Epn2

The protein encoded by this gene is a member of the epsin protein family. Epsin proteins are endocytic adaptors that function in the formation of clatherin-coated vesicles. Epsins contain a highly conserved N-terminal homology domain that binds phosphatidylinositol 4,5-bisphosphate in the plasma membrane, two or three ubiquitin interacting motifs, two clathrin-binding motifs, a cluster of aspartate-proline-tryptophan/phenylalanine repeats, and two or three asparagine-proline-phenylalanine tripeptide repeats at the C-terminus. In mouse, simultaneous knockout of this gene and its paralog results in embryonic arrest due to disruption of Notch signaling, suggesting a role as a specialized endocytic adaptor. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2015]

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 Epn2 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 Epn2 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 Epn2 gene, providing context for its role in the cell.