Dnajb13

Predicted to enable protein-folding chaperone binding activity and unfolded protein binding activity. Predicted to be involved in axonemal central apparatus assembly and chaperone cofactor-dependent protein refolding. Located in axoneme; sperm flagellum; and sperm head-tail coupling apparatus. Part of radial spoke. Is expressed in several structures, including brain ventricle and choroid plexus; ventricular layer; and white fat. Human ortholog(s) of this gene implicated in primary ciliary dyskinesia 34. Orthologous to human DNAJB13 (DnaJ heat shock protein family (Hsp40) member B13). [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 Dnajb13 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 Dnajb13 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 Dnajb13 gene, providing context for its role in the cell.