Target Name: RNF152
NCBI ID: G220441
Review Report on RNF152 Target / Biomarker Content of Review Report on RNF152 Target / Biomarker
RNF152
Other Name(s): RN152_HUMAN | RING-type E3 ubiquitin transferase RNF152 | ring finger protein 152 | RING finger protein 152 | Ring finger protein 152 | E3 ubiquitin-protein ligase RNF152

RNA-Nucleic Acid Binding Protein: RNF152 as A Potential Drug Target

RNA-Nucleic Acid (RNA) folding is a process that plays a crucial role in the development and regulation of various proteins. One of the key proteins involved in this process is RNA-Nucleic Acid (RNA-DNA) binding proteins, such as RNF152 (RN152_HUMAN). RNF152 is a nuclear protein that is expressed in various tissues and cells of the human body. Its function in the cell is not well understood, but it is known to be involved in the regulation of gene expression and DNA replication. As a drug target and biomarker, the study of RNF152 is of great interest to researchers.

RNF152 is a member of the RNA-DNA binding family, which includes proteins such as TRIM22 and p167. These proteins share a conserved domain that includes a nucleotide-binding oligomerization (NBO) domain, a conserved core domain, and a C-terminal Tudor domain. The NBO domain is responsible for the protein's nuclear localization and is involved in the formation of RNA-DNA binding interactions. The conserved core domain is involved in the formation of the protein's stability and functions, while the C-terminal Tudor domain is involved in the protein's interactions with other cellular components.

RNA-DNA binding proteins have been implicated in various cellular processes, including DNA replication, gene expression, and chromosomal stability. They have also been implicated in the development and progression of various diseases, including cancer. Therefore, the study of RNF152 and its potential as a drug target is of great interest.

One of the functions of RNF152 is its role in the regulation of gene expression. RNA-DNA binding proteins have been shown to play a role in the regulation of gene expression by binding to specific DNA sequences and modulating the activity of RNA polymerase. In the case of RNF152, studies have shown that it can interact with specific DNA sequences and regulate the activity of RNA polymerase. This interaction between RNF152 and DNA sequences suggests that it may be a potential drug target.

Another function of RNF152 is its role in the regulation of DNA replication. RNA-DNA binding proteins have been shown to play a role in the regulation of DNA replication by binding to specific DNA sequences and modulating the activity of DNA replication factors. In the case of RNF152, studies have shown that it can interact with specific DNA sequences and regulate the activity of DNA replication factors. This interaction between RNF152 and DNA sequences suggests that it may be a potential drug target.

In addition to its role in the regulation of gene expression and DNA replication, RNF152 has also been shown to play a role in the regulation of chromosomal stability. RNA-DNA binding proteins have been shown to play a role in the regulation of chromosomal stability by binding to specific DNA sequences and modulating the activity of chromosomal stability factors. In the case of RNF152, studies have shown that it can interact with specific DNA sequences and regulate the activity of chromosomal stability factors. This interaction between RNF152 and DNA sequences suggests that it may be a potential drug target.

Overall, the study of RNF152 is of great interest as a potential drug target and biomarker. Its function in the regulation of gene expression, DNA replication, and chromosomal stability suggests that it may be a useful target for small molecule inhibitors. Further research is needed to fully understand the functions of RNF152 and its potential as a drug target.

Protein Name: Ring Finger Protein 152

Functions: E3 ubiquitin-protein ligase mediating 'Lys-63'-linked polyubiquitination of RRAGA in response to amino acid starvation. Thereby, regulates mTORC1 signaling and plays a role in the cellular response to amino acid availability (PubMed:25936802). Also mediates 'Lys-48'-linked polyubiquitination of target proteins and their subsequent targeting to the proteasome for degradation. Induces apoptosis when overexpressed (PubMed:21203937)

The "RNF152 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 RNF152 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

More Common Targets

RNF157 | RNF157-AS1 | RNF165 | RNF166 | RNF167 | RNF168 | RNF169 | RNF17 | RNF170 | RNF175 | RNF180 | RNF181 | RNF182 | RNF183 | RNF185 | RNF186 | RNF187 | RNF19A | RNF19B | RNF2 | RNF20 | RNF207 | RNF208 | RNF212 | RNF212B | RNF213 | RNF213-AS1 | RNF214 | RNF215 | RNF216 | RNF216-IT1 | RNF216P1 | RNF217 | RNF217-AS1 | RNF220 | RNF222 | RNF224 | RNF225 | RNF227 | RNF24 | RNF25 | RNF26 | RNF31 | RNF32 | RNF32-DT | RNF34 | RNF38 | RNF39 | RNF4 | RNF40 | RNF41 | RNF43 | RNF44 | RNF5 | RNF5P1 | RNF6 | RNF7 | RNF7P1 | RNF8 | RNFT1 | RNFT2 | RNGTT | RNH1 | RNLS | RNMT | RNPC3 | RNPC3-DT | RNPEP | RNPEPL1 | RNPS1 | RNPS1P1 | RNR1 | RNR2 | RNU1-1 | RNU1-100P | RNU1-108P | RNU1-11P | RNU1-134P | RNU1-18P | RNU1-3 | RNU1-31P | RNU1-32P | RNU1-36P | RNU1-38P | RNU1-4 | RNU1-42P | RNU1-55P | RNU1-61P | RNU1-63P | RNU1-72P | RNU1-73P | RNU1-78P | RNU1-7P | RNU1-82P | RNU1-88P | RNU105B | RNU11 | RNU12 | RNU2-1 | RNU2-17P