Target Name: USP19
NCBI ID: G10869
Review Report on USP19 Target / Biomarker Content of Review Report on USP19 Target / Biomarker
USP19
Other Name(s): Ubiquitin thioesterase 19 | Ubiquitin specific peptidase 19, transcript variant 1 | ubiquitin specific protease 19 | ubiquitin thiolesterase 19 | ZMYND9 | Zinc finger MYND domain-containing protein 9 | Deubiquitinating enzyme 19 | Ubiquitin specific protease 19 | Ubiquitin-specific-processing protease 19 | ubiquitin specific peptidase 19 | deubiquitinating enzyme 19 | UBP19_HUMAN | Ubiquitin thiolesterase 19 | Ubiquitin carboxyl-terminal hydrolase 19 (isoform 1) | ubiquitin-specific-processing protease 19 | zinc finger MYND domain-containing protein 9 | USP19 variant 1 | Ubiquitin carboxyl-terminal hydrolase 19 | KIAA0891 | ubiquitin thioesterase 19

USP19: A Potential Drug Target and Biomarker for Ubiquitin-Proteasome Complex (UPC) Involvement in Human Diseases

Introduction

The ubiquitin-proteasome (UPC) system is a complex protein biosynthesis and degradation pathway that plays a crucial role in various cellular processes, including DNA replication, virus infection, and cancer progression. Mutations in UPC components have been implicated in numerous diseases, including cancer , neurodegenerative disorders, and neuroinflammation. The USP19 gene, located on chromosome 19, has been identified as a potential drug target and biomarker for UPC involvement in human diseases.

USP19 and Ubiquitin

Ubiquitin is a 76-kDa protein that plays a central role in the regulation of protein stability and degradation. It is composed of two subunits, a 43-kDa alpha-subunit and a 26-kDa beta-subunit, that are held together by a disulfide bond. Ubiquitin can covalently bind to a wide variety of protein targets, often through its E1 domain, which consists of a single amino acid, lysine. This covalent binding is critical for the regulation of protein stability and degradation, as well as the assembly and disassembly of various protein-protein interactions.

In addition to its role in protein regulation, Ubiquitin is also involved in the formation of the ubiquitin-proteasome complex (UPC), a highly specialized protein degradation pathway that is responsible for the clearance of damaged or dysfunctional proteins. The UPC is composed of a series of highly conserved subunits, including the 26-kDa beta-subunit, which is the core component of the complex. The 26-kDa beta-subunit is responsible for the formation of the UPC and for the regulation of its assembly, disassembly, and activity.

USP19 and the UPC

The USP19 gene is located on chromosome 19 and encodes for the protein USP19. USP19 is a 21-kDa protein that is highly conserved at its amino acid sequence, with only four amino acid differences between its human and mouse counterparts. These differences include a single amino acid substitution in the N-terminus of the protein, which has implications for its stability and localization in the cell.

Expression and Localization

USP19 is expressed in a variety of tissues and cells, including the liver, pancreas, and neural tissues. It is also expressed in various cell types, including cancer cells, and has been shown to play a role in the development and progression of cancer. USP19 has been shown to localize to the endoplasmic reticulum (ER) and to play a role in the regulation of endoplasmic reticulum-associated protein (ER-associated protein) levels.

Drug Sensitivity and Inhibition

Several studies have investigated the drug sensitivity of USP19 and its potential as a drug target. USP19 has been shown to be sensitive to inhibitors of the protein kinase C (PKC), a known regulator of UPC activity. In addition, USP19 has been shown to be sensitive to inhibitors of the nucleotide-binding oligomerization domain (NBO domain), a known regulator of DNA replication and repair. These findings suggest that USP19 may be a potential drug target for diseases that are characterized by the disruption of the UPC.

Biomarker Assays

To further investigate the potential utility of USP19 as a drug target, several biomarker assays have been developed. One approach is to use Ubiquitin-proteasome assays, which can be used to measure the levels of Ubiquitin in cells and to assess the stability of damaged or dysfunctional proteins. These assays can be used to

Protein Name: Ubiquitin Specific Peptidase 19

Functions: Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked ubiquitin chains

The "USP19 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 USP19 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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