S100A6 Protein, Human

The S100A6 Protein serves as a pivotal calcium sensor and modulator, actively contributing to cellular calcium signaling. Through interactions with various proteins, including TPR-containing proteins, S100A6 indirectly participates in diverse physiological processes, such as the reorganization of the actin cytoskeleton and cell motility. Existing as a homodimer with a head-to-tail assembly of two subunits, S100A6 binds two calcium ions in a cooperative manner. Its calcium-dependent interaction with CACYBP, ANXA2, ANXA11, SUGT1, and tropomyosin reveals its role in orchestrating complex molecular interactions. Moreover, S100A6 interacts with TP53, displaying higher affinity for TP53 phosphorylated on its N-terminal domain and lower affinity for TP53 phosphorylated on its C-terminal domain. The interaction with PPP5C, mediated by TPR repeats, is calcium-dependent and modulates PPP5C activity, emphasizing S100A6's regulatory influence in cellular processes. Additionally, its interaction with TPPP inhibits TPPP dimerization, as reported in recent studies.