EID2
| EP300 interacting inhibitor of differentiation 2 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | EID2 | ||||||
| Alt. symbols | CRI2 | ||||||
| NCBI gene | 163126 | ||||||
| HGNC | 28292 | ||||||
| OMIM | 609773 | ||||||
| RefSeq | NM_153232 | ||||||
| UniProt | Q8N6I1 | ||||||
| Other data | |||||||
| Locus | Chr. 19 q13.2 | ||||||
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EP300 interacting inhibitor of differentiation 2, also known as EID2 is a human gene.[1]
Function
[edit]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.
References
[edit]- ^ 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". Gene. 318: 35–43. doi:10.1016/j.gene.2003.06.001. PMID 14585496.
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