Human ether à go‐go potassium channels (hEAG1) open in response to membrane depolarization and they are inhibited by Ca2+/calmodulin (CaM), presumably binding to the C‐terminal domain of the channel subunits. Deletion of the cytosolic N‐terminal domain resulted in complete abolition of Ca2+/CaM sensitivity suggesting the existence of further CaM binding sites. A peptide array‐based screen of the entire cytosolic protein of hEAG1 identified three putative CaM‐binding domains, two in the C‐terminus (BD‐C1: 674–683, BD‐C2: 711–721) and one in the N‐terminus (BD‐N: 151–165). Binding of GST‐fusion proteins to Ca2+/CaM was assayed with fluorescence correlation spectroscopy, surface plasmon resonance spectroscopy and precipitation assays. In the presence of Ca2+, BD‐N and BD‐C2 provided dissociation constants in the nanomolar range, BD‐C1 bound with lower affinity. Mutations in the binding domains reduced inhibition of the functional channels by Ca2+/CaM. Employment of CaM‐EF‐hand mutants showed that CaM binding to the N‐ and C‐terminus are primarily dependent on EF‐hand motifs 3 and 4. Hence, closure of EAG channels presumably requires the binding of multiple CaM molecules in a manner more complex than previously assumed.