Fig. 1.
Fig. 1. Structure of CBP adapted from Shikama et al.8. / Not all known CBP interacting proteins are shown. Amino acid numbers are approximate. HAT, histone acetyltransferase domain; CH, cysteine/histidine-rich region; BROMO, Bromodomain. Bromodomains are found in most histone acetyltransferases and in many chromatin-associated factors. Bromodomains specifically bind to acetylated lysine.167 CBP and p300 interact with tissue-specific (eg, MyoD), broadly expressed (eg, nuclear receptors), and general (eg, TFIIB and TBP) transcription factors. In addition, CBP and p300 interact with oncoproteins, including c-Jun and c-Fos, and tumor supressor proteins such as p53. CBP and p300 also interact with other HAT-containing molecules, such as p/CAF, SRC-1, and ACTR. Finally, CBP and p300 regulate the activity of signal-dependent transcriptional activators such as CREB and the STATs.

Structure of CBP adapted from Shikama et al.8 

Not all known CBP interacting proteins are shown. Amino acid numbers are approximate. HAT, histone acetyltransferase domain; CH, cysteine/histidine-rich region; BROMO, Bromodomain. Bromodomains are found in most histone acetyltransferases and in many chromatin-associated factors. Bromodomains specifically bind to acetylated lysine.167 CBP and p300 interact with tissue-specific (eg, MyoD), broadly expressed (eg, nuclear receptors), and general (eg, TFIIB and TBP) transcription factors. In addition, CBP and p300 interact with oncoproteins, including c-Jun and c-Fos, and tumor supressor proteins such as p53. CBP and p300 also interact with other HAT-containing molecules, such as p/CAF, SRC-1, and ACTR. Finally, CBP and p300 regulate the activity of signal-dependent transcriptional activators such as CREB and the STATs.

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