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EID2

From Wikipedia, the free encyclopedia
EID2
Identifiers
AliasesEID2, CRI2, EID-2, EP300 interacting inhibitor of differentiation 2
External IDsOMIM: 609773; MGI: 2681174; GeneCards: EID2
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_153232

NM_198425

RefSeq (protein)

NP_694964

NP_940817

Location (UCSC)Chr 19: 39.54 – 39.54 MbChr 7: 27.97 – 27.97 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

EP300 interacting inhibitor of differentiation 2, also known as EID2, is a human gene.[5]

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]
  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000176396 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000046058 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ 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.