| http://purl.uniprot.org/citations/18263876 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18263876 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18263876 | http://www.w3.org/2000/01/rdf-schema#comment | "Metnase, also known as SETMAR, is a SET and transposase fusion protein with an undefined role in mammalian DNA repair. The SET domain is responsible for histone lysine methyltransferase activity at histone 3 K4 and K36, whereas the transposase domain possesses 5'-terminal inverted repeat (TIR)-specific DNA binding, DNA looping, and DNA cleavage activities. Although the transposase domain is essential for Metnase function in DNA repair, it is not clear how a protein with sequence-specific DNA binding activity plays a role in DNA repair. Here, we show that human homolog of the ScPSO4/PRP19 (hPso4) forms a stable complex with Metnase on both TIR and non-TIR DNA. The transposase domain essential for Metnase-TIR interaction is not sufficient for its interaction with non-TIR DNA in the presence of hPso4. In vivo, hPso4 is induced and co-localized with Metnase following ionizing radiation treatment. Cells treated with hPso4-siRNA failed to show Metnase localization at DSB sites and Metnase-mediated stimulation of DNA end joining coupled to genomic integration, suggesting that hPso4 is necessary to bring Metnase to the DSB sites for its function(s) in DNA repair."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m800150200"xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m800150200"xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Lee S.H."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Lee S.H."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Lee Y.J."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Lee Y.J."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Park S.J."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Park S.J."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Hromas R.A."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Hromas R.A."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Beck B.D."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Beck B.D."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Roman Y."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/author | "Roman Y."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/pages | "9023-9030"xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/pages | "9023-9030"xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/title | "Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair."xsd:string |
| http://purl.uniprot.org/citations/18263876 | http://purl.uniprot.org/core/title | "Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair."xsd:string |