Targeting Ubiquitin-Proteasome System Enzyme UBE2T for Therapeutic Applications

Target Name: UBE2T

NCBI ID: G29089

UBE2T

Targeting Ubiquitin-Proteasome System Enzyme UBE2T for Therapeutic Applications

Ubiquitin (Ub) conjugating enzyme E2 T, also known as UBE2T, is a protein that plays a crucial role in the regulation of protein degradation in the body. It is a member of the Ubiquitin-proteasome system (UPS), which is a complex protein-protein interaction network that helps to ensure the degradation of damaged or unnecessary proteins. Mutations in the UBE2T gene have been linked to a variety of diseases, including cancer, neurodegenerative diseases, and systemic inflammatory disorders. As a result, targeting UBE2T has become an important research focus in the field of genetics and pharmacology.

UBE2T is a 23-kDa protein that is expressed in a variety of tissues and cells in the body. It is highly conserved, with a calculated pI of 5.5 and a predicted monomeric molecular weight of 46 kDa. UBE2T is composed of a catalytic active center and a C-terminal region that is involved in its substrate recognition and transport. The catalytic active center is the site of the enzyme's catalytic activity and is responsible for the formation of the Ubiquitin bond, which is a covalent bond formed between the amino acids that make up the Ubiquitin protein and the amino acid that is added to the target protein.

The UBE2T gene is located on chromosome 11p and has been implicated in the development of a number of diseases. For example, mutations in the UBE2T gene have been linked to the development of various cancers, including breast cancer, colon cancer, and neurobladder cancer. In addition, UBE2T mutations have also been linked to the development of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease.

Targeting UBE2T has become an important research focus in the field of pharmacology because of its involvement in the regulation of protein degradation. UBE2T has been shown to play a role in the degradation of a variety of proteins, including muscle protein and huntingtin protein. In addition, UBE2T has also been shown to play a role in the regulation of cellular signaling pathways, including the TGF-β pathway.

One potential approach to targeting UBE2T is to use small molecules that can inhibit its catalytic activity. This approach is based on the idea that by inhibiting the activity of UBE2T, it will be possible to reduce the amount of protein that is degraded by the enzyme and potentially slow down or halt the progression of diseases associated with increased protein degradation.

There are currently several drugs that are being developed as potential UBE2T inhibitors. These drugs include:

1. UBE2T inhibitors: These drugs work by binding to the active center of UBE2T and inhibiting its catalytic activity. One such drug is called UBE2T-targeting peptide 1 (UTP1), which is a small molecule that binds to the active center of UBE2T and inhibits its catalytic activity. UTP1 has been shown to be effective in preclinical studies in treating a variety of diseases, including cancer and neurodegenerative diseases.
2. Ubiquitin-proteasome system modulators: These drugs work by modulating the activity of the UPS in a variety of ways, including by increasing the amount of protein that is loaded onto the enzyme for degradation, or by decreasing the amount of protein that is released from the enzyme. One such drug is called colchicine, which is a natural compound that has been shown to be effective in treating a variety of neurodegenerative diseases.

Another approach to targeting UBE2T is to use antibodies that are designed to specifically bind to UBE2T. These antibodies are

Protein Name: Ubiquitin Conjugating Enzyme E2 T

Functions: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair. Acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway (PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:19589784, PubMed:28437106). Also mediates monoubiquitination of FANCL and FANCI (PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:19589784). May contribute to ubiquitination and degradation of BRCA1 (PubMed:19887602). In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:20061386)

The "UBE2T Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about UBE2T comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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