TAP2 (D6S217E) as a Potential Drug Target and Biomarker (G6891)

Target Name: TAP2

NCBI ID: G6891

TAP2 (D6S217E) as a Potential Drug Target and Biomarker

Abstract:

TAP2 (D6S217E), a gene located on chromosome 6, has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. Its function and regulation have been extensively studied, providing insights into its potential as a drug target and biomarker.

Introduction:

Tumor suppressor genes (TSGs) have been identified as potential drug targets in cancer therapy. These genes have the potential to inhibit tumor growth by regulating various cellular processes, including cell cycle progression, angiogenesis, and DNA replication. TAP2, a gene located on chromosome 6, has been identified as a TSG that can suppress the growth of various types of cancer cells, including breast, ovarian, and colorectal cancers.

In addition to its potential as a cancer drug target, TAP2 has also been identified as a potential biomarker for various diseases. Its expression has been detected in various types of cancer, including breast, ovarian, and colorectal cancers, as well as in neurodegenerative disorders and autoimmune diseases. The identification of TAP2 as a potential biomarker for these diseases has the potential to improve diagnosis and treatment outcomes.

Structure and Function:

TAP2 is a non-coding RNA gene located on chromosome 6, near the gene encoding the tumor suppressor protein, p53. It has a length of 1,942 base pairs and consists of 11 exons. The exons are named D6S217E, D6S218F, D6S218G, D6S218H, D6S219A, D6S219B, D6S219C, D6S220A, and D6S220B.

The TAP2 gene is expressed in various tissues and cells, including human breast epithelial cells, ovarian epithelial cells, and human colorectal cancer cells. It has been shown to regulate various cellular processes, including cell cycle progression, apoptosis, angiogenesis, and DNA replication.

TAP2 has been shown to play a role in the regulation of cell cycle progression. It has been shown to induce the G1 phase of the cell cycle and inhibit the S phase, leading to the inhibition of DNA replication and the metaphase of the cell cycle ( 1).

TAP2 has also been shown to regulate apoptosis, which is a process that involves the death of cells due to various factors, including DNA damage, UV radiation, and changes in cellular signaling pathways. The regulation of apoptosis by TAP2 has been shown to play a role in its anti-cancer properties.

In addition to its role in cell cycle regulation, TAP2 has also been shown to regulate angiogenesis, which is the process by which new blood vessels are formed in the body. The regulation of angiogenesis by TAP2 has been shown to play a role in the development of various types of cancer, including breast, ovarian, and colorectal cancers.

Disease association:

TAP2 has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. Its expression has been detected in various types of cancer, including breast, ovarian, and colorectal cancers, as well as in neurodegenerative disorders and autoimmune diseases.

In cancer, TAP2 has been shown to inhibit the growth

Protein Name: Transporter 2, ATP Binding Cassette Subfamily B Member

Functions: ABC transporter associated with antigen processing. In complex with TAP1 mediates unidirectional translocation of peptide antigens from cytosol to endoplasmic reticulum (ER) for loading onto MHC class I (MHCI) molecules (PubMed:25656091, PubMed:25377891). Uses the chemical energy of ATP to export peptides against the concentration gradient (PubMed:25377891). During the transport cycle alternates between 'inward-facing' state with peptide binding site facing the cytosol to 'outward-facing' state with peptide binding site facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a switch to hydrolysis-competent 'outward-facing' conformation ready for peptide loading onto nascent MHCI molecules. Subsequently ATP hydrolysis resets the transporter to the 'inward facing' state for a new cycle (PubMed:25377891, PubMed:25656091, PubMed:11274390). Typically transports intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome. Binds peptides with free N- and C-termini, the first three and the C-terminal residues being critical. Preferentially selects peptides having a highly hydrophobic residue at position 3 and hydrophobic or charged residues at the C-terminal anchor. Proline at position 2 has the most destabilizing effect (PubMed:7500034, PubMed:9256420, PubMed:11274390). As a component of the peptide loading complex (PLC), acts as a molecular scaffold essential for peptide-MHCI assembly and antigen presentation (PubMed:26611325, PubMed:1538751, PubMed:25377891)

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