Vim

Enables protein phosphatase 2A binding activity and protein tyrosine kinase binding activity. Involved in several processes, including decidualization; positive regulation of glial cell proliferation; and response to vitamin D. Located in axon; cell body; and perinuclear region of cytoplasm. Biomarker of Chagas disease; cerebral infarction; hyperthyroidism; nephrosis; and pulmonary hypertension. Human ortholog(s) of this gene implicated in atherosclerosis; autoimmune disease (multiple); and cataract 30. Orthologous to human VIM (vimentin). [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 Vim 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 Vim 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 Vim gene, providing context for its role in the cell.