Vamp2

Enables calmodulin binding activity; phospholipid binding activity; and syntaxin-1 binding activity. Involved in secretion by cell and synaptic vesicle endocytosis. Acts upstream of or within several processes, including Golgi to plasma membrane protein transport; cellular response to insulin stimulus; and long-term synaptic potentiation. Located in several cellular components, including secretory vesicle; storage vacuole; and trans-Golgi network. Part of synaptobrevin 2-SNAP-25-syntaxin-1a complex. Is active in glutamatergic synapse. Is expressed in several structures, including alimentary system; integumental system; nervous system; respiratory system; and sensory organ. Orthologous to human VAMP2 (vesicle associated membrane protein 2). [provided by Alliance of Genome Resources, Jul 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 mouse Vamp2 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 Vamp2 gene in mouse 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 mouse Vamp2 gene, providing context for its role in the cell.