Dusp22

Predicted to enable phosphoprotein phosphatase activity; protein tyrosine kinase binding activity; and protein tyrosine kinase inhibitor activity. Predicted to be involved in several processes, including cellular response to epidermal growth factor stimulus; negative regulation of focal adhesion assembly; and positive regulation of JNK cascade. Predicted to act upstream of or within several processes, including negative regulation of T cell mediated immunity; negative regulation of T cell receptor signaling pathway; and negative regulation of transcription by RNA polymerase II. Predicted to be located in cytoplasm and leading edge of lamellipodium. Predicted to be part of filamentous actin. Predicted to be active in cytosol and plasma membrane. Orthologous to human DUSP22 (dual specificity phosphatase 22). [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 rat Dusp22 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 Dusp22 gene in rat 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 rat Dusp22 gene, providing context for its role in the cell.