Target Name: SENP3
NCBI ID: G26168
Review Report on SENP3 Target / Biomarker Content of Review Report on SENP3 Target / Biomarker
SENP3
Other Name(s): SUMO-1-specific protease 3 | SMT3IP1 | SSP3 | SUSP3 | SUMO1/sentrin/SMT3 specific peptidase 3 | Sentrin/SUMO-specific protease 3 | Sentrin/SUMO-specific protease 3 (SENP3) | Sentrin-specific protease 3 | SUMO specific peptidase 3 | Sentrin/SUMO-specific protease SENP3 | sentrin/SUMO-specific protease 3 | SENP3_HUMAN | Ulp1

SENP3: A Potential Drug Target and Biomarker for SUMO-1-Specific Protease 3

SUMO-1-specific protease 3 (SENP3) is a protein that plays a crucial role in the regulation of protein-protein interactions, which is a critical process in various biological processes. The SENP3 gene has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

SENP3: The Enigma of Protein-Protein Interactions

Protein-protein interactions (PPIs) are the interactions between two or more proteins that are involved in various cellular processes, including signaling, regulation of cell division, and tissue structure. These interactions are regulated by a variety of factors, including SENP3.

SENP3 is a 23-kDa protein that is expressed in various tissues and cells, including the brain, pancreas, and muscle. It is composed of 116 amino acid residues and has a calculated pI of 6.9. SENP3 is involved in the regulation of PPIs by a unique mechanism, which involves the formation of a covalent complex with a specific protein, called SUMO-1.

SUMO-1: The Unveiled Partner of SENP3

SUMO-1 is a small protein that belongs to the N-end domain superfamily (N-end rule-mediated protein-protein interactions) and is expressed in various tissues and cells. SUMO-1 is involved in the regulation of various cellular processes, including cell signaling, cell division, and tissue structure.

The SUMO-1 gene has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. SUMO-1 has been shown to play a role in the regulation of PPIs by SENP3, which suggests that SENP3 may be a promising drug target for various diseases.

SENP3 as a Drug Target: Potential and Limitations

SENP3 has been shown to be involved in the regulation of PPIs by SUMO-1, which suggests that it may be a potential drug target for various diseases. One of the main potential targets of SENP3 is cancer, where SENP3 has been shown to promote the growth and survival of various cancer cell types.

SENP3 has also been shown to be involved in the regulation of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. These diseases are characterized by the progressive loss of brain cells and can cause a range of symptoms, including cognitive impairment and motor dysfunction.

SENP3 has also been shown to be involved in the regulation of autoimmune disorders, such as rheumatoid arthritis and multiple sclerosis. These disorders are characterized by the immune system attacking the body's own tissues, leading to inflammation and joint damage.

Making SENP3 a Promising Biomarker: Potential and Limitations

SENP3 has also been shown to be involved in the regulation of various cellular processes, including cell signaling, cell division, and tissue structure. This suggests that it may be a promising biomarker for various diseases.

One of the main potential applications of SENP3 as a biomarker is its potential to diagnose and monitor the effectiveness of various therapeutic treatments. For example, SENP3 levels have been shown to be regulated in response to various therapeutic treatments, which could be used as a biomarker to track the effectiveness of these treatments.

SENP3 has also been shown to be involved in the regulation of cellular processes that are associated with aging, such as the accumulation of intracellular aggregates and the disruption of cellular home

Protein Name: SUMO Specific Peptidase 3

Functions: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates (PubMed:16608850, PubMed:32832608). Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability (PubMed:15743823). Deconjugates SUMO2 and SUMO3 from CDCA8 (PubMed:18946085). Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300 (PubMed:19680224). Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1 (PubMed:19015314). Plays a role in the regulation of sumoylation status of ZNF148 (PubMed:18259216). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Deconjugates SUMO2 from KAT5 (PubMed:32832608)

The "SENP3 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 SENP3 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

SENP3-associated complex | SENP3-EIF4A1 | SENP5 | SENP6 | SENP7 | SENP8 | SEPHS1 | SEPHS1P4 | SEPHS1P6 | SEPHS2 | SEPSECS | SEPSECS-AS1 | SEPT5-GP1BB | SEPTIN1 | SEPTIN10 | SEPTIN11 | SEPTIN12 | SEPTIN14 | SEPTIN2 | SEPTIN3 | SEPTIN4 | SEPTIN4-AS1 | SEPTIN5 | SEPTIN6 | SEPTIN7 | SEPTIN7-DT | SEPTIN7P11 | SEPTIN7P14 | SEPTIN7P2 | SEPTIN7P6 | SEPTIN7P9 | SEPTIN8 | SEPTIN9 | SERAC1 | SERBP1 | SERBP1P3 | SERF1A | SERF1B | SERF2 | SERF2-C15ORF63 | SERGEF | SERHL | SERINC1 | SERINC2 | SERINC3 | SERINC4 | SERINC5 | Serine (or cysteine) proteinase inhibitor clade F | Serine palmitoyltransferase | Serine protease | Serine protease inhibitor | Serine-aspartate repeat-containing protein I-like | SERP1 | SERP2 | SERPINA1 | SERPINA10 | SERPINA11 | SERPINA12 | SERPINA13P | SERPINA2 | SERPINA3 | SERPINA4 | SERPINA5 | SERPINA6 | SERPINA7 | SERPINA9 | SERPINB1 | SERPINB10 | SERPINB11 | SERPINB12 | SERPINB13 | SERPINB2 | SERPINB3 | SERPINB4 | SERPINB5 | SERPINB6 | SERPINB7 | SERPINB8 | SERPINB9 | SERPINB9-AS1 | SERPINB9P1 | SERPINC1 | SERPIND1 | SERPINE1 | SERPINE2 | SERPINE3 | SERPINF1 | SERPINF2 | SERPING1 | SERPINH1 | SERPINI1 | SERPINI2 | SERTAD1 | SERTAD2 | SERTAD3 | SERTAD4 | SERTAD4-AS1 | SERTM1 | SERTM2 | Serum amyloid protein