| http://purl.uniprot.org/citations/18713399 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18713399 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18713399 | http://www.w3.org/2000/01/rdf-schema#comment | "Histone methylation homeostasis is achieved by controlling the balance between methylation and demethylation to maintain chromatin function and developmental regulation. In animals, a conserved Jumonji C (JmjC) domain was found in a large group of histone demethylases. However, it is still unclear whether plants also contain the JmjC domain-containing active histone demethylases. Here we performed genome-wide screen and phylogenetic analysis of JmjC domain-containing proteins in the dicot plant, Arabidopsis, and monocot plant rice, and found 21 and 20 JmjC domain-containing, respectively. We also examined the expression of JmjC domain-containing proteins and compared them to human JmjC counterparts for potential enzymatic activity. The spatial expression patterns of the Arabidopsis JmjC domain-containing genes revealed that they are all actively transcribed genes. These active plant JmjC domain-containing genes could possibly function in epigenetic regulation to antagonize the activity of the large number of putative SET domain-containing histone methyltransferase activity to dynamically regulate histone methylation homeostasis."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1744-7909.2008.00692.x"xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1744-7909.2008.00692.x"xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Cui X."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Cui X."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Cao X."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Cao X."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Liu C."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Liu C."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Li G."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Li G."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Lu F."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Lu F."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Wang X.-J."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/author | "Wang X.-J."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/name | "J. Integr. Plant Biol."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/name | "J. Integr. Plant Biol."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/pages | "886-896"xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/pages | "886-896"xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/title | "Comparative analysis of JmjC domain-containing proteins reveals the potential histone demethylases in Arabidopsis and rice."xsd:string |
| http://purl.uniprot.org/citations/18713399 | http://purl.uniprot.org/core/title | "Comparative analysis of JmjC domain-containing proteins reveals the potential histone demethylases in Arabidopsis and rice."xsd:string |