UHRF2: A Potential Drug Target and Biomarker (G115426)

Target Name: UHRF2

NCBI ID: G115426

UHRF2

UHRF2: A Potential Drug Target and Biomarker

Unlike most proteins, UHRF2 (Ultimate Reading Finger 2) is not a true protein. It is a non-coding RNA molecule that functions as a scaffold to recruit chromatin proteins to specific genomic regions. Despite its non-protein nature, UHRF2 has been shown to play a critical role in various cellular processes, including cell growth, differentiation, and genomic stability.

Recently, researchers have discovered that UHRF2 can also serve as a potential drug target and biomarker. Its unique structure and various post-transcriptional modifications, such as its ability to form a stable complex with histone H3 lysine 27 (H3K27), have led to the hypothesis that UHRF2 could be a valuable target for small molecule inhibitors.

In addition to its potential as a drug target, UHRF2 has also been shown to be a valuable biomarker for various diseases, including cancer, neurodegenerative diseases, and psychiatric disorders. Its expression has been observed in a wide range of tissues and has been associated with various cellular processes, including cell growth, migration, and apoptosis.

The identification of UHRF2 as a potential drug target and biomarker has important implications for both the pharmaceutical industry and basic science. The development of small molecule inhibitors targeting UHRF2 could lead to new treatments for various diseases. Additionally, its potential as a biomarker could be used to diagnose and monitor disease progression.

The Structure and Function of UHRF2

UHRF2 is a non-coding RNA molecule that was discovered through a combination of biochemical, genetic, and bioinformatic studies. It is approximately 200 nucleotides long and has a unique structure that includes a 5'-end that is rich in conserved amino acids residues, a 3'-end that is rich in conserved acidic and basic residues, and a middle region that is rich in hydrophobic and hydrophilic residues.

One of the most significant features of UHRF2 is its ability to form a stable complex with histone H3 lysine 27 (H3K27). This complex is composed of UHRF2, H3, and the histone-remodeling enzyme histone-modifying complex 1 (HMC1) [6 ]. The H3K27-UHRF2 complex is important for the regulation of gene expression and has been implicated in various cellular processes, including cell growth, apoptosis, and chromatin remodeling.

In addition to its role in chromatin remodeling, UHRF2 has also been shown to play a critical role in the regulation of cellular processes that are independent of its nuclear function, such as cell migration and the development of tissues. Its expression has been observed in various tissues, including brain, heart, liver, and muscle, and has been associated with processes such as cell migration, invasion, and metastasis.

UHRF2 as a Potential Drug Target

The unique structure and functions of UHRF2 make it an attractive target for small molecule inhibitors. Its ability to form a stable complex with H3K27 and its involvement in various cellular processes that are independent of its nuclear function make it a promising target for inhibitors that can modulate its activity without affecting its role in chromatin remodeling.

Recent studies have shown that UHRF2 is responsive to small molecule inhibitors that target its activity in various cellular processes, including the regulation of cell growth, apoptosis, and migration. For example, studies have shown that inhibitors of the tyrosine kinase p53 can inhibit UHRF2- H3K27

Protein Name: Ubiquitin Like With PHD And Ring Finger Domains 2

Functions: E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair (PubMed:15178429, PubMed:29506131, PubMed:27743347, PubMed:23404503). Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them (PubMed:27129234, PubMed:24813944). This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (By similarity). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thereby inducing G1 arrest (PubMed:15178429, PubMed:15361834, PubMed:21952639). Ubiquitinates also PCNP leading to its degradation by the proteasome (PubMed:14741369, PubMed:12176013). Plays an active role in DNA damage repair by ubiquitinating p21/CDKN1A leading to its proteosomal degradation (PubMed:29923055). Promotes also DNA repair by acting as an interstrand cross-links (ICLs) sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent activation (PubMed:30335751). Contributes to UV-induced DNA damage response by physically interacting with ATR in response to irradiation, thereby promoting ATR activation (PubMed:33848395)

The "UHRF2 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 UHRF2 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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