Involved in transcriptional repression. May act by repressing E2F-regulated genes in mature differentiated cells, but is not an antagonist of E2FA. Restricts cell division and is involved in the coordination between cell proliferation and endoreduplication during development. May play a role during the transition from skotomorphogenesis to photomorphogenesis. Regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(SKP2A) complex. Heterodimer with DP proteins. Interacts preferentially with DPB, but also with DPA. No interaction with DPB when phosphorylated. Interacts with SKP2A, CDKA-1 and maize retinoblastoma-related protein RBR1. Component of a DREAM-like complex which modulates a variety of developmentally regulated genes and of the mitotic genes in proliferating and differentiated cells. Interacts with MYB3R3 at later stages of leaves development (PubMed:26069325). Interaction with either DPA or DPB are unable to induce a nuclear localization. A number of isoforms are produced. According to EST sequences. Expressed in meristematic areas, vascular tissues, apical part of the roots, cotyledons, upper region of the hypocotyls, trichomes, young flower buds and pollen grains. Expressed in a cell cycle-dependent manner. Not detected at the G1/S transition, but increases during the progression into S phase and peaks after the passage into G2. Down-regulated by light. The N-terminal region (1-100) is important for both SKP2A binding and ubiquitin-mediated degradation. Phosphorylated by cyclin-dependent kinase. Phosphorylation is necessary to target E2FC for proteolysis. Belongs to the E2F/DP family.