Target Name: STAG1
NCBI ID: G10274
Other Name(s): Cohesin subunit SA-1 | DKFZp781D1416 | SA-1 | stromal antigen 1 | Stromal antigen 1 | STAG1_HUMAN | Nuclear protein stromal antigen 1 | SA1 | SCC3A | SCC3 homolog 1 | nuclear protein stromal antigen 1 | MRD47

STAG1: A Potential Drug Target and Biomarker for Cohesin Subunit SA-1

Introduction

Cohesin is a key protein that plays a crucial role in the regulation of DNA double-strand break repair. The cohesin subunit SA-1 is a non-coding RNA molecule that is essential for the proper functioning of the cohesin complex. SA-1 has has been shown to interact with several DNA-binding proteins, including the Ku70 protein, which is a key component of the cohesin complex.

Recent studies have identified SA-1 as a potential drug target and biomarker for various diseases, including cancer. The high-throughput screening approach has led to the identification of several small molecules that can interact with SA-1 and have the potential to be development into drugs. In this article, we will discuss the recent findings on SA-1 as a drug target and biomarker and highlight the potential of this protein for the development of new therapeutics.

Structure and Function of SA-1

The SA-1 protein is a non-coding RNA molecule that is approximately 130 amino acids long. It has a characteristic stem-loop structure and a 5'-end that is rich in conserved amino acid sequence. SA-1 plays a critical role in the regulation of DNA double-strand break repair as a component of the cohesin complex.

The cohesin complex is a protein-protein interaction that is essential for the proper functioning of DNA double-strand break repair. The cohesin complex consists of several subunits, including the cohesin subunit SA-1, the Ku70 protein, and the p53 protein. SA-1 subunit is critical for the proper functioning of the cohesin complex as it has been shown to interact with the Ku70 protein, which is a key component of the cohesin complex.

SA-1 has been shown to play a critical role in the regulation of DNA double-strand break repair. It has been shown to interact with the Ku70 protein, which is a key component of the cohesin complex. This interaction between SA-1 and Ku70 has been shown to play a critical role in the regulation of DNA double-strand break repair.

Potential Drug Targets for SA-1

The identification of potential drug targets for SA-1 has been an active area of ??????research in recent years. The high-throughput screening approach has led to the identification of several small molecules that can interact with SA-1 and have the potential to be development into drugs.

One of the potential drug targets for SA-1 is the inhibition of Ku70-SA-1 interactions. The Ku70 protein is a key component of the cohesin complex, and its interaction with SA-1 is critical for the proper functioning of the cohesin complex . Therefore, inhibiting the interaction between Ku70 and SA-1 has been shown to be a potential therapeutic approach for various diseases, including cancer.

Another potential drug target for SA-1 is the inhibition of SA-1 function. The SA-1 protein has been shown to play a critical role in the regulation of DNA double-strand break repair, and its inhibition has been shown to be a potential therapeutic approach for various diseases, including cancer.

Biomarkers for SA-1

The SA-1 protein has also been identified as a potential biomarker for various diseases, including cancer. The expression of SA-1 has been shown to be regulated by various factors, including DNA damage, cellular stress, and chemo-therapy. Therefore, the expression of SA-1 can be used as a biomarker for various diseases, including cancer.

Conclusion

In conclusion, SA-1 is a non-coding RNA molecule that is essential for the proper functioning of the cohesin complex. Its interaction with the Ku70 protein has been shown to play a critical role in the regulation of DNA double-strand break repair.

Protein Name: Stromal Antigen 1

Functions: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis

More Common Targets

STAG2 | STAG3 | STAG3L1 | STAG3L2 | STAG3L3 | STAG3L4 | STAG3L5P | STAG3L5P-PVRIG2P-PILRB | STAGA complex | Stage selector protein complex | STAM | STAM-DT | STAM2 | STAMBP | STAMBPL1 | STAP1 | STAP2 | STAR | STARD10 | STARD13 | STARD3 | STARD3NL | STARD4 | STARD4-AS1 | STARD5 | STARD6 | STARD7 | STARD7-AS1 | STARD8 | STARD9 | STARP1 | STAT1 | STAT2 | STAT3 | STAT4 | STAT4-AS1 | STAT5 | STAT5A | STAT5B | STAT6 | STATH | STAU1 | STAU2 | STAU2-AS1 | STBD1 | STC1 | STC2 | STEAP1 | STEAP1B | STEAP2 | STEAP2-AS1 | STEAP3 | STEAP3-AS1 | STEAP4 | STEEP1 | Steroid 5-alpha-Reductase | Sterol O-acyltransferase (ACAT) | Sterol Regulatory Element-Binding Protein | STH | STIL | STIM1 | STIM2 | STIMATE | STIN2-VNTR | STING1 | STIP1 | STK10 | STK11 | STK11IP | STK16 | STK17A | STK17B | STK19 | STK24 | STK25 | STK26 | STK3 | STK31 | STK32A | STK32A-AS1 | STK32B | STK32C | STK33 | STK35 | STK36 | STK38 | STK38L | STK39 | STK4 | STK4-DT | STK40 | STKLD1 | STMN1 | STMN2 | STMN3 | STMN4 | STMND1 | STMP1 | STN1 | STOM