{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(6)"],"submitter":["Wang XS"],"pubmed_abstract":["HOIL-1 is a RING-between-RING-family E3 ubiquitin ligase and a component of the linear ubiquitin chain assembly complex. Although most E3 ubiquitin ligases conjugate ubiquitin to protein lysine sidechains, HOIL-1 has also been reported to ubiquitinate hydroxyl groups in protein serine and threonine sidechains and glucosaccharides, such as glycogen and its building block maltose, in vitro. However, HOIL-1 substrate specificity is currently poorly defined. Here, we show that HOIL-1 is unable to ubiquitinate lysine but can efficiently ubiquitinate serine and a variety of model and physiologically relevant di- and monosaccharides in vitro. We identify a critical catalytic histidine residue, His510, in the flexible catalytic site of HOIL-1 that enables this O-linked ubiquitination and prohibits"],"journal":["Life science alliance"],"pagination":["e202503243"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11962058"],"repository":["biostudies-literature"],"pubmed_title":["The RBR E3 ubiquitin ligase HOIL-1 can ubiquitinate diverse non-protein substrates in vitro."],"pmcid":["PMC11962058"],"pubmed_authors":["Lechtenberg BC","Cerra A","Goddard-Borger ED","Cobbold SA","Mak KHT","Payne RJ","Wang XS","Corcilius L","Jochem M","Silke J","Jiou J","Komander D"],"additional_accession":[]},"is_claimable":false,"name":"The RBR E3 ubiquitin ligase HOIL-1 can ubiquitinate diverse non-protein substrates in vitro.","description":"HOIL-1 is a RING-between-RING-family E3 ubiquitin ligase and a component of the linear ubiquitin chain assembly complex. Although most E3 ubiquitin ligases conjugate ubiquitin to protein lysine sidechains, HOIL-1 has also been reported to ubiquitinate hydroxyl groups in protein serine and threonine sidechains and glucosaccharides, such as glycogen and its building block maltose, in vitro. However, HOIL-1 substrate specificity is currently poorly defined. Here, we show that HOIL-1 is unable to ubiquitinate lysine but can efficiently ubiquitinate serine and a variety of model and physiologically relevant di- and monosaccharides in vitro. We identify a critical catalytic histidine residue, His510, in the flexible catalytic site of HOIL-1 that enables this O-linked ubiquitination and prohibits","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-06-02T06:51:30.724Z","creation":"2025-07-01T03:05:35.733Z"},"accession":"S-EPMC11962058","cross_references":{"pubmed":["40169258"],"doi":["10.26508/lsa.202503243"]}}