| http://purl.uniprot.org/citations/11988099 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11988099 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11988099 | http://www.w3.org/2000/01/rdf-schema#comment | "A highly conserved multisubunit enzymic complex, SWI/SNF, participates in the regulation of eukaryote gene expression through its ability to remodel chromatin. While a single component of SWI/SNF, Swi2 or a related protein, can perform this function in vitro, the other components appear to modulate the activity and specificity of the complex in vivo. Here we describe the cloning of hELD/OSA1, a 189 KDa human homologue of Drosophila Eld/Osa protein, a constituent of Drosophila SWI/SNF. By comparing conserved peptide sequences in Eld/Osa homologues we define three domains common to all family members. A putative DNA binding domain, or ARID (AT-rich DNA-interacting domain), may function in targetting SWI/SNF to chromatin. Two other domains unique to Eld/Osa proteins, EHD1 and EHD2, map to the C-terminus. We show that EHD2 mediates binding to Brahma-related gene 1 (BRG1), a human homologue of yeast Swi2. EHD1 and EHD2 also appear capable of interacting with each other. Using an antibody raised against EHD2 of hELD/OSA1, we detected Eld/Osa1 in endogenous SWI/SNF complexes derived from mouse brain."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3640255"xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3640255"xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "Barker N."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "Barker N."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "Olave I.A."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "Olave I.A."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "Clevers H."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "Clevers H."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "Hurlstone A.F."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "Hurlstone A.F."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "van Noort M."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/author | "van Noort M."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/pages | "255-264"xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/pages | "255-264"xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/title | "Cloning and characterization of hELD/OSA1, a novel BRG1 interacting protein."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/title | "Cloning and characterization of hELD/OSA1, a novel BRG1 interacting protein."xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/volume | "364"xsd:string |
| http://purl.uniprot.org/citations/11988099 | http://purl.uniprot.org/core/volume | "364"xsd:string |