EFS: A Signaling Protein in Cellular Signaling (G10278)

Target Name: EFS

NCBI ID: G10278

Content of Review Report on EFS Target / Biomarker

EFS

EFS: A Signaling Protein in Cellular Signaling

Signal transduction proteins are a family of transmembrane proteins that play a crucial role in intracellular signaling. One of the most well-known signaling proteins is the SH3-containing protein, EFS (Eukaryotic signal- transducing protein). EFS is a protein that is expressed in a wide range of cell types, including neurons, muscle cells, and blood vessels. It is involved in a number of different signaling pathways, including the regulation of cell growth, differentiation, and survival.

The SH3 domain of EFS is a unique feature that gives it its name. The SH3 domain is a type of protein domain that is characterized by a single domain that contains a highly conserved amino acid sequence. The SH3 domain is responsible for the protein's ability to interact with other proteins, as well as its ability to undergo structural changes that regulate its activity.

One of the key functions of EFS is its role in intracellular signaling. EFS is involved in a number of different signaling pathways, including the regulation of cell growth, differentiation, and survival. For example, EFS has been shown to play a role in the regulation of cell proliferation, and has been shown to interact with proteins that are involved in cell cycle progression.

In addition to its role in intracellular signaling, EFS is also involved in the regulation of cell-cell interactions. EFS is a protein that is involved in the formation of tight junctions, which are a type of barrier that separates cells and allows them to communicate with one another. tight junctions are important for the proper functioning of many different cell types, including neurons and muscle cells.

EFS is also involved in the regulation of cell survival. The SH3 domain of EFS is responsible for its ability to interact with proteins that are involved in cell survival, such as Bcl-2. Bcl-2 is a protein that is involved in the regulation of cell growth and differentiation, and is thought to play a role in the regulation of cell survival. EFS has been shown to interact with Bcl-2, and has been shown to be regulated by Bcl-2.

Despite its involvement in a number of different signaling pathways, EFS is not yet a well-studied protein. There are many questions about the exact function of EFS, and more research is needed to fully understand its role in intracellular signaling. However, the studies that have been done on EFS suggest that it is an important protein that is involved in many different signaling pathways.

In conclusion, EFS is a protein that is involved in a number of different signaling pathways. Its unique SH3 domain, as well as its involvement in the regulation of cell growth, differentiation, and survival, make it an important protein that should be further studied. Future research on EFS may reveal new functions for this protein, and may lead to the development of new treatments for a variety of diseases.

Protein Name: Embryonal Fyn-associated Substrate

Functions: Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May serve as an activator of SRC and a downstream effector. Interacts with the SH3 domain of FYN and with CRK, SRC, and YES (By similarity)

The "EFS 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 EFS 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

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