Dynll2

Enables identical protein binding activity and scaffold protein binding activity. Predicted to be involved in microtubule-based process. Part of cytoplasmic dynein complex. Is active in glutamatergic synapse and postsynaptic density. Orthologous to human DYNLL2 (dynein light chain LC8-type 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 rat Dynll2 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 Dynll2 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 Dynll2 gene, providing context for its role in the cell.