NHLRC1: A Protein Involved in Cellular Regulation and Disease

Target Name: NHLRC1

NCBI ID: G378884

NHLRC1

NHLRC1: A Protein Involved in Cellular Regulation and Disease

NHLRC1 (NHL repeat containing E3 ubiquitin protein ligase 1) is a protein that is expressed in various tissues throughout the body, including the brain, spleen, and kidney. It is a member of the ubiquitin gene family, which consists of 20 different proteins that play a critical role in the regulation of protein stability and degradation.

NHLRC1 is a 17-kDa protein that consists of 155 amino acid residues. It has a unique structure that is composed of a long N-terminal region that contains an E3 ubiquitin protein ligase domain, as well as a short C-terminal region that contains a conserved domain that is similar to the N-terminal region of other ubiquitin proteins.

The E3 ubiquitin protein ligase domain is a key component of NHLRC1's function. This domain consists of a single alpha-helices that is responsible for the formation of a covalent complex with target proteins. The E3 ubiquitin protein ligase domain is able to ubiquitinate ( polymerase) target proteins, which means it can add a ubiquitin tag to the target protein. This allows the target protein to be targeted for degradation via the ubiquitin-proteasome system.

NHLRC1 has been shown to play a critical role in the regulation of various cellular processes, including cell division, apoptosis (programmed cell death), and inflammation. For example, studies have shown that NHLRC1 is involved in the regulation of cell cycle progression, and that it is able to alter the levels of various cellular proteins in response to different environmental conditions.

In addition to its role in cellular regulation, NHLRC1 has also been shown to be involved in the development and progression of certain diseases. For example, studies have shown that NHLRC1 is involved in the development of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease . Additionally, NHLRC1 has also been shown to be involved in the regulation of inflammation, which is a critical factor in the development of many diseases, including cancer.

Given its involvement in so many different cellular processes, it is not surprising that NHLRC1 has generated a lot of interest as a potential drug target. Many researchers are actively searching for small molecules that can interact with the E3 ubiquitin protein ligase domain of NHLRC1 and enhance its function. This hope is based on the idea that drugs that can interact with NHLRC1 may be able to disrupt its ability to form covalent complexes with target proteins and inhibit its function in the ubiquitin-proteasome system.

In addition to its potential as a drug target, NHLRC1 has also been shown to be a potential biomarker for several diseases. For example, studies have shown that the levels of NHLRC1 are altered in the brains of individuals with certain neurological disorders, such as Alzheimer's disease and Parkinson's disease. Additionally, research has also shown that NHLRC1 is involved in the regulation of inflammation, which is a critical factor in the development of many diseases, including cancer.

Overall, NHLRC1 is a protein that has a significant impact on cellular regulation and has been shown to be involved in the development and progression of many different diseases. As a result, it is an attractive target for drug development and research. Further studies are needed to fully understand the role of NHLRC1 in cellular regulation and its potential as a drug and biomarker.

Protein Name: NHL Repeat Containing E3 Ubiquitin Protein Ligase 1

Functions: E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway

The "NHLRC1 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 NHLRC1 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