Ppih

Predicted to enable cyclosporin A binding activity; peptidyl-prolyl cis-trans isomerase activity; and ribonucleoprotein complex binding activity. Predicted to be involved in positive regulation of viral genome replication; protein folding; and protein peptidyl-prolyl isomerization. Predicted to be located in nuclear speck. Predicted to be part of U4/U6 snRNP and U4/U6 x U5 tri-snRNP complex. Predicted to be active in cytoplasm and intracellular membrane-bounded organelle. Is expressed in several structures, including central nervous system; extraembryonic component; and retina. Orthologous to human PPIH (peptidylprolyl isomerase H). [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 mouse Ppih 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 Ppih 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 Ppih gene, providing context for its role in the cell.