UBR2: A Potential Drug Target and Biomarker for the Treatment of Various Diseases

Target Name: UBR2

NCBI ID: G23304

UBR2

UBR2: A Potential Drug Target and Biomarker for the Treatment of Various Diseases

Introduction

Unfolded proteins play a crucial role in various cellular processes and are involved in many diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. One of the key proteins involved in the regulation of protein stability is ubiquitin (U), which is a protein that plays a central role in the ubiquitination and degradation of proteins. UBR2, a member of the ubiquitin-protein ligase (UPL) family, is an essential enzyme that regulates the activity of U for the ubiquitination of target proteins. In this article, we discuss the potential drug target and biomarker properties of UBR2, highlighting its unique function in cellular processes and its potential as a therapeutic agent for various diseases.

Structure and Function of UBR2

UBR2 is a 26 kDa protein that is composed of 218 amino acid residues. It belongs to the family of UPLs and is responsible for the catalytic activation of U for ubiquitination. The protein has a distinct N-terminal region that contains a nucleotide-binding oligomerization domain (NBO), which is responsible for the interaction with U's active site. The NBO is a domain that contains a nucleotide-binding oligomerization motif (NBM) and is responsible for the recruitment of U's substrate protein onto the protein.

The central region of UBR2 contains a parallel beta-sheet structure, which is characteristic of the UPLs. The sheet is composed of three beta-helical subdomains that give the protein its beta-sheet architecture. The beta-sheet is responsible for the stability of the protein and is involved in the regulation of its activity. The sheet is also involved in the formation of the protein-protein interaction, which is an important aspect of protein function.

The C-terminus of UBR2 contains a C-terminal domain that is responsible for the protein's stability and modification. This domain has been shown to play a role in the regulation of protein stability and has been implicated in the development of various diseases, including cancer.

Function of UBR2

UBR2 is involved in the regulation of protein stability by ubiquitination. Ubiquitination is the process by which proteins are covalently linked to the ubiquitin molecule, which can either promote or ubiquitinate the target protein. UBR2 plays a key role in the ubiquitination of target proteins by interacting with the protein and activating its ubiquitinylation state.

The activity of UBR2 is regulated by several factors, including the concentration of U, the temperature, and the pH. UBR2 has a Michaelis-Menten kinetics, which means that its activity increases with increasing U concentration and decreasing pH. The protein also has a significant affinity for its substrate, which is reflected by its high substrate specificity.

UBR2 has been shown to play a role in the regulation of various cellular processes, including cell growth, apoptosis, and autophagy. In addition, UBR2 has been implicated in the development of various diseases, including cancer.

Drug Targeting and Biomarker Properties

The potential drug targeting of UBR2 comes from its involvement in the regulation of protein stability and its association with various diseases. UBR2 has been shown to play a role in the regulation of cancer cell growth, apoptosis, and autophagy, making it an attractive target for cancer therapies.

One of the most promising strategies for targeting UBR2 is the inhibition of its activity by small molecules. A variety of small molecules have been shown to inhibit the activity of UBR2, including inhibitors of the NBO domain and the C-terminus domain. These inhibitors have been shown to reduce the ubiquitination of various proteins, including

Protein Name: Ubiquitin Protein Ligase E3 Component N-recognin 2

Functions: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (PubMed:15548684, PubMed:20835242). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A (By similarity). Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (PubMed:20298436). Required for spermatogenesis, promotes, with Tex19.1, SPO11-dependent recombination foci to accumulate and drive robust homologous chromosome synapsis (By similarity). Polyubiquitinates LINE-1 retrotransposon encoded, LIRE1, which induces degradation, inhibiting LINE-1 retrotransposon mobilization (By similarity). Catalyzes ubiquitination and degradation of the N-terminal part of NLRP1 following NLRP1 activation by pathogens and other damage-associated signals: ubiquitination promotes degradation of the N-terminal part and subsequent release of the cleaved C-terminal part of NLRP1, which polymerizes and forms the NLRP1 inflammasome followed by host cell pyroptosis (By similarity)

The "UBR2 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 UBR2 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;
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•   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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