CREB-binding protein, also known as CREBBP or CBP or KAT3A, (where CREB is cAMP response element-binding protein) is a coactivator encoded by the CREBBPgene in humans, located on chromosome 16p13.3.[5][6] CBP has intrinsic acetyltransferase functions; it is able to add acetyl groups to both transcription factors as well as histone lysines, the latter of which has been shown to alter chromatin structure making genes more accessible for transcription.[7][8][9][10] This relatively unique acetyltransferase activity is also seen in another transcription enzyme, EP300 (p300). Together, they are known as the p300-CBP coactivator family and are known to associate with more than 16,000 genes in humans; however, while these proteins share many structural features, emerging evidence suggests that these two co-activators may promote transcription of genes with different biological functions.[7][11][12]
For example, CBP alone has been implicated in a wide variety of pathophysiologies including colorectal cancer as well as head and neck squamous cell carcinoma. In these diseases, association of CBP with β-catenin has been shown to promote cancer cell proliferation and disease aggressiveness, whereas p300/ β-catenin leads to cell differentiation and/ or apoptosis.[11][13] CBP has also been shown to help modulate liver function via maintenance of energy homeostasis in response to changes in cell nutrition conditions by regulating the activity of transcription factors and genes responsible for lipogenesis and gluconeogenesis.[6] CBP is also implicated in the etiologies of several other diseases including hematologic malignancies and other solid tumors, diabetes, schizophrenia, Alzheimer's disease, depression, and many other neurological conditions.[14][15][16][17][18]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Chan HM, La Thangue NB (July 2001). "p300/CBP proteins: HATs for transcriptional bridges and scaffolds". Journal of Cell Science. 114 (Pt 13): 2363–2373. doi:10.1242/jcs.114.13.2363. PMID11559745.
^Guo P, Chen W, Li H, Li M, Li L (October 2018). "The Histone Acetylation Modifications of Breast Cancer and their Therapeutic Implications". Pathology & Oncology Research. 24 (4): 807–813. doi:10.1007/s12253-018-0433-5. PMID29948617. S2CID47020435.
^Amidfar M, de Oliveira J, Kucharska E, Budni J, Kim YK (September 2020). "The role of CREB and BDNF in neurobiology and treatment of Alzheimer's disease". Life Sciences. 257: 118020. doi:10.1016/j.lfs.2020.118020. PMID32603820. S2CID220287306.