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http://purl.uniprot.org/citations/10673037http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10673037http://www.w3.org/2000/01/rdf-schema#comment"Reversible histone acetylation plays an important role for chromatin structure and gene expression. The acetylation state of core histones is controlled by histone acetyltransferases and histone deacetylases. Here we report the cloning and characterization of the mouse histone deacetylase 1 (HDAC1) gene. The mouse genome contains several HDAC1-related structures representing the HDAC1 gene and at least three pseudogenes. The HDAC1 gene comprises 14 exons ranging from 49 to 539 bp. Interestingly the murine HDAC1 gene strongly resembles the previously published mouse HDAC2 gene (Zeng et al., J. Biol. Chem. 273 (1998) 28921-28930). The sizes of ten of the 14 exons are identical for both genes and the splicing sites for 11 introns align in identical positions suggesting a gene duplication event. The HDAC1 gene is located only 128 bp downstream from the MARCKS-related protein (MRP) gene in a tail-to-tail orientation. The murine MRP gene was previously mapped to a conserved gene cluster on chromosome 4 sharing linkage homology to human chromosome 1p32-36. The genes for HDAC1 and MRP are co-expressed in a variety of cell types. In the genome of 129SV mice the largest intervening sequence of the HDAC1 gene, intron 3, harbors a complete copy of the endogenous retrovirus MuERV-L. In contrast the HDAC1 gene in other mouse strains such as C57B16, C3H/An and C-RY lacks the retrovirus. Our study provides useful tools for future targeted gene disruption studies."xsd:string
http://purl.uniprot.org/citations/10673037http://purl.org/dc/terms/identifier"doi:10.1016/s0167-4781(99)00203-1"xsd:string
http://purl.uniprot.org/citations/10673037http://purl.uniprot.org/core/author"Seiser C."xsd:string
http://purl.uniprot.org/citations/10673037http://purl.uniprot.org/core/author"Bartl S."xsd:string
http://purl.uniprot.org/citations/10673037http://purl.uniprot.org/core/author"Khier H."xsd:string
http://purl.uniprot.org/citations/10673037http://purl.uniprot.org/core/author"Schuettengruber B."xsd:string
http://purl.uniprot.org/citations/10673037http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10673037http://purl.uniprot.org/core/name"Biochim Biophys Acta"xsd:string
http://purl.uniprot.org/citations/10673037http://purl.uniprot.org/core/pages"365-373"xsd:string
http://purl.uniprot.org/citations/10673037http://purl.uniprot.org/core/title"Molecular cloning and characterization of the mouse histone deacetylase 1 gene: integration of a retrovirus in 129SV mice."xsd:string
http://purl.uniprot.org/citations/10673037http://purl.uniprot.org/core/volume"1489"xsd:string
http://purl.uniprot.org/citations/10673037http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10673037
http://purl.uniprot.org/citations/10673037http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10673037
http://purl.uniprot.org/uniprot/#_O09106-mappedCitation-10673037http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10673037
http://purl.uniprot.org/uniprot/#_P28667-mappedCitation-10673037http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10673037
http://purl.uniprot.org/uniprot/#_Q58E49-mappedCitation-10673037http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10673037
http://purl.uniprot.org/uniprot/P28667http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10673037
http://purl.uniprot.org/uniprot/O09106http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10673037
http://purl.uniprot.org/uniprot/Q58E49http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10673037