Protein Domain : p53-like tetramerisation domain superfamily IPR036674

Type	Homologous_superfamily
Description	The p53 protein is a tetrameric transcription factor that plays a central role in the prevention of neoplastic transformation [ ]. Oligomerization appears to be essential for the tumour suppressing activity of p53. p53 can be divided into different functional domains: an N-terminal transactivation domain, a proline-rich domain, a DNA-binding domain (), a tetramerisation domain and a C-terminal regulatory region. The tetramerisation domain of human p53 extends from residues 325 to 356, and has a 4-helical bundle fold. The tetramerisation domain is essential for DNA binding, protein-protein interactions, post-translational modifications, and p53 degradation [ , ].This superfamily also includes the structural-related C-terminal SARAH (Salvador-RassF-Hippo) domain found in tumor suppressors such as Serine/threonine-protein kinase 4 (human Hippo homologue, Mst), Serine/threonine-protein kinase 3, Serine/threonine-protein kinase cst-1 and Serine/threonine-protein kinase hippo, which is involved in dimerisation [].
Short Name	p53_tetramer_sf