Target Name: USP25
NCBI ID: G29761
Review Report on USP25 Target / Biomarker Content of Review Report on USP25 Target / Biomarker
USP25
Other Name(s): deubiquitinating enzyme 25 | USP25 variant 3 | ubiquitin thiolesterase 25 | Ubiquitin specific peptidase 25 | Ubiquitin carboxyl-terminal hydrolase 25 | ubiquitin specific peptidase 25 | Ubiquitin specific peptidase 25, transcript variant 3 | ubiquitin thioesterase 25 | Deubiquitinating enzyme 25 | USP21 | ubiquitin-specific processing protease 25 | Ubiquitin specific protease 25 | Ubiquitin thioesterase 25 | Ubiquitin-specific-processing protease 25 | USP on chromosome 21 | Ubiquitin carboxyl-terminal hydrolase 25 (isoform USP25a) | UBP25_HUMAN | Ubiquitin-specific processing protease 25

USP25: A Potential Drug Target and Biomarker

Unlike most proteins, USP25 is synthesized in the liver and has no known cellular localization. It is a small non-cysteine 鈥嬧?媝rotein with 25 amino acid residues, which is the reason for its name. Despite its small size, USP25 has a significant role in the regulation of protein degradation in the liver. USP25 is an essential enzyme in the deubiquitination pathway, which is a critical process in protein homeostasis.

The deubiquitination pathway is a complex process that involves the removal of misfolded or damaged proteins from the cell. This process is critical for maintaining cellular homeostasis and for the regulation of various cellular processes, including cell growth, apoptosis, and inflammation. also important for the regulation of protein stability and for the detoxification of harmful substances.

USP25 is a key enzyme in the deubiquitination pathway by participating in the recognition and removal of misfolded or damaged proteins. It does this by forming a covalent complex with the target protein and then using its ATP-dependent transmembrane domain to promote the addition of a ubiquitin tag to the protein. This ubiquitin tag allows for the targeted degradation of the protein by the 26S proteasome, a complex responsible for the efficient degradation of damaged or misfolded proteins.

USP25's role in the deubiquitination pathway is further confirmed by its deficiency leading to the accumulation of a variety of proteins in the liver, including some known to be associated with disease, such as amyloidosis-related proteins. The accumulation of these proteins suggests that USP25 plays an important biological role in the liver, and if it does not work properly, it may contribute to the development of a variety of diseases.

In addition to its role in the deubiquitination pathway, USP25 has also been shown to play a role in the regulation of protein stability and cell signaling pathways. USP25 has been shown to interact with several protein partners, including the transcription factor, p53, and the protein kinase , B-cell signaling pathway.

USP25 has also been shown to play a role in the regulation of cellular processes, including cell growth, apoptosis, and inflammation. For example, USP25 has been shown to be involved in the regulation of the levels of the protein, p16INK4a, which is a known regulator of cell apoptosis. Additionally, USP25 has been shown to be involved in the regulation of the levels of the protein, nuclear factor kappa B (NF-kappa-B), which is a known regulator of inflammation.

In conclusion, USP25 is a small non-cysteine 鈥嬧?媝rotein that plays a critical role in the regulation of protein degradation in the liver. Its deficiency can lead to the occurrence of various diseases and is also related to cell signaling and cell growth. USP25 is a potential drug target and biomarker for the treatment of various diseases.

Protein Name: Ubiquitin Specific Peptidase 25

Functions: Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains

The "USP25 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 USP25 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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