Atg14

Predicted to enable GTPase binding activity; phosphatidylinositol 3-kinase inhibitor activity; and protein-membrane adaptor activity. Predicted to be involved in several processes, including early endosome to late endosome transport; macroautophagy; and regulation of protein phosphorylation. Predicted to act upstream of or within defense response to other organism; endosome to lysosome transport; and regulation of triglyceride metabolic process. Predicted to be located in several cellular components, including mitochondria-associated endoplasmic reticulum membrane contact site; phagocytic vesicle; and phagophore assembly site membrane. Predicted to be part of phosphatidylinositol 3-kinase complex, class III. Predicted to be active in autophagosome and phagophore assembly site. Predicted to be extrinsic component of omegasome membrane and extrinsic component of phagophore assembly site membrane. Orthologous to human ATG14 (autophagy related 14). [provided by Alliance of Genome Resources, Apr 2025]

A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in rat Atg14 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.

Biological processes and signaling networks where the Atg14 gene in rat plays a role, providing insight into its function and relevance in health or disease.

The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.

Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.

Describes the biological processes, cellular components, and molecular functions associated with the rat Atg14 gene, providing context for its role in the cell.