{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Brewitz L"],"funding":["Cancer Research UK","Wellcome Trust","Biotechnology and Biological Sciences Research Council"],"pagination":["102129"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9293771"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["298(8)"],"pubmed_abstract":["Epidermal growth factor-like domains (EGFDs) have important functions in cell-cell signaling. Both secreted and cell surface human EGFDs are subject to extensive modifications, including aspartate and asparagine residue C3-hydroxylations catalyzed by the 2-oxoglutarate oxygenase aspartate/asparagine-β-hydroxylase (AspH). Although genetic studies show AspH is important in human biology, studies on its physiological roles have been limited by incomplete knowledge of its substrates. Here, we redefine the consensus sequence requirements for AspH-catalyzed EGFD hydroxylation based on combined analysis of proteomic mass spectrometric data and mass spectrometry-based assays with isolated AspH and peptide substrates. We provide cellular and biochemical evidence that the preferred site of EGFD hydr"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Combined proteomic and biochemical analyses redefine the consensus sequence requirement for epidermal growth factor-like domain hydroxylation."],"pmcid":["PMC9293771"],"funding_grant_id":["C8717/A18245","28285","106244/Z/14/Z","BB/R000344/1","BB/J003018/1"],"pubmed_authors":["Onisko BC","Brewitz L","Schofield CJ"],"additional_accession":[]},"is_claimable":false,"name":"Combined proteomic and biochemical analyses redefine the consensus sequence requirement for epidermal growth factor-like domain hydroxylation.","description":"Epidermal growth factor-like domains (EGFDs) have important functions in cell-cell signaling. Both secreted and cell surface human EGFDs are subject to extensive modifications, including aspartate and asparagine residue C3-hydroxylations catalyzed by the 2-oxoglutarate oxygenase aspartate/asparagine-β-hydroxylase (AspH). Although genetic studies show AspH is important in human biology, studies on its physiological roles have been limited by incomplete knowledge of its substrates. Here, we redefine the consensus sequence requirements for AspH-catalyzed EGFD hydroxylation based on combined analysis of proteomic mass spectrometric data and mass spectrometry-based assays with isolated AspH and peptide substrates. We provide cellular and biochemical evidence that the preferred site of EGFD hydr","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-05-09T20:47:49.906Z","creation":"2022-08-08T22:20:25.957Z"},"accession":"S-EPMC9293771","cross_references":{"pubmed":["35700824"],"doi":["10.1016/j.jbc.2022.102129"]}}