Target Name: USP38
NCBI ID: G84640
Review Report on USP38 Target / Biomarker Content of Review Report on USP38 Target / Biomarker
USP38
Other Name(s): ubiquitin specific peptidase 38 | FLJ35970 | Deubiquitinating enzyme 38 | Ubiquitin specific peptidase 38, transcript variant 2 | ubiquitin-specific-processing protease 38 | ubiquitin specific protease 38 | Ubiquitin specific protease 38 | deubiquitinating enzyme 38 | Ubiquitin carboxyl-terminal hydrolase 38 | USP38 variant 2 | Ubiquitin thioesterase 38 | Ubiquitin carboxyl-terminal hydrolase 38 (isoform 1) | KIAA1891 | ubiquitin thiolesterase 38 | USP38 variant 1 | Ubiquitin-specific-processing protease 38 | UBP38_HUMAN | HP43.8KD | OTTHUMP00000220204 | Ubiquitin carboxyl-terminal hydrolase 38 (isoform 2) | Ubiquitin specific peptidase 38, transcript variant 1 | Ubiquitin thiolesterase 38 | ubiquitin thioesterase 38

USP38: A Protein Involved in Cell Signaling and Degradation

USP38 ( Ubiquitin Specific Peptidase 38 ) is a protein that is expressed in a wide range of tissues throughout the body, including the brain, muscle, liver, and pancreas. It is a member of the ubiquitin system, which is a system of protein degradation that is important for maintaining cellular homeostasis and regulating various cellular processes.

USP38 is a 21-kDa protein that is composed of 21 amino acid residues. It has a distinct N-terminus that is rich in positively charged amino acids, which is known as an electrolyte. This feature makes USP38 an ion-pairing partner that can interact with positively charged proteins in the cell, allowing it to participate in various cellular processes.

One of the unique features of USP38 is its specificity for a particular class of proteins known as ubiquitin-proteasome system (UPS) proteins. These proteins are involved in the degradation of damaged or dysfunctional proteins, and USP38 is specifically designed to target and degrade them. This property makes USP38 a potential drug target or biomarker for various diseases associated with protein homeostasis, such as neurodegenerative disorders, cancer, and diseases of the liver and pancreas.

The structure and function of USP38 are closely related to its ubiquitin-like activity. USP38 has a conserved catalytic core that is similar to that of other UPS proteins, and it has a distinct N-terminus that is involved in the formation of a covalent complex with its substrate proteins. This complex is formed by a process called suicide inhibition, which allows the substrate protein to be degraded by the ubiquitin-proteasome system.

Suicide inhibition is a critical mechanism that allows the UPS to function in a highly specific and efficient manner. It ensures that only correctly targeted proteins are degraded, and that the degradation process is carried out in a highly controlled manner. The ability of USP38 to form this complex and to participate in the UPS system is a unique feature that gives it its specificity and allows it to be a potential drug target or biomarker.

USP38 has been shown to play a role in a variety of cellular processes, including the regulation of protein homeostasis, cell signaling, and inflammation. For example, USP38 has been shown to be involved in the degradation of beta-amyloid peptides, which are a hallmark of Alzheimer's disease. This suggests that USP38 may have therapeutic potential for the treatment of Alzheimer's disease.

In addition to its role in the UPS, USP38 has also been shown to play a role in cell signaling and inflammation. It has been shown to be involved in the regulation of cell signaling pathways, including the TGF-beta pathway. This suggests that USP38 may have therapeutic potential for the treatment of various diseases associated with inflammation and cellular signaling, such as cancer and neurodegenerative disorders.

The specificity of USP38 as a drug target or biomarker is its ability to interact with positively charged proteins in the cell. This feature allows it to participate in a variety of cellular processes, including the regulation of protein homeostasis, cell signaling, and inflammation. It also allows it to be targeted with small molecules, which can be used to inhibit its activity and prevent the development of diseases associated with these processes.

In conclusion, USP38 is a protein that has important roles in the regulation of protein homeostasis, cell signaling, and inflammation. Its specificity as a UPS protein and its ability to interact with positively charged proteins make it a potential drug target or biomarker for a variety of diseases. Further research is needed to fully understand the mechanisms of its function and its potential as a therapeutic agent.

Protein Name: Ubiquitin Specific Peptidase 38

Functions: Deubiquitinating enzyme exhibiting a preference towards 'Lys-63'-linked ubiquitin chains

The "USP38 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 USP38 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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