USP7: A Protein At The Center of Cell Signaling Pathways and Disease Development

Target Name: USP7

NCBI ID: G7874

USP7

USP7: A Protein At The Center of Cell Signaling Pathways and Disease Development

USP7 (Unconventional Signaling Pathway 7) is a protein that is expressed in various tissues throughout the body. It is a key regulator of cell signaling pathways and has been implicated in a wide range of biological processes. While USP7 has been studied extensively, much of its biology remains poorly understood.

One of the key functions of USP7 is its role in cell signaling pathways. USP7 is a component of several signaling pathways that are involved in a wide range of biological processes, including cell growth, differentiation, and inflammation. It is well known that USP7 plays a key role in the regulation of T cell development and function, and that it is involved in the development of cancer.

Another function of USP7 is its role in the regulation of cell adhesion. USP7 is involved in the formation of tight junctions, which are critical for the proper functioning of cells and are involved in various signaling pathways. It is also involved in the regulation of cell-cell adhesion, which is important for the development and maintenance of tissues and organs.

In addition to its role in cell signaling pathways and cell adhesion, USP7 is also involved in the regulation of inflammation. It is a key regulator of the production of pro-inflammatory cytokines, and it is involved in the regulation of the immune response.

Given its involvement in a wide range of biological processes, USP7 is a promising drug target. Researchers have identified several potential small molecules that can inhibit USP7 activity, and these molecules have been tested in a variety of preclinical models. Some of the most promising candidates for USP7 inhibitors include compounds that are derived from natural compounds, such as those found in plants and animals, as well as compounds that are synthesized artificially.

In addition to its potential as a drug, USP7 is also an attractive biomarker for the study of various diseases. Given its involvement in a wide range of biological processes, it is possible that USP7 may be involved in the development of many different diseases. For example, USP7 is involved in the regulation of cell signaling pathways, which are critical for the development and maintenance of tissues and organs. As such, it is possible that USP7 may be involved in the development of many different diseases, including cancer, autoimmune diseases, and neurodegenerative diseases.

Overall, USP7 is a protein that has significant involvement in a wide range of biological processes, and as such, it is a promising drug target and a promising biomarker for the study of various diseases. Further research is needed to fully understand the role of USP7 in these processes and to develop effective treatments for the prevention and treatment of its various diseases.

Protein Name: Ubiquitin Specific Peptidase 7

Functions: Hydrolase that deubiquitinates target proteins such as FOXO4, KAT5, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148, PubMed:25865756, PubMed:26678539, PubMed:28655758). Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation (PubMed:15053880, PubMed:16845383, PubMed:18566590, PubMed:20153724). Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell growth repression and apoptosis (PubMed:25283148). Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis (PubMed:11923872, PubMed:26786098). Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity (PubMed:16964248). In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML (PubMed:18716620). Deubiquitinates KMT2E/MLL5 preventing KMT2E/MLL5 proteasomal-mediated degradation (PubMed:26678539). Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6 (PubMed:22466611, PubMed:22466612). Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1 (PubMed:21745816, PubMed:22411829). Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111). Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex (PubMed:20601937). Able to mediate deubiquitination of histone H2B; it is however unsure whether this activity takes place in vivo (PubMed:20601937). Exhibits a preference towards 'Lys-48'-linked ubiquitin chains (PubMed:22689415). Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222). Plays a role in the maintenance of the circadian clock periodicity via deubiquitination and stabilization of the CRY1 and CRY2 proteins (PubMed:27123980). Deubiquitinates REST, thereby stabilizing REST and promoting the maintenance of neural progenitor cells (PubMed:21258371). Deubiquitinates SIRT7, inhibiting SIRT7 histone deacetylase activity and regulating gluconeogenesis (PubMed:28655758). Involved in the regulation of WASH-dependent actin polymerization at the surface of endosomes and the regulation of endosomal protein recycling (PubMed:26365382). It maintains optimal WASH complex activity and precise F-actin levels via deubiquitination of TRIM27 and WASHC1 (PubMed:26365382)

The "USP7 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 USP7 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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