KCNIP1: A Potential Drug Target and Biomarker (G30820)

Target Name: KCNIP1

NCBI ID: G30820

KCNIP1

KCNIP1: A Potential Drug Target and Biomarker

K cannon-pyruvate synthase (KCNIP1) is a gene that encodes a protein involved in the citric acid cycle, a critical metabolic pathway that generates energy in the form of ATP. Mutations in the KCNIP1 gene have been linked to various cellular and physiological processes, including energy metabolism, brain function, and cancer development. As a result, KCNIP1 has emerged as a promising drug target and biomarker for a variety of diseases.

The KCNIP1 gene is located on chromosome 16 and encodes a protein with 215 amino acid residues. The protein is composed of a N-terminal transmembrane domain, a catalytic domain, and a C-terminal cytoplasmic domain. The catalytic domain is responsible for the protein's catalytic activity and is the region where the majority of the protein's function is concentrated.

The KCNIP1 protein functions as a key player in the citric acid cycle, catalyzing the conversion of pyruvate to acetyl-CoA, a critical step in the cycle. This catalytic activity is critical for maintaining cellular energy homeostasis and for the production of ATP, which is the energy currency of the cell. Mammalian cells have two main types of mitochondria, each with its own set of genes that encode the proteins required for the citric acid cycle. These genes are responsible for maintaining the cellular energy homeostasis and for generating ATP through the citric acid cycle.

In addition to its role in the citric acid cycle, KCNIP1 has been shown to play a role in various cellular processes that are critical for cell survival. For example, studies have shown that mutations in the KCNIP1 gene are associated with a variety of cellular processes that are important for cell survival, including cell division, apoptosis, and stress resistance.

One of the most promising aspects of KCNIP1 as a drug target is its druggable nature. The catalytic domain of the protein is the most likely to be targeted by small molecules, such as drugs that can inhibit the activity of the enzyme. Several small molecules have been shown to interact with the catalytic domain of KCNIP1 and to inhibit its activity. These drugs have been shown to be effective in a variety of cellular and animal models of cancer, including inhibiting the growth of cancer cells, suppressing the formation of new blood vessels, and modulating cellular signaling pathways.

Another promising aspect of KCNIP1 is its potential as a biomarker for cancer. The cytoplasmic domain of the protein is the region where it is most likely to interact with the cellular environment and may be the best indicator of its expression levels. Several studies have shown that KCNIP1 is expressed in a variety of cancer types, including breast, lung, and ovarian cancer. Additionally, studies have shown that levels of KCNIP1 are often elevated in cancer cells compared to normal cells, making it a potential biomarker for cancer.

In conclusion, KCNIP1 is a gene that has been linked to a variety of cellular and physiological processes, including energy metabolism, cell division, and cancer development. Its catalytic domain makes it a promising drug target, and its expression is often elevated in cancer cells, making it a potential biomarker for cancer. Further research is needed to fully understand the role of KCNIP1 in these processes and to develop effective treatments for the prevention and treatment of various diseases.

Protein Name: Potassium Voltage-gated Channel Interacting Protein 1

Functions: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND1/Kv4.1 and KCND2/Kv4.2 currents. Increases the presence of KCND2 at the cell surface

The "KCNIP1 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 KCNIP1 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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