RGS17

This gene encodes a member of the regulator of G-protein signaling family. This protein contains a conserved, 120 amino acid motif called the RGS domain and a cysteine-rich region. The protein attenuates the signaling activity of G-proteins by binding to activated, GTP-bound G alpha subunits and acting as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. [provided by RefSeq, Jul 2008]

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 RGS17 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 RGS17 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 RGS17 gene, providing context for its role in the cell.