RPS27A: A Protein Regulator of Cell Division and Cellular Processes

Target Name: RPS27A

NCBI ID: G6233

RPS27A

RPS27A: A Protein Regulator of Cell Division and Cellular Processes

Ubiquitin-CEP52 (RPS27A) is a protein that plays a critical role in the regulation of cell division and the turnover of cellular components. It is a key player in the ubiquitin system, a network of proteins that work together to tag and transport damaged or dysfunctional proteins to the end of the cell. RPS27A is a 27-kDa protein that is composed of two heavy chains and two light chains. It is expressed in most tissues of the body and is involved in various cellular processes, including cell division, apoptosis, and inflammation.

One of the unique features of RPS27A is its ability to interact with other proteins and molecules. It has multiple interaction sites, including interaction with DNA, RNA, protein tyros, and histones. These interactions play a critical role in the regulation of cellular processes, including DNA replication, gene expression, and cell division.

In addition to its role in cellular processes, RPS27A is also a potential drug target. Its interaction with other proteins and molecules makes it a potential target for small molecules and antibodies that can modulate its activity. For example, some studies have suggested that inhibiting RPS27A activity may have therapeutic benefits for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

Another potential application of RPS27A is its use as a biomarker. Its expression is often reduced in diseases, including cancer, and its levels can be used as a diagnostic marker for disease. For example, studies have shown that RPS27A expression is often reduced in various types of cancer, including breast, ovarian, and prostate cancer. This suggests that RPS27A may be a useful biomarker for these diseases.

Finally, RPS27A is also a target for CRISPR/Cas9 genome editing. The ubiquitin system plays a critical role in the regulation of gene expression, and RPS27A is involved in the ubiquitin-proteasome system, which is the major mechanism for removing damaged or dysfunctional proteins from the cell. By targeting RPS27A with CRISPR/Cas9, researchers may be able to introduce mutations or other genetic changes into the protein that could be used to treat or prevent various diseases.

In conclusion, RPS27A is a protein that plays a critical role in the regulation of cell division and the turnover of cellular components. Its multiple interaction sites and its ability to modulate the activity of other proteins make it a potential drug target and a useful biomarker for various diseases. Additionally, RPS27A is also a target for CRISPR/Cas9 genome editing, which may be used to introduce mutations or other genetic changes into the protein. Further research is needed to fully understand the role of RPS27A in cellular processes and its potential as a drug target and biomarker.

Protein Name: Ribosomal Protein S27a

Functions: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling

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•   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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