Sh3glb1

Enables fatty acid binding activity; lysophosphatidic acid acyltransferase activity; and phosphatidylinositol 3-kinase activator activity. Involved in several processes, including autophagic cell death; positive regulation of autophagosome assembly; and regulation of intrinsic apoptotic signaling pathway by p53 class mediator. Acts upstream of or within 'de novo' post-translational protein folding; phosphatidic acid biosynthetic process; and positive regulation of establishment of protein localization to mitochondrion. Located in membrane. Part of protein-containing complex. Is expressed in several structures, including cerebellum; cerebral cortex; otocyst; and spleen. Orthologous to human SH3GLB1 (SH3 domain containing GRB2 like, endophilin B1). [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 Sh3glb1 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 Sh3glb1 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 Sh3glb1 gene, providing context for its role in the cell.