TY - JOUR AB - CREB binding protein (CBP) is a transcriptional cofactor with intrinsic histone acetyl transferase activity (HAT). We have observed that CBP interacts with BRCA2 and mediates post-translational glycosylation of BRCA2. The binding of CBP to the amino-terminal region of BRCA2 is necessary for the glycosylation at residue 272 of BRCA2. Digestion with peptide N-glycosidase F indicates that the glycosylation of BRCA2 is N-linked. It is possible that this novel CBP-mediated post-translational N-glycosylation activity alters the conformation of CBP-interacting proteins, leading to regulation of gene expression, cell growth and differentiation. AD - Cancer Biology Program, Department of OB/GYN, Morehouse School of Medicine, Georgia Cancer Center for Excellence, Grady Health System, Atlanta, GA 30303, USA null AU - Siddique,Habibur AU - Rao,Veena,N. AU - Reddy,E.,Shyam P. DA - 2009/08/01 DO - 10.3892/ijo_00000351 EP - 391 IS - 2 JO - Int J Oncol PY - 2009 SN - 1019-6439 1791-2423 SP - 387 ST - CBP-mediated post-translational N-glycosylation of BRCA2 T2 - International Journal of Oncology TI - CBP-mediated post-translational N-glycosylation of BRCA2 UR - https://doi.org/10.3892/ijo_00000351 VL - 35 ER -