Dnaja4

Predicted to enable protein-folding chaperone binding activity and unfolded protein binding activity. Predicted to be involved in several processes, including negative regulation of endothelial cell migration; negative regulation of inclusion body assembly; and protein refolding. Predicted to be located in membrane. Predicted to be active in cytosol. Is expressed in several structures, including adrenal gland; alimentary system; brain; genitourinary system; and respiratory system. Orthologous to human DNAJA4 (DnaJ heat shock protein family (Hsp40) member A4). [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 mouse Dnaja4 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 Dnaja4 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.

Describes the biological processes, cellular components, and molecular functions associated with the mouse Dnaja4 gene, providing context for its role in the cell.