"Ubiquitin regulates various cellular processes in eukaryotic cells, and different ubiquitins connected in different ways form complex topological structures of polyubiquitin chains that determine the fate of proteins, including targeting to proteasomal degradation, protein transport, DNA damage repair, immune signaling, etc. Different ubiquitins can be recognized by certain ubiquitin-associated domains (UBAs). UBA domains have been identified in 10 members of the mammalian AMPK-related kinase family (MARK1, MARK2, MARK3, MARK4, SIK, QIK, QSK, BRSK1, BRSK2, SNRK) located immediately after their kinase domains. In this study, we found that the UBA domains of hSNRK and hMARK3 in this protein kinase family can bind to ubiquitin both in vitro and in cell lysates, and hMARK3-UBA can bind to four types of tetraubiquitin chains: M1, K11, K27, and K63. To confirm the reliability of this binding, we constructed hMARK3-UBA mutant proteins, and the results showed that the mutants lost the ability to bind to M1-linked ubiquitin chains."