Parp8

Predicted to enable kinase binding activity; pentosyltransferase activity; and protein serine/threonine kinase activator activity. Predicted to be involved in endoplasmic reticulum unfolded protein response and protein auto-ADP-ribosylation. Predicted to be active in endoplasmic reticulum tubular network and nuclear envelope. Orthologous to human PARP8 (poly(ADP-ribose) polymerase family member 8). [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 Parp8 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 Parp8 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 Parp8 gene, providing context for its role in the cell.