Target Name: Proteasome 20S
NCBI ID: P13009
Review Report on Proteasome 20S Target / Biomarker Content of Review Report on Proteasome 20S Target / Biomarker
Proteasome 20S
Other Name(s): 20S Core | 20S core particle

P200, A Potential Drug Target and Biomarker for Various Diseases

Proteasome 20S (20S Core), also known as P200, is a protein that is found in the endoplasmic reticulum (ER) and is involved in the regulation of protein interactions and degradation. P200 has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

The 20S Core is a subunit of the proteasome, which is a complex protein that plays a crucial role in regulating protein synthesis in the cell. The proteasome is composed of a large protein known as the 20S subunit and smaller proteins known as the 6.2S and 17S subunits. The 20S subunit is responsible for recognizing and interacting with target proteins, which are then degraded in the cytosol.

P200 is a 20S subunit that contains a unique N-terminus and a unique C-terminus. The N-terminus of P200 contains a nucleotide acid sequence that is similar to the active site of the proteasome, which suggests that it may be involved in protein -protein interactions that regulate the activity of the proteasome. The C-terminus of P200 contains a unique glycine residue, which is also known as a glycine tail, which is involved in protein-protein interactions and may be a potential binding site for small molecules or other proteins.

P200 has been shown to play a role in the regulation of protein interactions and degradation in various cell types. For example, studies have shown that P200 can interact with the protein known as N-terminal-pro-Q2 (N-Q2), which is a component of the endoplasmic reticulum-associated protein (ER-associated protein) family. N-Q2 is a transmembrane protein that is involved in the regulation of protein folding and degradation, and it has been shown to interact with various proteins, including P200.

In addition to its role in protein-protein interactions, P200 has also been shown to play a role in the regulation of protein degradation. Studies have shown that P200 can interact with the protein known as calbindin, which is a calcium-binding protein that is involved in the regulation of protein stability and degradation. Calbindin has been shown to interact with P200 and can enhance the degradation of various proteins, including the protein known as p53, which is a well-known tumor suppressor protein.

P200 has also been shown to play a role in the regulation of protein synthesis and translation. Studies have shown that P200 can interact with the protein known as translation factor 1 (TF-1), which is a protein that is involved in the regulation of protein synthesis and translation. TF-1 has been shown to interact with P200 and can enhance the stability of various proteins, including the protein known as ribosomal subunit alpha (rRNA), which is a component of the ribosome.

In conclusion, P200 is a protein that is involved in the regulation of protein interactions and degradation. It has been shown to interact with various proteins, including N-Q2, calbindin, and TF-1. Its unique N-terminus and C-terminus , as well as its ability to enhance the degradation of various proteins, make it a potential drug target and biomarker for various diseases. Further research is needed to fully understand the role of P200 in the regulation of protein interactions and degradation.

Protein Name: Proteasome 20S

The "Proteasome 20S 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 Proteasome 20S 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

Proteasome 26S | Proteasome Complex | Protein arginine N-methyltransferase | Protein disulfide-isomerase | Protein farnesyltransferase | Protein geranylgeranyltransferase type II | Protein kinase C | Protein Kinase D (PKD) | Protein kinase N | Protein NDRG2 (isoform a) | Protein Phosphatase | Protein Phosphatase 2A | Protein Phosphatase 2B | Protein phosphatase 6 | Protein phosphatase-1 | Protein transport protein Sec61 complex | Protein Tyrosine Phosphatase (PTP) | Protein Tyrosine Phosphatase Type IVA | Protein-Synthesizing GTPase (Elongation Factor) | Protocadherin | PROX1 | PROX1-AS1 | PROX2 | PROZ | PRPF18 | PRPF19 | PRPF3 | PRPF31 | PRPF38A | PRPF38B | PRPF39 | PRPF4 | PRPF40A | PRPF40B | PRPF4B | PRPF6 | PRPF8 | PRPH | PRPH2 | PRPS1 | PRPS1L1 | PRPS2 | PRPSAP1 | PRPSAP2 | PRR11 | PRR12 | PRR13 | PRR13P1 | PRR13P3 | PRR14 | PRR14L | PRR15 | PRR15L | PRR16 | PRR18 | PRR19 | PRR20B | PRR20C | PRR20D | PRR21 | PRR22 | PRR23A | PRR23B | PRR23C | PRR23D1 | PRR23E | PRR25 | PRR27 | PRR29 | PRR3 | PRR30 | PRR32 | PRR34 | PRR34-AS1 | PRR35 | PRR36 | PRR4 | PRR5 | PRR5-ARHGAP8 | PRR5L | PRR7 | PRR7-AS1 | PRR9 | PRRC1 | PRRC2A | PRRC2B | PRRC2C | PRRG1 | PRRG2 | PRRG3 | PRRG4 | PRRT1 | PRRT2 | PRRT3 | PRRT3-AS1 | PRRT4 | PRRX1 | PRRX2 | PRSS1 | PRSS12