ANKRD13D: A Potential Drug Target and Biomarker (G338692)

Target Name: ANKRD13D

NCBI ID: G338692

ANKRD13D: A Potential Drug Target and Biomarker

Ankyrin A protein, also known as ANKRD13D, is a nuclear protein that plays a crucial role in the regulation of mitochondrial function and energy metabolism. It is a key regulator of the mitochondrial translation machinery, which is responsible for the production of proteins from mRNA to functional proteins. ANKRD13D is highly conserved across various species, and its sequence and structure have been conserved in bacteria, yeast, plants, and animals.

The ANKRD13D protein is composed of 158 amino acid residues and has a calculated molecular mass of 19.1 kDa. It has a distinct N-terminal and C-terminal region, which contain the N-terminal domain and the C-terminal domain, respectively. The N-terminal domain is composed of a unique farnesylated cysteine residue, which is important for its stability and function. The C-terminal domain has a conserved glycine residue, which is involved in the protein-protein interaction.

The ANKRD13D protein has been shown to play a critical role in the regulation of mitochondrial translation. It is a negative regulator of the translation machinery, which means that it prevents the initiation of protein synthesis by translating mRNA into the cytoplasm. This is done by binding to the eIF4F complex, which is the first protein that forms during the translation of mRNA. By binding to eIF4F, ANKRD13D prevents the formation of the eIF4F-ANKRD13D complex, which is responsible for the transfer of the amino acids from the mRNA to the ribosome.

The ANKRD13D protein is also involved in the regulation of mitochondrial dynamics. It plays a role in the regulation of mitochondrial fission and fusion, as well as the regulation of mitochondrial size and shape. This is done by interacting with the mitochondrial proteinBeclin-1 (BECN1), which is involved in the regulation of mitochondrial dynamics.

In addition to its role in the regulation of mitochondrial function, ANKRD13D has also been shown to be involved in the regulation of cellular processes that are independent of mitochondrial function. For example, ANKRD13D has been shown to play a role in the regulation of cell adhesion, as well as the regulation of the cytoskeleton.

The ANKRD13D protein is a potential drug target due to its involvement in the regulation of mitochondrial function and energy metabolism. Its unique farnesylated cysteine residue and conserved N-terminal and C-terminal regions make it an attractive target for small molecules. Additionally, its role in the regulation of mitochondrial dynamics and its involvement in the regulation of cellular processes independent of mitochondrial function make it a promising target for drugs with diverse mechanisms of action.

In conclusion, ANKRD13D is a highly conserved protein that plays a critical role in the regulation of mitochondrial function and energy metabolism. Its unique farnesylated cysteine residue and conserved N-terminal and C-terminal regions make it an attractive target for small molecules, and its involvement in the regulation of mitochondrial dynamics and cellular processes independent of mitochondrial function make it a promising target for drugs with diverse mechanisms of action. Further research is needed to fully understand the role of ANKRD13D in the regulation of mitochondrial function and to develop effective drugs that target this protein.

Protein Name: Ankyrin Repeat Domain 13D

Functions: Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane

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