PSMD3: A promising drug target and biomarker for the 26S proteasome regulatory subunit S3

Target Name: PSMD3

NCBI ID: G5709

PSMD3

PSMD3: A promising drug target and biomarker for the 26S proteasome regulatory subunit S3

Introduction

Proteasomes are key protein structures that remove damaged or unnecessary proteins from cells, thereby maintaining cellular homeostasis. The 26S proteasome is a highly efficient proteasome that is responsible for regulating the proteasomal system in eukaryotic cells. The 26S proteasome regulatory subunit S3 is a key protein that interacts with the 26S proteasome and regulates its activity. The regulation of S3 by other proteins is a critical process that ensures the proper functioning of the proteasomal system.

PSMD3, also known as 26S proteasome regulatory subunit S3, is a protein that is expressed in various cell types of the human body. PSMD3 plays a crucial role in regulating the activity of the 26S proteasome. It functions as a scaffold to interact with the 26S proteasome, allowing it to recognize and bind to specific protein targets in the cell.

PSMD3 is a 26S proteasome regulatory subunit S3 that is composed of 21 kilodalton (kDa) of protein and 4 kDa of a N-terminal alpha helix. It has a calculated pI of 1.8 and a predicted localization in the cytoplasm. PSMD3 is expressed in various cell types, including the brain, heart, liver, and kidney.

PSMD3 functions as a negative regulator of the 26S proteasome. It has been shown to interact with several 26S proteasome subunits, including the 26S proteasome regulatory subunit S100, also known as the alpha-glutamyl-transferase (ATG) protein. The interaction between PSMD3 and S100 allows PSMD3 to regulate the activity of the 26S proteasome by inhibiting its activity.

PSMD3 has also been shown to interact with the protein ubiquitin. Ubiquitin is a ubiquitous protein that plays a crucial role in protein degradation and modification. The interaction between PSMD3 and ubiquitin allows PSMD3 to regulate the activity of ubiquitin, which is involved in protein degradation.

PSMD3 has been shown to play a role in the regulation of cellular processes such as cell growth, apoptosis, and inflammation. For example, studies have shown that PSMD3 can inhibit the activity of the 26S proteasome, leading to the accumulation of damaged or unnecessary proteins and the onset of cellular stress. This contributes to the regulation of cell growth, apoptosis, and inflammation.

PSMD3 is also a potential drug target in the development of various diseases. The regulation of the 26S proteasome by PSMD3 is a critical process that ensures the proper functioning of the proteasomal system. The dysregulation of PSMD3 has been implicated in the development of various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

PSMD3 has also been shown to be a potential biomarker for various diseases. The dysregulation of PSMD3 has been implicated in the development of various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. Therefore, the regulation of PSMD3 by other proteins is an important process that can be used as a biomarker for various diseases.

Conclusion

PSMD3 is a protein that plays a crucial role in the regulation of the 26S proteasome system. Its interaction with the 26S proteasome regulatory subunit S100 and the protein ubiquitin allows it to regulate the activity of the proteasome and ensure the proper functioning of the cell. The dysregulation of PSMD3 has

Protein Name: Proteasome 26S Subunit, Non-ATPase 3

Functions: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair

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