ZNG1A: A promising drug target and biomarker for the treatment of cancer

Target Name: ZNG1A

NCBI ID: G55871

ZNG1A

ZNG1A: A promising drug target and biomarker for the treatment of cancer

Introduction

ZNG1A (COBW domain-containing protein 1, isoform 1) is a protein that has been identified as a potential drug target and biomarker for the treatment of various diseases, including cancer. ZNG1A is a member of the Zinc finger gene family, which is known for its ability to regulate gene expression and play a role in various cellular processes. The identification and characterization of ZNG1A as a potential drug target and biomarker makes it an attractive target for further research and development of new treatments for cancer and other diseases.

The Zinc finger gene family

Zinc finger genes are a family of transmembrane proteins that contain a conserved zinc finger motif. This motif is a characteristic protein-coding region that is composed of a conserved core sequence and at least one Zinc finger that is involved in protein-protein interactions and can interact with various cellular components. Zinc finger genes have been identified in various organisms, including humans, and have been shown to play a role in various cellular processes, including cell signaling, gene regulation, and disease.

Function and localization of ZNG1A

ZNG1A is a protein that is expressed in various tissues and cells of the body, including the brain, heart, liver, and cancer cells. It is localized to the endoplasmic reticulum (ER) and the cytoplasm of cells. ZNG1A is a 21-kDa protein that has a molecular weight of approximately 21 kDa. It consists of a unique N-terminus that is involved in protein-protein interactions and a unique C-terminus that contains a Zinc finger and a conserved domain that is involved in protein-protein interactions.

Expression and regulation of ZNG1A

ZNG1A is expressed in various tissues and cells of the body and has been shown to play a role in various cellular processes, including cell signaling, gene regulation, and disease. ZNG1A is regulated by various factors, including post-transcriptional regulation, post-translational modification and Protein interactions, etc.

ZNG1A as a drug target

The identification of ZNG1A as a potential drug target makes it an attractive target for the development of new treatments for cancer and other diseases. ZNG1A is known to interact with various cellular components, including the protein kinase kinase (PKC) and the transcription factorPDGF2. These interactions make ZNG1A a potential target for small molecules that can inhibit PKC activity or enhance PDGF2 signaling.

In addition, ZNG1A has also been shown to interact with various other proteins, including the protein serine kinase (PKG2) and the protein kinase (CK) kinase. These interactions suggest that ZNG1A may also need to interact with other proteins to exert its functions.

ZNG1A as a biomarker

The identification of ZNG1A as a potential biomarker for cancer makes it an attractive target for the development of new diagnostic tests for cancer. ZNG1A is expressed in various tissues and cells of the body, including cancer cells, and has been shown to be involved in the regulation of cellular processes that are relevant to cancer development.

In addition, ZNG1A has also been shown to be involved in the regulation of cellular processes that are relevant to other diseases, including cardiovascular disease and neurodegenerative diseases. These findings suggest that ZNG1A may be a valuable biomarker for the detection and treatment of various diseases.

Conclusion

ZNG1A is a protein that has been identified as a potential drug target and biomarker for the treatment of cancer and other diseases. ZNG1A is known to interact with various cellular components, including the protein kinase kin

Protein Name: Zn Regulated GTPase Metalloprotein Activator 1A

Functions: Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1A to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1

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•   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;
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•   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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