PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22659170-6 2012 AIRE with mutations that mimicked acetylated K243 and K253 in the SAND domain had reduced transactivation activity and accumulated into fewer and larger nuclear bodies, whereas mutations that mimicked the unacetylated lysines were functionally similar to wild-type AIRE. Lysine 218-225 autoimmune regulator Homo sapiens 0-4 25158603-3 2014 RESULTS: In this study, we have precisely mapped, by mass spectrometry experiments, the sites of protein acetylation and, by mutagenesis assays, we have described a set of acetylated lysines as being crucial in influencing the subcellular localization of AIRE. Lysine 183-190 autoimmune regulator Homo sapiens 255-259 25158603-4 2014 Furthermore, we have also determined that the de-acetyltransferase enzymes HDAC1-2 are involved in the lysine de-acetylation of AIRE. Lysine 103-109 autoimmune regulator Homo sapiens 128-132 25158603-5 2014 CONCLUSIONS: On the basis of our results and those reported in literature, we propose a model in which lysines acetylation increases the stability of AIRE in the nucleus. Lysine 103-110 autoimmune regulator Homo sapiens 150-154 22036612-7 2011 In contrast, a positive correlation between AIRE expression and histone H3 lysine 4 trimethylation, an active chromatin mark, was found in the AIRE promoter in human and mouse TECs. Lysine 75-81 autoimmune regulator Homo sapiens 44-48 22036612-7 2011 In contrast, a positive correlation between AIRE expression and histone H3 lysine 4 trimethylation, an active chromatin mark, was found in the AIRE promoter in human and mouse TECs. Lysine 75-81 autoimmune regulator Homo sapiens 143-147 19446523-4 2009 The structure reveals a detailed network of interactions between the protein and the amino-terminal residues of histone H3, and particularly key electrostatic interactions of a conserved aspartic acid 297 in AIRE with the unmodified lysine 4 of histone H3 (H3K4). Lysine 233-239 autoimmune regulator Homo sapiens 208-212 16403019-7 2006 Furthermore, we show by in vitro binding assays that AIRE interacts with multiple members of the nuclear transport receptor importin alpha family, mainly alpha1, alpha3, and alpha5, and that these interactions depend on the intactness of the Arg-Lys-rich NLS of AIRE. Lysine 246-249 autoimmune regulator Homo sapiens 53-57