Target Name: AGAP2
NCBI ID: G116986
Review Report on AGAP2 Target / Biomarker Content of Review Report on AGAP2 Target / Biomarker
AGAP2
Other Name(s): ArfGAP with GTPase domain, ankyrin repeat and PH domain 2 | AGAP2 variant 2 | phosphoinositide 3-kinase enhancer | ArfGAP with GTPase domain, ankyrin repeat and PH domain 2, transcript variant 1 | Phosphatidylinositol-3-kinase enhancer | ArfGAP with GTPase domain, ankyrin repeat and PH domain 2, transcript variant 2 | CENTG1 | AGAP2 variant 1 | Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2 | cnt-g1 | AGAP2_HUMAN | phosphatidylinositol 3-kinase enhancer | AGAP-2 | Cnt-g1 | GGAP2 | centaurin-gamma-1 | Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2 (isoform PIKE-L) | Arf GAP with GTP-binding protein-like, ANK repeat and PH domains 2 | GTP-binding and GTPase-activating protein 2 | PIKE | centaurin, gamma 1 | KIAA0167 | Phosphoinositide 3-kinase enhancer | FLJ16430 | Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2 (isoform PIKE-A) | GTP-binding and GTPase activating protein 2 | Phosphatidylinositol 3-kinase enhancer | Centaurin-gamma-1

AGAP2: A Potential Drug Target and Biomarker

AGAP2 (ArfGAP with GTPase domain, ankyrin repeat and PH domain 2) is a protein that has been identified as a potential drug target and biomarker. It is a key regulator of the actinin-associated protein (AAP) complex, which is involved in a variety of cellular processes, including cytoskeletal organization, intracellular signaling, and cell survival. The AGAP2 protein has been shown to play a crucial role in the regulation of cell adhesion, migration, and invasion, and it is a potential target for small molecule inhibitors.

The AGAP2 protein is composed of several domains, including a GTPase domain, ankyrin repeat, and PH domain 2. The GTPase domain is responsible for the protein's catalytic activity and is involved in the regulation of protein-protein interactions. The ankyrin repeat is a conserved sequence that is found in a variety of proteins and is known for its role in protein stability and localization. The PH domain 2 is a conserved sequence that is involved in protein-protein interactions and may be involved in the regulation of cellular processes such as cell adhesion and migration.

Studies have shown that AGAP2 is involved in a variety of cellular processes, including the regulation of cell adhesion, migration, and invasion. For example, AGAP2 has been shown to play a role in the regulation of cell-cell adhesion by regulating the activity of the protein cadherin. In addition, AGAP2 has been shown to be involved in the regulation of cell migration by regulating the activity of the protein protamine 2 (PRM2), which is a protein that is involved in the production of vasodilatory signals in response to changes in cellular tension.

In addition to its role in cellular processes, AGAP2 has also been shown to be involved in the regulation of protein-protein interactions. For example, AGAP2 has been shown to interact with the protein tyrosine kinase (TK) and the protein Fyn, and these interactions may be involved in the regulation of cellular processes such as cell signaling and protein stability.

Given its involvement in a variety of cellular processes, AGAP2 is a potential drug target for small molecule inhibitors. Studies have shown that AGAP2 is a good candidate for inhibition with small molecules such as inhibitors of the GTPase domain, the ankyrin repeat, and the PH domain 2. In addition, AGAP2 has been shown to be involved in the regulation of cell adhesion, migration, and invasion, which makes it a promising target for drugs that are able to modulate these processes.

In conclusion, AGAP2 is a protein that has been shown to play a crucial role in a variety of cellular processes, including cell adhesion, migration, and invasion. It is a potential drug target and biomarker, and its regulation by small molecules makes it an attractive target for the development of new pharmaceuticals. Further research is needed to fully understand the role of AGAP2 in cellular processes and to develop effective inhibitors of its activity.

Protein Name: ArfGAP With GTPase Domain, Ankyrin Repeat And PH Domain 2

Functions: GTPase-activating protein (GAP) for ARF1 and ARF5, which also shows strong GTPase activity. Isoform 1 participates in the prevention of neuronal apoptosis by enhancing PI3 kinase activity. It aids the coupling of metabotropic glutamate receptor 1 (GRM1) to cytoplasmic PI3 kinase by interacting with Homer scaffolding proteins, and also seems to mediate anti-apoptotic effects of NGF by activating nuclear PI3 kinase. Isoform 2 does not stimulate PI3 kinase but may protect cells from apoptosis by stimulating Akt. It also regulates the adapter protein 1 (AP-1)-dependent trafficking of proteins in the endosomal system. It seems to be oncogenic. It is overexpressed in cancer cells, prevents apoptosis and promotes cancer cell invasion

The "AGAP2 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 AGAP2 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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