As a regulator of transcription via chromatin remodeling, p300 is a histone acetyltransferase that binds to adenovirus E1A protein and may play a role in its transforming capacity. EID-2 (EP300-interacting inhibitor of differentiation 2), also known as CREBBP/EP300 inhibitor 2, is a 236 amino acid nuclear protein that cooperates with EID-2B to bind to the C-terminus of p300 to inhibit its activity. It also represses MYOD-dependent transcription and muscle differentiation. By interacting with SMAD2, SMAD3 and SMAD4, EID-2 selectively blocks the formation of TGFB-induced SMAD3-SMAD4 complex, thereby repressing TGFB/SMAD3-dependent signaling. Though it is abundantly expressed in placenta, EID-2 is highly expressed in skeletal muscle, heart, liver, brain and kidney. There are two isoforms of EID-2 that are produced as a result of alternative splicing events.