| http://purl.uniprot.org/citations/11948178 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11948178 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11948178 | http://www.w3.org/2000/01/rdf-schema#comment | "We have cloned and characterized a human cDNA that belongs to the histone deacetylase family, which we designate as HDAC11. The predicted HDAC11 amino acid sequence reveals an open reading frame of 347 residues with a corresponding molecular mass of 39 kDa. Sequence analyses of the putative HDAC11 protein indicate that it contains conserved residues in the catalytic core regions shared by both class I and II mammalian HDAC enzymes. Putative orthologues of HDAC11 exist in primate, mouse, Drosophila, and plant. Epitope-tagged HDAC11 protein expressed in mammalian cells displays histone deacetylase activity in vitro. Furthermore, HDAC11's enzymatic activity is inhibited by trapoxin, a known histone deacetylase inhibitor. Multiple tissue Northern blot and real-time PCR experiments show that the high expression level of HDAC11 transcripts is limited to kidney, heart, brain, skeletal muscle, and testis. Epitope-tagged HDAC11 protein localizes predominantly to the cell nucleus. Co-immunoprecipitation experiments indicate that HDAC11 may be present in protein complexes that also contain HDAC6. These results indicate that HDAC11 is a novel and unique member of the histone deacetylase family and it may have distinct physiological roles from those of the known HDACs."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111871200"xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111871200"xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/author | "Gao L."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/author | "Gao L."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/author | "Asselbergs F."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/author | "Asselbergs F."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/author | "Atadja P."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/author | "Atadja P."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/author | "Cueto M.A."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/author | "Cueto M.A."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/pages | "25748-25755"xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/pages | "25748-25755"xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/title | "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/title | "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family."xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11948178 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11948178 |
| http://purl.uniprot.org/citations/11948178 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11948178 |