Anti-EID1

E1A-like inhibitor of differentiation-1 (EID-1), an acetyltransferase enzyme, binds both the retinoblastoma protein (Rb), a regulator of cell cycle and tissue specific transcription, and the adenovirus E1A-associated cellular p300 transcriptional co-activator protein. EID-1 inhibits cellular differentiation by blocking the histone acetyltransferase activity of p300. EID-1 also acetylates both histones and non-histone proteins such as NCOA3 co-activator. By acetylating histones, EID-1 gives a specific tag for transcriptional activation. In addition to binding Rb and p300, EID-1 also binds to phosphorylated CREB protein, mediating cAMP gene regulation. EID-1 augments the activity of phosphorylated CREB and activates transcription of cAMP responsive genes as a co-activator. Protein function: Interacts with RB1 and EP300 and acts as a repressor of MYOD1 transactivation. Inhibits EP300 and CBP histone acetyltransferase activity. May be involved in coupling cell cycle exit to the transcriptional activation of genes required for cellular differentiation. May act as a candidate coinhibitory factor for NR0B2 that can be directly linked to transcription inhibitory mechanisms. [The UniProt Consortium]