SWIB domain found in BRG1-associated factor 60C (BAF60C) and similar proteins
BAF60C, also termed SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3 (SMARCD3), or 60 kDa BRG-1/Brm-associated factor subunit C, is a core subunit of the SWI/SNF chromatin-remodeling complex that activates the transcription of fatty acid oxidation genes during fasting. It is involved in chromatin remodeling and hepatic lipid metabolism. It is also essential for cardiomyocyte differentiation at the early heart development. Moreover, BAF60C drives glycolytic metabolism in the muscle and improves systemic glucose homeostasis through Deptor-mediated Akt activation. Furthermore, BAF60C epigenetically regulates epithelial-mesenchymal transition (EMT) by activating WNT signaling pathways.
Feature 1:putative peptide binding site [polypeptide binding site]
Evidence:
Comment:The SWIB domain and the MDM2 domain share a common evolutionary origin and thus adopt similar structures, which suggests the SWIB domain may interact with a helical peptide through a cleft on the surface.
Comment:Based on the structural evidence that MDM2 domain binds p53 or other peptides.