Plk3

This gene encodes a member of the highly conserved polo-like kinase family of serine/threonine kinases. Members of this family are characterized by an amino-terminal catalytic domain and a carboxy-terminal bipartite polo box domain that functions as a substrate-binding motif and a cellular localization signal. Polo-like kinases have primarily been implicated in cell cycle regulation. In mouse, this protein that has been reported to localize to the nucleolus during interphase but is undetectable during mitosis, following nucleolus dissociation during prophase. The protein relocalizes to the nucleolus just prior to cytokinesis and peak levels are detected during G1 of interphase. This gene has been implicated in regulation of entry into S phase, with RNAi-induced depletion resulting in failure to re-enter the cell cycle. Mice deficient for this gene exhibit increased weight and tumor development at advanced age. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]

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 Plk3 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 Plk3 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 Plk3 gene, providing context for its role in the cell.