The protein encoded by this gene may function as an endogenous suppressor of TGF-beta signaling and inhibits differentiation by blocking the histone acetyltransferase activity of p300, class I histone deacetylase, HDACs. The N-terminal portion of EID-2 was required for the binding to HDACs. This region was also involved in the transcriptional repression and nuclear localization, suggesting the importance of the involvement of HDACs in the EID-2 function. EID-2 inhibits TGF-beta/Smad transcriptional responses. EID-2 interacts constitutively with Smad proteins, and most strongly with Smad3. Stable expression of EID-2 in the TGF-beta1-responsive cell line inhibits endogenous Smad3-Smad4 complex formation and TGF-beta1-induced expression of p21 and p15. EID-2 displays developmentally regulated expression with high levels in adult heart and brain. Overexpression of EID-2 inhibits muscle-specific gene expression through inhibition of MyoD-dependent transcription. This inhibitory effect on gene expression can be explained by EID-2's ability to associate with and inhibit the acetyltransferase activity of p300.
^Ji A, Dao D, Chen J, MacLellan WR (October 2003). "EID-2, a novel member of the EID family of p300-binding proteins inhibits transactivation by MyoD". Gene318: 35–43. doi:10.1016/j.gene.2003.06.001. PMID14585496.