PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25123533-2 2014 Although many lysine acetyltransferases (KATs) have been characterized as being capable of acetylating multiple lysine residues on histones, how different factors such as enzyme complexes or external stimuli (e.g. KAT activators or inhibitors) alter KAT specificity remains elusive. Lysine 14-20 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 41-44 28161493-8 2017 In this review, we summarize the current basic knowledge on the specific roles of lysine acetyltransferase (KAT) and lysine deacetylase (KDAC) complexes in brain development and the different neurodevelopmental disorders that are associated with dysfunctional lysine (de)acetylation machineries. Lysine 82-88 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 108-111 27990297-5 2016 We show that the mitochondrial stress-induced transcription coactivator hnRNAP2 acetylates Lys 8 of H4 through an intrinsic histone lysine acetyltransferase (KAT) activity with Arg 48 and Arg 50 of hnRNAP2 being essential for acetyl-CoA binding and acetyltransferase activity. Lysine 91-94 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 158-161 31087293-0 2019 Measurement and Analysis of Lysine Acetylation by KAT Complexes In Vitro and In Vivo. Lysine 28-34 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 50-53 26303527-2 2015 Acetylation is controlled by complexes containing opposing lysine and histone acetyltransferase (KAT and HAT) and deacetylase (KDAC and HDAC) activities. Lysine 59-65 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 97-100 25123533-2 2014 Although many lysine acetyltransferases (KATs) have been characterized as being capable of acetylating multiple lysine residues on histones, how different factors such as enzyme complexes or external stimuli (e.g. KAT activators or inhibitors) alter KAT specificity remains elusive. Lysine 14-20 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 214-217 20188666-3 2010 Here we show that Gcn5, a KAT that functions in transcription, works in parallel with Rtt109, the H3 lysine 56 KAT, to promote RC nucleosome assembly. Lysine 101-107 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 26-29 25478886-4 2014 It is now widely referred to as lysine acetylation orchestrated by lysine acetyl transferase (KAT) and lysine deacetylase (KDAC) and influences many cellular functions. Lysine 32-38 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 94-97 22600735-2 2012 Although large amounts of lysine acetylation sites have been identified via large-scale mass spectrometry or traditional experimental methods, the lysine (K)-acetyl-transferase (KAT) responsible for the acetylation of a given protein or lysine site remains largely unknown due to the experimental limitations of KAT substrate identification. Lysine 26-32 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 178-181 22600735-2 2012 Although large amounts of lysine acetylation sites have been identified via large-scale mass spectrometry or traditional experimental methods, the lysine (K)-acetyl-transferase (KAT) responsible for the acetylation of a given protein or lysine site remains largely unknown due to the experimental limitations of KAT substrate identification. Lysine 26-32 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 312-315 22600735-2 2012 Although large amounts of lysine acetylation sites have been identified via large-scale mass spectrometry or traditional experimental methods, the lysine (K)-acetyl-transferase (KAT) responsible for the acetylation of a given protein or lysine site remains largely unknown due to the experimental limitations of KAT substrate identification. Lysine 147-153 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 178-181 22600735-2 2012 Although large amounts of lysine acetylation sites have been identified via large-scale mass spectrometry or traditional experimental methods, the lysine (K)-acetyl-transferase (KAT) responsible for the acetylation of a given protein or lysine site remains largely unknown due to the experimental limitations of KAT substrate identification. Lysine 147-153 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 312-315 22600735-4 2012 In our previous study, we developed the acetylation set enrichment based (ASEB) computer program to predict which KAT-families are responsible for the acetylation of a given protein or lysine site. Lysine 185-191 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 114-117 21964354-3 2012 Although over 20 lysine (K)-acetyl-transferases (KATs) have been characterized, which KAT is responsible for a given protein or lysine site acetylation is mostly unknown. Lysine 17-23 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 49-52 21964354-4 2012 In this work, we collected KAT-specific acetylation sites manually and analyzed sequence features surrounding the acetylated lysine of substrates from three main KAT families (CBP/p300, GCN5/PCAF, and the MYST family). Lysine 125-131 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 162-165 21964354-5 2012 We found that each of the three KAT families acetylates lysines with different sequence features. Lysine 56-63 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 32-35 21964354-6 2012 Based on these differences, we developed a computer program, Acetylation Set Enrichment Based method to predict which KAT-families are responsible for acetylation of a given protein or lysine site. Lysine 185-191 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 118-121 20188666-3 2010 Here we show that Gcn5, a KAT that functions in transcription, works in parallel with Rtt109, the H3 lysine 56 KAT, to promote RC nucleosome assembly. Lysine 101-107 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 111-114 34769235-2 2021 Several reports of lysine acetyltransferase (KAT) activity by NAA10 exist, but others have not been able to find any NAA10-derived KAT activity, the latter of which is supported by structural studies. Lysine 19-25 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 45-48 33467728-4 2021 Overall, this work highlights that KAT8 has a broader substrate scope beyond natural lysine, and contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase (KAT) family. Lysine 85-91 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 35-38 33467728-4 2021 Overall, this work highlights that KAT8 has a broader substrate scope beyond natural lysine, and contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase (KAT) family. Lysine 194-200 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 35-38 33938178-2 2021 Bound to the APP adaptor protein Fe65 and the lysine acetyltransferase (KAT) Tip60, AICD translocates to the nucleus. Lysine 46-52 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 72-75 33931138-6 2021 Here, we describe the predominant epigenetic changes that can affect key KAT superfamily members during carcinogenesis and briefly highlight the pharmacological potential of employing lysine acetyltransferase inhibitors (KATi) for cancer therapy. Lysine 184-190 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 73-76 32747680-1 2020 Histone lysine acetyltransferase (KAT)-catalyzed acetylation of lysine residues in histone tails plays a key role in regulating gene expression in eukaryotes. Lysine 8-14 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 34-37 32747680-1 2020 Histone lysine acetyltransferase (KAT)-catalyzed acetylation of lysine residues in histone tails plays a key role in regulating gene expression in eukaryotes. Lysine 64-70 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 34-37 32747680-4 2020 Our results demonstrate that human KAT enzymes have an ability to catalyze an efficient acetylation of longer lysine analogs, whereas shorter lysine analogs are not substrates for KATs. Lysine 110-116 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 35-38 32747680-4 2020 Our results demonstrate that human KAT enzymes have an ability to catalyze an efficient acetylation of longer lysine analogs, whereas shorter lysine analogs are not substrates for KATs. Lysine 142-148 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 35-38 32747680-5 2020 Kinetics analyses showed that lysine is a superior KAT substrate to its analogs with altered chain length, implying that lysine has an optimal chain length for KAT-catalyzed acetylation reaction. Lysine 30-36 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 51-54 32747680-5 2020 Kinetics analyses showed that lysine is a superior KAT substrate to its analogs with altered chain length, implying that lysine has an optimal chain length for KAT-catalyzed acetylation reaction. Lysine 30-36 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 160-163 32747680-5 2020 Kinetics analyses showed that lysine is a superior KAT substrate to its analogs with altered chain length, implying that lysine has an optimal chain length for KAT-catalyzed acetylation reaction. Lysine 121-127 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 51-54 32747680-5 2020 Kinetics analyses showed that lysine is a superior KAT substrate to its analogs with altered chain length, implying that lysine has an optimal chain length for KAT-catalyzed acetylation reaction. Lysine 121-127 thiosulfate sulfurtransferase like domain containing 1 Homo sapiens 160-163