Cux1 (CUTL1, CDP, CDP/Cux) is a homeodomain protein that in humans is encoded by the CUX1gene.1234
The protein encoded by this gene is a member of the homeodomain family of DNA binding proteins. It regulates gene expression, morphogenesis, and differentiation and it also plays a role in cell cycle progression, particularly at S-phase. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined, and the p200 isoform of Cux1 is processed proteolytically to smaller active isoforms, such as p110.4 Cux1 DNA binding is stimulated by activation of the PAR2/F2RL1 cell-surface G-protein-coupled receptor in fibroblasts and breast-cancer epithelial cells to regulate Matrix metalloproteinase 10, Interleukin1-alpha, and Cyclo-oxygenase 2 (COX2) genes.5
^Gupta, Sunita; Luong Mai X, Bleuming Sylvia A, Miele Angela, Luong Michael, Young Daniel, Knudsen Erik S, Van Wijnen Andre J, Stein Janet L, Stein Gary S (September 2003). "Tumor suppressor pRB functions as a co-repressor of the CCAAT displacement protein (CDP/cut) to regulate cell cycle controlled histone H4 transcription". J. Cell. Physiol. (United States) 196 (3): 541–56. doi:10.1002/jcp.10335. ISSN0021-9541. PMID12891711.
Ottolenghi S, Mantovani R, Nicolis S, et al. (1990). "DNA sequences regulating human globin gene transcription in nondeletional hereditary persistence of fetal hemoglobin". Hemoglobin13 (6): 523–41. doi:10.3109/03630268908993104. PMID2481658.
Nepveu A (2001). "Role of the multifunctional CDP/Cut/Cux homeodomain transcription factor in regulating differentiation, cell growth and development". Gene270 (1–2): 1–15. doi:10.1016/S0378-1119(01)00485-1. PMID11403998.
Neufeld EJ, Skalnik DG, Lievens PM, Orkin SH (1993). "Human CCAAT displacement protein is homologous to the Drosophila homeoprotein, cut". Nat. Genet.1 (1): 50–5. doi:10.1038/ng0492-50. PMID1301999.
Chernousov MA, Stahl RC, Carey DJ (1996). "Schwann cells secrete a novel collagen-like adhesive protein that binds N-syndecan". J. Biol. Chem.271 (23): 13844–53. doi:10.1074/jbc.271.23.13844. PMID8662884.
Lievens PM, Tufarelli C, Donady JJ, et al. (1997). "CASP, a novel, highly conserved alternative-splicing product of the CDP/cut/cux gene, lacks cut-repeat and homeo DNA-binding domains, and interacts with full-length CDP in vitro". Gene197 (1–2): 73–81. doi:10.1016/S0378-1119(97)00243-6. PMID9332351.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Chattopadhyay S, Whitehurst CE, Chen J (1998). "A nuclear matrix attachment region upstream of the T cell receptor beta gene enhancer binds Cux/CDP and SATB1 and modulates enhancer-dependent reporter gene expression but not endogenous gene expression". J. Biol. Chem.273 (45): 29838–46. doi:10.1074/jbc.273.45.29838. PMID9792700.
Martin-Soudant N, Drachman JG, Kaushansky K, Nepveu A (2000). "CDP/Cut DNA binding activity is down-modulated in granulocytes, macrophages and erythrocytes but remains elevated in differentiating megakaryocytes". Leukemia14 (5): 863–73. doi:10.1038/sj.leu.2401764. PMID10803519.
Santaguida M, Ding Q, Bérubé G, et al. (2002). "Phosphorylation of the CCAAT displacement protein (CDP)/Cux transcription factor by cyclin A-Cdk1 modulates its DNA binding activity in G(2)". J. Biol. Chem.276 (49): 45780–90. doi:10.1074/jbc.M107978200. PMID11584018.
Dintilhac A, Bernués J (2002). "HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences". J. Biol. Chem.277 (9): 7021–8. doi:10.1074/jbc.M108417200. PMID11748221.