Dnajc9

Predicted to enable heat shock protein binding activity; histone binding activity; and protein-folding chaperone binding activity. Predicted to be involved in nucleosome assembly and positive regulation of ATP-dependent activity. Predicted to be located in several cellular components, including cytosol; extracellular space; and nucleoplasm. Predicted to be part of protein folding chaperone complex. Predicted to be active in cytoplasm and nucleus. Is expressed in several structures, including alimentary system; brain; connective tissue; genitourinary system; and immune system. Orthologous to human DNAJC9 (DnaJ heat shock protein family (Hsp40) member C9). [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 Dnajc9 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 Dnajc9 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 Dnajc9 gene, providing context for its role in the cell.