DNAJB1

This gene encodes a member of the DnaJ or Hsp40 (heat shock protein 40 kD) family of proteins. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. The encoded protein is a molecular chaperone that stimulates the ATPase activity of Hsp70 heat-shock proteins in order to promote protein folding and prevent misfolded protein aggregation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]

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 human DNAJB1 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 DNAJB1 gene in human 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 human DNAJB1 gene, providing context for its role in the cell.