Invading virus is recognized by one of pattern recognition receptors, RIG-I-like receptor (RLR), to activate antiviral RLR signaling pathway. Abnormal activation of PRRs will lead to chronic inflammation, immune organ damage, and even autoimmune diseases. In order to prevent the premature or excessive activation of antiviral signals, the body has established a perfect regulatory system to prevent the disorder of signal transduction process. Post-translational modification (PTM) of proteins is a key mechanism for regulating the stability and activity of pattern recognition receptors and their downstream signaling proteins, while ubiquitination (UB) is an important part of protein post-translational modification in antiviral signaling pathways and has extensively studied. Of these, K48- and K63-linked ubiquitination is the most common:K48-linked ubiquitin chains can cause degradation of target proteins via the proteasomal pathway, while K63-linked ubiquitin chains can promote protein activation and cell signaling. RIG-I, MAVS, TBK1 and TRAF family member proteins are the signaling molecules of RLR signaling, and the ubiquitination mechanism of these proteins has also been studied. This paper discusses the research progress of K48 and K63 ubiquitination in antiviral immune signaling pathways, especially the ubiquitination modification of proteins in signaling pathways triggered by RIG-I-like receptors.