When WNT binds to its receptor Frizzled (FZD) to activate the signalling, Dishevelled (DVL), the central component of Wnt signalling, is phosphorylated by redundant Casein kinase 1 (CK1) isoforms ε or δ, to transduce the signal downstream. Here, we mutated key serine/threonine residues in the intrinsically disordered region (IDR) between the PDZ and DEP domains. Either to alanine to prevent phosphorylation, or to glutamic acid to mimic phosphorylation, or we deleted these residues altogether. We investigated the impact of these mutations on DVL’s interactome using proximity labeling with TurboID-tagged fusion proteins at N-terminus of DVL.