Disabled-2 (Dab2) is a clathrin associated sorting protein (CLASP), which functions as an adaptor protein, particularly important in the early stages of clathrin mediated endocytosis (CME), one of the major uptake pathways of eukaryotic cells[1,2]. The CME cargo is often transmembrane receptors and consequently CME, and thus also Dab2, play vital roles in cell signaling. In the CME process, Dab2, other CLASPs, and the major adaptor protein AP-2 form an intricate interaction network, that bridges between clathrin, the membrane, and the cargo, in the end resulting in the clathrin coated vesicle to be internalized[2]. While AP-2 is usually required for successful CME, Dab2 is a special CLASP as it has been shown to mediate CME independently of AP-2[3]. Dab2 comprises a folded N-terminal domain (around 150 residues) containing binding sites for membrane components and receptor cargo, which is followed by a long intrinsically disordered region (IDR, around 600 residues). The IDR contains multiple, and repetitive, small amino acid motifs that are expected binding sites for clathrin, AP-2, and other CLASPs, in addition to multiple (putative) phosphorylation sites. We use solution NMR to study Dab2’s conformational dynamics, its interaction with CME partner proteins, and the effects of differential phosphorylations, which will shed light on Dab2’s function in both the AP-2 dependent and independent CME protein network. A region of the Dab2 IDR is found to sample multiple local conformations on a slow exchange time scale, and interaction studies with EH domains of the partner CLASP Eps15 reveal multiple interaction sites with apparent different dynamics.