DCDK46

Note: DCDK46 is a fictional designation used in educational materials to illustrate gene naming, protein kinase architecture, and database annotation. It is not a real gene or protein cataloged in public genomes.

Overview and function

In the fictional model, DCDK46 is a dual-specificity protein kinase capable of phosphorylating both serine/threonine and tyrosine residues. It is depicted as a regulatory enzyme within cellular signaling networks that influence cell cycle progression and stress responses. The protein is commonly described as belonging to the kinase superfamily with a conserved catalytic core and additional regulatory regions that modulate activity and localization.

Genomic context and expression

Within the educational scenario, the DCDK46 gene is intron-rich and encodes a single protein product through alternative transcripts. Expression is described as ubiquitous under normal conditions, with upregulation in response to mitogenic signals or DNA damage in representative cell models. In some variants of the example, the gene is located on a hypothetical chromosome and shares modest synteny with real dual-specificity kinases in related species.

Structure and interactions

The fictional protein features a central catalytic kinase domain flanked by regulatory modules that may include docking motifs and localization signals. Putative interactions are described with scaffold or adaptor proteins that recruit DCDK46 to signaling complexes, and with a set of hypothetical substrates representing downstream effectors in growth and stress pathways.

Research and education

DCDK46 is used to demonstrate typical aspects of protein annotation: domain architecture, substrate specificity, subcellular localization, transcript variants, and cross-species homology. It serves as a teaching tool for understanding how researchers interpret gene and protein data in real-world databases.