker.

Structure and Function

TRRAPs are characterized by a unique nucleotide-binding oligomerization (NBO) domain, which is responsible for the protein's stability and stability-dependent interactions. This domain is composed of a nucleotide-binding oligomerization domain and a C-terminal hypervariable region (HVR). The NBO domain is responsible for the protein's stability by forming a stable complex with the nucleotide. The C-terminus of TRRAP contains a series of highly conserved amino acids, which are involved in the protein's stability and interaction with various cellular components.

TRRAP is involved in various cellular processes, including DNA replication, transcription, and cell growth. During DNA replication, TRRAP is known to play a role in the initiation of DNA replication by binding to the template DNA and promoting the formation of an active complex with the complex protein p53. This interaction between TRRAP and p53 is critical for the regulation of DNA replication and the maintenance of genetic integrity.

During transcription, TRRAP is involved in the regulation of gene expression by binding to the RNA polymerase II complex. This interaction between TRRAP and RNA polymerase II is critical for the regulation of gene expression and the production of various RNA molecules.

TRRAP is also involved in the regulation of cell growth and the maintenance of cellular homeostasis. This is achieved by the regulation of various cellular processes, including cell adhesion, migration, and the regulation of cell apoptosis.

Potential Drug Target

TRRAP has been identified as a potential drug target due to its involvement in various cellular processes that are crucial for human health. One of the main drug targets for TRRAP is the regulation of cell apoptosis. TRRAP has been shown to play a role in the regulation of cell apoptosis by binding to the B-cell lymphoma 1 (Bcl-2) protein. This interaction between TRRAP and Bcl-2 has been shown to promote the inhibition of cell apoptosis and the survival of cancer cells.

Another potential drug target for TRRAP is the regulation of DNA replication. TRRAP has been shown to play a role in the regulation of DNA replication by binding to the DNA replication factor, DFN1. This interaction between TRRAP and DFN1 has been shown to promote the initiation of DNA replication and the formation of the replication complex.

TRRAP has also been shown to play a role in the regulation of cell growth and the maintenance of cellular homeostasis. This is achieved by the regulation of various cellular processes, including cell adhesion, migration, and the regulation of cell apoptosis.

Biomarker

TRRAP has also been shown to be a potential biomarker for various diseases, including cancer. This is achieved by the regulation of various cellular processes that are crucial for cancer cell growth and survival. One of the main biomarkers for TRRAP is the expression of TRRAP, which is often decreased in cancer cells compared to normal cells. This decrease in TRRAP expression has been shown to promote the growth and survival of cancer cells, making it an attractive biomarker for cancer diagnosis and treatment.

Conclusion

In conclusion, TRRAP is a unique protein that is involved in various cellular processes that are crucial for human health. Its involvement in the regulation of cell apoptosis, DNA replication,

Protein Name: Transformation/transcription Domain Associated Protein

Functions: Adapter protein, which is found in various multiprotein chromatin complexes with histone acetyltransferase activity (HAT), which gives a specific tag for epigenetic transcription activation. Component of the NuA4 histone acetyltransferase complex which is responsible for acetylation of nucleosomal histones H4 and H2A. Plays a central role in MYC transcription activation, and also participates in cell transformation by MYC. Required for p53/TP53-, E2F1- and E2F4-mediated transcription activation. Also involved in transcription activation mediated by the adenovirus E1A, a viral oncoprotein that deregulates transcription of key genes. Probably acts by linking transcription factors such as E1A, MYC or E2F1 to HAT complexes such as STAGA thereby allowing transcription activation. Probably not required in the steps following histone acetylation in processes of transcription activation. May be required for the mitotic checkpoint and normal cell cycle progression. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome. May play a role in the formation and maintenance of the auditory system (By similarity)

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•   the target screening and validation;
•   expression level;
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