Linear ubiquitin chains play pivotal roles in immune signaling by augmenting NF‐κB activation and suppressing programmed cell death induced by various stimuli. A20‐binding inhibitor of NF‐κB 1 (ABIN1) binds to linear ubiquitin chains and attenuates NF‐κB activation and cell death induction. Although interactions with linear ubiquitin chains are thought to play a role in ABIN1‐mediated suppression of NF‐κB and cell death, the underlying molecular mechanisms remain unclear. Here, we show that upon stimulation by Toll‐like receptor (TLR) ligands, ABIN1 is phosphorylated on Ser 83 and functions as a selective autophagy receptor. ABIN1 recognizes components of the MyD88 signaling complex via interaction with linear ubiquitin chains conjugated to components of the complex in TLR signaling, which leads to autophagic degradation of signaling proteins and attenuated NF‐κB signaling. Our current findings indicate that phosphorylation and linear ubiquitination also play a role in downregulation of signaling via selective induction of autophagy.