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http://purl.uniprot.org/citations/29915238http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29915238http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29915238http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/29915238http://www.w3.org/2000/01/rdf-schema#comment"Biochemical, structural and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) to be a 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 to be more closely related to the JmjC hydroxylases than to the JmjC demethylases. Biophysical and mutation studies show that JMJD7 has a unique dimerization mode, with interactions between monomers involving both N- and C-terminal regions and disulfide bond formation. A proteomic approach identifies two related members of the translation factor (TRAFAC) family of GTPases, developmentally regulated GTP-binding proteins 1 and 2 (DRG1/2), as activity-dependent JMJD7 interactors. Mass spectrometric analyses demonstrate that JMJD7 catalyzes Fe(II)- and 2OG-dependent hydroxylation of a highly conserved lysine residue in DRG1/2; amino-acid analyses reveal that JMJD7 catalyzes (3S)-lysyl hydroxylation. The functional assignment of JMJD7 will enable future studies to define the role of DRG hydroxylation in cell growth and disease."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.org/dc/terms/identifier"doi:10.1038/s41589-018-0071-y"xsd:string
http://purl.uniprot.org/citations/29915238http://purl.org/dc/terms/identifier"doi:10.1038/s41589-018-0071-y"xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Coleman M.L."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Coleman M.L."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Hall C."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Hall C."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Yang M."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Yang M."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Fischer R."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Fischer R."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Schofield C.J."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Schofield C.J."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Struwe W.B."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Struwe W.B."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Davis S."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Davis S."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Ge W."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Ge W."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Kessler B.M."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Kessler B.M."xsd:string
http://purl.uniprot.org/citations/29915238http://purl.uniprot.org/core/author"Ratcliffe P.J."xsd:string