Dnajb5

Predicted to enable protein-folding chaperone binding activity and unfolded protein binding activity. Predicted to be involved in chaperone cofactor-dependent protein refolding and response to unfolded protein. Predicted to act upstream of or within negative regulation of transcription by RNA polymerase II. Predicted to be located in nucleus. Predicted to be active in cytosol. Orthologous to human DNAJB5 (DnaJ heat shock protein family (Hsp40) member B5). [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 Dnajb5 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 Dnajb5 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 Dnajb5 gene, providing context for its role in the cell.