ZAP70: A Non-Code RNA Molecule as A Drug Target and Biomarker

Target Name: ZAP70

NCBI ID: G7535

ZAP70

ZAP70: A Non-Code RNA Molecule as A Drug Target and Biomarker

ZAP70 (Zinc Finger Protein 70), also known as STD-4, is a non-coding RNA molecule that plays a critical role in the development and progression of various diseases, including cancer. ZAP70 has been identified as a drug potential target and biomarker due to its unique structure and biology.

The ZAP70 protein is composed of a nucleotide base, a protein domain, and a C-terminal hypervariable region (HVR). The nucleotide base consists of a cytosine residue, which is flanked by two adenine residues, while the protein domain consists of a single alpha-helices region. The C-terminus of the ZAP70 protein is a unique feature that consists of a double-stranded RNA structure that can form a hairpin loop and can tether the protein to various cellular structures.

ZAP70 is a non-coding RNA molecule that plays a critical role in the development and progression of various diseases, including cancer.

One of the most significant functions of ZAP70 is its role in cell signaling. ZAP70 has been shown to play a role in the regulation of cell growth, cell differentiation, and cell survival. ZAP70 has been shown to interact with various proteins, including the transcription factor, NF-kappa-B, and the protein kinase, APRF1. These interactions play a critical role in the regulation of cellular processes such as cell division, apoptosis, and angiogenesis.

In addition to its role in cell signaling, ZAP70 has also been shown to play a role in the regulation of gene expression. ZAP70 has been shown to interact with various RNA-binding proteins, including the protein, HIF1伪. This interaction between ZAP70 and HIF1伪 plays a critical role in the regulation of gene expression, including the regulation of cell growth and differentiation.

The ZAP70 protein has also been shown to play a role in the regulation of cellular processes such as cell adhesion, migration and invasion. ZAP70 has been shown to interact with the protein, E-cadherin, which is involved in cell-cell adhesion and is a critical factor in the regulation of cell migration and invasion.

ZAP70 has also been shown to play a role in the regulation of cellular signaling pathways that are involved in cancer progression. ZAP70 has been shown to interact with various proteins involved in the regulation of cell signaling pathways, including the protein, TGF-β1. This The interaction between ZAP70 and TGF-β1 plays a critical role in the regulation of cell signaling pathways that are involved in cancer progression.

ZAP70 has also been shown to play a role in the regulation of cellular processes that are involved in aging and age-related diseases. ZAP70 has also been shown to interact with the protein, SIRT1. This interaction between ZAP70 and SIRT1 plays a critical role in the regulation of cellular processes that are involved in aging and age-related diseases.

In conclusion, ZAP70 is a non-coding RNA molecule that plays a critical role in the development and progression of various diseases, including cancer. ZAP70 has been shown to interact with various proteins involved in the regulation of cell signaling, cell adhesion, migration and invasion, and cellular signaling pathways. These interactions play a critical role in the regulation of cellular processes that are involved in the development and progression of various diseases, including cancer. Therefore, ZAP70 is a potential drug target and biomarker.

Protein Name: Zeta Chain Of T Cell Receptor Associated Protein Kinase 70

Functions: Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD247/CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD247/CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR)

The "ZAP70 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 ZAP70 comprehensively, including but not limited to:
•   general information;
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•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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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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