| http://purl.uniprot.org/citations/22570628 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22570628 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22570628 | http://www.w3.org/2000/01/rdf-schema#comment | "Epigenetic modifications influence gene expression and provide a unique mechanism for fine-tuning cellular differentiation and development in multicellular organisms. Here we report on the biological functions of UTX-1, the Caenorhabditis elegans homologue of mammalian UTX, a histone demethylase specific for H3K27me2/3. We demonstrate that utx-1 is an essential gene that is required for correct embryonic and postembryonic development. Consistent with its homology to UTX, UTX-1 regulates global levels of H3K27me2/3 in C. elegans. Surprisingly, we found that the catalytic activity is not required for the developmental function of this protein. Biochemical analysis identified UTX-1 as a component of a complex that includes SET-16(MLL), and genetic analysis indicates that the defects associated with loss of UTX-1 are likely mediated by compromised SET-16/UTX-1 complex activity. Taken together, these results demonstrate that UTX-1 is required for many aspects of nematode development; but, unexpectedly, this function is independent of its enzymatic activity."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pgen.1002647"xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pgen.1002647"xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Salcini A.E."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Salcini A.E."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Sidoli S."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Sidoli S."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Di Schiavi E."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Di Schiavi E."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Vandamme J."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Vandamme J."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Lettier G."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Lettier G."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Noerregaard Jensen O."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/author | "Noerregaard Jensen O."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/name | "PLoS Genet."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/name | "PLoS Genet."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/pages | "E1002647"xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/pages | "E1002647"xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/title | "The C. elegans H3K27 demethylase UTX-1 is essential for normal development, independent of its enzymatic activity."xsd:string |
| http://purl.uniprot.org/citations/22570628 | http://purl.uniprot.org/core/title | "The C. elegans H3K27 demethylase UTX-1 is essential for normal development, independent of its enzymatic activity."xsd:string |