Dnajb3

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. Located in acrosomal vesicle and centrosome. Is expressed in several structures, including alimentary system; brain; genitourinary system; immune system; and respiratory system. Orthologous to human DNAJB3 (DnaJ heat shock protein family (Hsp40) member B3). [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 mouse Dnajb3 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 Dnajb3 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.