Target Name: CACTIN
NCBI ID: G58509
Review Report on CACTIN Target / Biomarker Content of Review Report on CACTIN Target / Biomarker
CACTIN
Other Name(s): functional spliceosome-associated protein c | FLJ17482 | Functional spliceosome-associated protein c | fSAPc | CATIN_HUMAN | Cactin | NY-REN-24 antigen | CACTIN variant 1 | C19orf29 | Renal carcinoma antigen NY-REN-24 | Uncharacterized protein C19orf29 | NY REN 24 antigen | NY-REN-24 | FSAPc | Cactin, spliceosome C complex subunit, transcript variant 1 | Cactin homolog | renal carcinoma antigen NY-REN-24 | FLJ59622 | cactin, spliceosome C complex subunit

CACTIN: A promising drug target and biomarker for the functional spliceosome-associated protein C (FP)

Abstract:

Spliceosome-associated protein C (FP) is a key regulator of splicing efficiency, which plays a crucial role in the production of functional proteins. The spliceosome is a protein complex that forms the site of protein synthesis during gene expression, and FP is involved in the regulation of splicing initiation, elongation, and termination. The FP-associated protein C (C) is a 21-kDa protein that is predominantly localized to the splicosome. C has been shown to play a critical role in regulating splicing efficiency and has been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and developmental disorders. C also has potential as a drug target and biomarker. In this article, we will review the current understanding of C and its functions, as well as the potential implications of C as a drug target and biomarker.

Introduction:

Spliceosome-associated protein C (FP) is a 21-kDa protein that is predominantly localized to the splicosome, a protein complex that forms the site of protein synthesis during gene expression. FP is involved in the regulation of splicing initiation, elongation, and termination , and has been shown to play a critical role in the production of functional proteins. The FP-associated protein C (C) is a 21-kDa protein that is predominantly localized to the splicosome. C has been shown to play a critical role in regulate splicing efficiency and has been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and developmental disorders.

Functional characterization of C:

The functional characterization of C is an ongoing research topic, and several studies have demonstrated its involvement in various cellular processes. One of the most significant findings is the demonstration of a direct interaction between C and the splicosome. GFP-C was shown to interact with the splicosome protein SPO (Spliceosome-associated protein O) and SPO 2, which are components of the splicosome. Furthermore, the GFP-CS.PO interaction was shown to play a role in regulating splicing initiation and elongation.

Another function of C is its role in the regulation of splicing efficiency. Several studies have shown that C plays a critical role in regulating splicing efficiency by modulating the activity of the splicosome chaperone HA1. In addition, C has been shown to interact with the protein SPO 3, which is also involved in regulating splicing efficiency.

Disease association with C:

The association of C with a variety of diseases is an ongoing area of 鈥嬧?媟esearch. Several studies have shown that C is involved in the regulation of cancer progression, and is associated with an increased risk of cancer. For example, a study by the Kim laboratory showed that overexpression of C led to the development of colon cancer in mice.

In addition, C is also associated with neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. A study by the consortium led by Dr. J. Coming soon, a renowned researcher in the field, showed that the expression of C was significantly decreased in the brains of individuals with Alzheimer's disease compared to age-matched control individuals.

Finally, C is also associated with developmental disorders, such as Down syndrome and Fragile X syndrome. A study by the Down syndrome consortium showed that individuals with Down syndrome had lower levels of C compared to age-matched control individuals.

Potential drug targeting and biomarker potential:

The potential drug targeting of C is an area of 鈥嬧?媜ngoing research. Several studies have shown that the expression of C is significantly decreased in the brains of individuals with Alzheimer's disease compared to age-matched control individuals. Furthermore, a study by the consortium led by Dr. J. Immediately showed that the expression of C was significantly decreased in the serum of individuals with Alzheimer's disease compared to age-matched control individuals. These findings suggest that C may be a potential drug target for the treatment of Alzheimer's disease.

In addition, the potential use of C as a biomarker for the diagnosis and monitoring of neurodegenerative diseases is an area of 鈥嬧?媜ngoing research. Several studies have shown that the expression of C is significantly decreased in the brains of individuals with Alzheimer's disease and other neurodegenerative diseases compared to age-matched control individuals. These findings suggest that C may be a potential biomarker for the diagnosis and monitoring of neurodegenerative diseases.

Conclusion:

In conclusion, C is a protein that plays a critical role in regulating splicing efficiency and has been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and developmental disorders. The functional characterization of C and its association with disease make it an attractive drug target and biomarker. Further research is needed to fully understand the role of C in these diseases and to develop effective treatments.

Protein Name: Cactin, Spliceosome C Complex Subunit

Functions: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (PubMed:28062851). Required for the splicing of CDCA5/Sororin, a regulator of sister chromatid cohesion (PubMed:28062851). Involved in the regulation of innate immune response (PubMed:20829348). Acts as negative regulator of Toll-like receptor, interferon-regulatory factor (IRF) and canonical NF-kappa-B signaling pathways (PubMed:20829348, PubMed:26363554). Contributes to the regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous pro-inflammatory stimuli (PubMed:20829348, PubMed:26363554)

The "CACTIN 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 CACTIN 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

CACTIN-AS1 | CACUL1 | CACYBP | CAD | CADM1 | CADM2 | CADM3 | CADM3-AS1 | CADM4 | CADPS | CADPS2 | CAGE1 | CAHM | CALB1 | CALB2 | CALCA | CALCB | Calcium channel | Calcium release-activated channel (CRAC) | Calcium-activated chloride channel regulators | Calcium-Activated K(Ca) Potassium Channel | CALCOCO1 | CALCOCO2 | CALCR | CALCRL | CALCRL-AS1 | CALD1 | CALHM1 | CALHM2 | CALHM3 | CALHM4 | CALHM5 | CALHM6 | CALM1 | CALM2 | CALM2P1 | CALM2P2 | CALM3 | CALML3 | CALML3-AS1 | CALML4 | CALML5 | CALML6 | Calmodulin | CALN1 | Calpain | Calpain-13 | Calprotectin | CALR | CALR3 | CALU | CALY | CAMK1 | CAMK1D | CAMK1G | CAMK2A | CAMK2B | CAMK2D | CAMK2G | CAMK2N1 | CAMK2N2 | CAMK4 | CAMKK1 | CAMKK2 | CAMKMT | CAMKV | CAMLG | CAMP | cAMP Phosphodiesterase | cAMP Responsive Element Binding Protein (CREB) | cAMP-Dependent protein kinase (PKA) | CAMSAP1 | CAMSAP2 | CAMSAP3 | CAMTA1 | CAMTA2 | CAND1 | CAND1.11 | CAND2 | Cannabinoid receptor | CANT1 | CANX | Cap-binding complex | CAP1 | CAP2 | CAPG | CAPN1 | CAPN10 | CAPN10-DT | CAPN11 | CAPN12 | CAPN13 | CAPN14 | CAPN15 | CAPN2 | CAPN3 | CAPN5 | CAPN6 | CAPN7 | CAPN8