| http://purl.uniprot.org/citations/29563586 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/29563586 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/29563586 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/29563586 | http://www.w3.org/2000/01/rdf-schema#comment | "Oxygenase-catalysed post-translational modifications of basic protein residues, including lysyl hydroxylations and Nε-methyl lysyl demethylations, have important cellular roles. Jumonji-C (JmjC) domain-containing protein 5 (JMJD5), which genetic studies reveal is essential in animal development, is reported as a histone Nε-methyl lysine demethylase (KDM). Here we report how extensive screening with peptides based on JMJD5 interacting proteins led to the finding that JMJD5 catalyses stereoselective C-3 hydroxylation of arginine residues in sequences from human regulator of chromosome condensation domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6). High-resolution crystallographic analyses reveal overall fold, active site and substrate binding/product release features supporting the assignment of JMJD5 as an arginine hydroxylase rather than a KDM. The results will be useful in the development of selective oxygenase inhibitors for the treatment of cancer and genetic diseases."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-018-03410-w"xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-018-03410-w"xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Islam S."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Islam S."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Schofield C.J."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Ge W."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Ge W."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Hopkinson R.J."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Hopkinson R.J."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Chowdhury R."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Chowdhury R."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Markolovic S."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Markolovic S."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Wilkins S.E."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Wilkins S.E."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Gannon J.M."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/author | "Gannon J.M."xsd:string |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/29563586 | http://purl.uniprot.org/core/name | "Nat. Commun."xsd:string |