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http://purl.uniprot.org/citations/15647280http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15647280http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15647280http://www.w3.org/2000/01/rdf-schema#comment"The multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase (HAT) complex performs critical functions in a variety of cellular processes including transcriptional activation, double strand DNA break repair, and apoptosis. We previously isolated the TRRAP/TIP60 complex from HeLa cells (Cai, Y., Jin, J., Tomomori-Sato, C., Sato, S., Sorokina, I., Parmely, T. J., Conaway, R. C., and Conaway, J. W. (2003) J. Biol. Chem. 278, 42733-42736). Analysis of proteins present in preparations of the TRRAP/TIP60 complex led to the identification of several new subunits, as well as several potential subunits including the YL1 protein. Here we present evidence that the YL1 protein is a previously unrecognized subunit of the TRRAP/TIP60 HAT complex. In addition, we present evidence that YL1 is also a component of a novel mammalian multiprotein complex that includes the SNF2-related helicase SRCAP and resembles the recently described Saccharomyces cerevisiae SWR1 chromatin remodeling complex. Taken together, our findings identify the YL1 protein as a new subunit of the TRRAP/TIP60 HAT complex, and they suggest that YL1 plays multiple roles in chromatin modification and remodeling in cells."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m500001200"xsd:string
http://purl.uniprot.org/citations/15647280http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m500001200"xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Florens L."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Florens L."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Jin J."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Jin J."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Cai Y."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Cai Y."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Washburn M.P."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Washburn M.P."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Swanson S.K."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Swanson S.K."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Workman J.L."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Workman J.L."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Conaway J.W."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Conaway J.W."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Conaway R.C."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Conaway R.C."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Kusch T."xsd:string
http://purl.uniprot.org/citations/15647280http://purl.uniprot.org/core/author"Kusch T."xsd:string