| http://purl.uniprot.org/citations/15701600 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15701600 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15701600 | http://www.w3.org/2000/01/rdf-schema#comment | "MBD2 and MBD3 are two proteins that contain methyl-CpG binding domains and have a transcriptional repression function. Both proteins are components of a large CpG-methylated DNA binding complex named MeCP1, which consists of the nucleosome remodeling and histone deacetylase complex Mi2-NuRD and MBD2. MBD3L2 (methyl-CpG-binding protein 3-like 2) is a protein with substantial homology to MBD2 and MBD3, but it lacks the methyl-CpG-binding domain. Unlike MBD3L1, which is specifically expressed in haploid male germ cells, MBD3L2 expression is more widespread. MBD3L2 interacts with MBD3 in vitro and in vivo, co-localizes with MBD3 but not MBD2, and does not localize to methyl-CpG-rich regions in the nucleus. In glutathione S-transferase pull-down assays, MBD3L2 is found associated with several known components of the Mi2-NuRD complex, including HDAC1, HDAC2, MTA1, MBD3, p66, RbAp46, and RbAp48. Gel shift experiments with nuclear extracts and a CpG-methylated DNA probe indicate that recombinant MBD3L2 can displace a form of the MeCP1 complex from methylated DNA. MBD3L2 acts as a transcriptional repressor when tethered to a GAL4-DNA binding domain. Repression by GAL4-MBD3L2 is relieved by MBD2 and vice versa, and repression by MBD2 from a methylated promoter is relieved by MBD3L2. The data are consistent with a role of MBD3L2 as a transcriptional modulator that can interchange with MBD2 as an MBD3-interacting component of the NuRD complex. Thus, MBD3L2 has the potential to recruit the MeCP1 complex away from methylated DNA and reactivate transcription."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m413492200"xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m413492200"xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Li H."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Li H."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Jiang C.-L."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Jiang C.-L."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Jin S.-G."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Jin S.-G."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Pfeifer G.P."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Pfeifer G.P."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Rauch T."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/author | "Rauch T."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/pages | "12700-12709"xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/pages | "12700-12709"xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/title | "MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/title | "MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing."xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/volume | "280"xsd:string |
| http://purl.uniprot.org/citations/15701600 | http://purl.uniprot.org/core/volume | "280"xsd:string |