Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

CBP/p300 Coactivators

  • Andrew S. Turnell
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_899-2

Definition

CBP is an acronym for cAMP-regulated-enhancer (CRE)-binding protein (CREB)-binding protein. p300 is a protein that is highly homologous to CBP and has been named according to its approximate molecular weight. Coactivators are a group of cellular proteins that enhance transcription factor-dependent transcriptional activation.

Characteristics

CBP was initially identified as an auxiliary cofactor required for the CREB-mediated activation of cAMP-stimulated gene transcription. CBP binds specifically, at CREs, to an activated CREB species which has been suitably modified through phosphorylation by the cAMP-responsive protein kinase, PKA. p300 was subsequently characterized, independently, upon the basis of its interaction with the protein product of the adenoviral transforming E1Agene and, like CBP, can function as a coactivator in CREB-mediated transcriptional activation. CBP, akin to p300, also binds to E1A. CBP and p300 are highly related at the amino acid sequence level,...

Keywords

Acute Myeloid Leukemia Esophageal Squamous Cell Carcinoma Mixed Lineage Leukemia Subunit APC5 Identical Enzymatic Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

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See Also

  1. (2012) Acetyltransferase. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 17. doi: 10.1007/978-3-642-16483-5_27Google Scholar
  2. (2012) Cell cycle. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 737. doi: 10.1007/978-3-642-16483-5_994Google Scholar
  3. (2012) Chromatin. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 825. doi: 10.1007/978-3-642-16483-5_1125Google Scholar
  4. (2012) Differentiation. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 1113. doi: 10.1007/978-3-642-16483-5_1616Google Scholar
  5. (2012) E3 ubiquitin ligase. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 1184. doi: 10.1007/978-3-642-16483-5_1771Google Scholar
  6. (2012) E4 ubiquitin ligase. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 1184. doi: 10.1007/978-3-642-16483-5_1772Google Scholar
  7. (2012) Loss of heterozygosity. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, pp 2075–2076. doi: 10.1007/978-3-642-16483-5_3415Google Scholar
  8. (2012) P53. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 2747. doi: 10.1007/978-3-642-16483-5_4331Google Scholar
  9. (2012) Transcription. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 3752. doi: 10.1007/978-3-642-16483-5_5899Google Scholar
  10. (2012) Transformation. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, pp 3757–3758. doi: 10.1007/978-3-642-16483-5_5913Google Scholar
  11. (2012) Tumor suppressor. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 3803. doi: 10.1007/978-3-642-16483-5_6056Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Cancer Research UK Institute for Cancer Studies, The Medical SchoolThe University of BirminghamEdgbastonUK