Dnajb7

Predicted to enable protein folding chaperone; protein-folding chaperone binding activity; and unfolded protein binding activity. Predicted to be involved in chaperone-mediated protein folding. Predicted to be active in cytoplasm and nucleus. Orthologous to human DNAJB7 (DnaJ heat shock protein family (Hsp40) member B7). [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 Dnajb7 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 Dnajb7 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 Dnajb7 gene, providing context for its role in the cell.