RPS27P22: A Promising Drug Target / Biomarker (G100131418)

Target Name: RPS27P22

NCBI ID: G100131418

RPS27P22

Other Name(s): Ribosomal protein S27 pseudogene 22 | RPS27_12_1218 | ribosomal protein S27 pseudogene 22

RPS27P22: A Promising Drug Target / Biomarker

The protein RPS27P22 is a key regulator of the Parlay domain in the RNA polymerase II complex, which is responsible for DNA replication in eukaryotic cells. The Parlay domain is a transmembrane protein that contains multiple nucleotide-binding oligomerization (NBO) domains, which are involved in protein-DNA interactions and are thought to play a role in the regulation of gene expression. RPS27P22 is a 22-kDa protein that is predominantly localized to the endoplasmic reticulum (ER) and is involved in the regulation of DNA replication, cell growth, and apoptosis.

The RPS27P22 protein is composed of a NBO1 domain, a NBO2 domain, and a NBO3 domain. The NBO1 and NBO2 domains are responsible for the protein's nucleotide-binding activity, while the NBO3 domain is involved in the protein's stability and functions as a negative regulator of the Parlay domain.

The NBO1 domain is a 63- amino acid protein that contains a nucleotide-binding oligomerization (NBO) domain and a protein-DNA interaction domain. The NBO1 domain is responsible for the protein's nucleotide-binding activity and is involved in the regulation of DNA replication. The NBO2 domain is a 21- amino acid protein that contains a nucleotide-binding oligomerization (NBO) domain and a protein-DNA interaction domain. The NBO2 domain is responsible for the protein's nucleotide-binding activity and is involved in the regulation of DNA replication. The NBO3 domain is a 12- amino acid protein that is responsible for the protein's stability and functions as a negative regulator of the Parlay domain.

The RPS27P22 protein plays a critical role in the regulation of DNA replication in eukaryotic cells. During DNA replication, the RPS27P22 protein is involved in the formation of the double helix and the recruitment of the necessary enzymes for the replication process. The RPS27P22 protein is also involved in the regulation of DNA repair, which is a critical process for the maintenance of genetic integrity in the cell.

The RPS27P22 protein is also involved in the regulation of cell growth and apoptosis. The RPS27P22 protein is a negative regulator of the Parlay domain, which means that it functions as an inhibitor of the Parlay domain's ability to bind to DNA. This function is important for the regulation of cell growth and apoptosis, as it allows the RPS27P22 protein to prevent the uncontrolled growth of cells.

The RPS27P22 protein is also involved in the regulation of inflammation. The RPS27P22 protein is a key regulator of the NF-kappa-B signaling pathway, which is a critical pathway involved in the regulation of inflammation and immune responses. The RPS27P22 protein is involved in the regulation of the NF-kappa-B signaling pathway by preventing the NF-kappa-B protein from interacting with the Parlay domain. This function is important for the regulation of inflammation, as it allows the RPS27P22 protein to prevent the uncontrolled growth of cells that could contribute to inflammation.

The RPS27P22 protein is also involved in the regulation of metabolism. The RPS27P22 protein is a regulator of the cellular metabolism, it is involved in the metabolism of glucose and lipids. This function is important for the regulation of metabolism, as it allows the RPS27P22 protein to regulate the amount of glucose and lipids that are available to the cell.

The RPS27P22 protein is also involved in the regulation of

Protein Name: Ribosomal Protein S27 Pseudogene 22

The "RPS27P22 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 RPS27P22 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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