Schematic diagram of the EKLF protein. Shown are N-terminal proline-rich and C-terminal (C2H2 zinc fingers; ZnF) DNA-binding domains. EKLF activity is modulated by posttranslational modifications that promote protein-protein interactions. The transactivation activity of EKLF (top) is associated with the phosphorylation status of threonine 41 and acetylation of lysine 288.^16-18  Acetylated K288 is involved in interactions with the chromatin-remodeling SWI/SNF-related complex (E-RC1) through the BRG1 subunit.^19-21  The repression activity of EKLF (bottom) relies on an acetylation of K302, enabling its interaction with corepressors Sin3a and HDAC1.^91,92  Sumoylation of K74 serves to tether components of NuRD repression complex via interaction with Mi2β and HDAC1.²³  EKLF is also a substrate for ubiquitination; however, this modification is not specific to any particular internal lysine.⁹³