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Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed:30449621, PubMed:35679869). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed:30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed:25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25411247, PubMed:25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed:30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed:14592445, PubMed:18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed:31722219). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = an N(4)-acetylcytidine in 18S rRNA + ADP + phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:51424"},{"database":"Rhea","id":"RHEA-COMP:13575"},{"database":"Rhea","id":"RHEA-COMP:13576"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:74900"},{"database":"ChEBI","id":"CHEBI:82748"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_03211"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25411247"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a cytidine in tRNA + acetyl-CoA + ATP + H2O = an N(4)-acetylcytidine in tRNA + ADP + phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53876"},{"database":"Rhea","id":"RHEA-COMP:13670"},{"database":"Rhea","id":"RHEA-COMP:13671"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:74900"},{"database":"ChEBI","id":"CHEBI:82748"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_03211"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a cytidine in mRNA + acetyl-CoA + ATP + H2O = an N(4)-acetylcytidine in mRNA + ADP + phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58480"},{"database":"Rhea","id":"RHEA-COMP:15145"},{"database":"Rhea","id":"RHEA-COMP:15146"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:74900"},{"database":"ChEBI","id":"CHEBI:82748"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30449621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35679869"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:58481"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30449621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35679869"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24786082"}],"value":"Specifically inhibited by remodelin (4-[2-(2-cyclopentylidenehydrazinyl)-4-thiazolyl]-benzonitrile, monohydrobromide), a hydrobromide salt molecule (PubMed:24786082). Remodelin can improve nuclear architecture, chromatin organization and fitness of cells from patients suffering from Hutchinson-Gilford progeria syndrome (HGPS); molecular mechanisms explaining the relation between NAT10 activity and nuclear architecture are however unclear (PubMed:24786082)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_03211"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17631499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18082603"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25653167"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34516797"}],"value":"Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). Interacts with THUMPD1 (PubMed:25653167). Interacts with SUN1 (via N-terminus) (PubMed:17631499). Interacts with TERT (PubMed:18082603)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9H0A0","intActId":"EBI-876527"},"interactantTwo":{"uniProtKBAccession":"P15880","geneName":"RPS2","intActId":"EBI-443446"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9H0A0","intActId":"EBI-876527"},"interactantTwo":{"uniProtKBAccession":"Q9NXG2","geneName":"THUMPD1","intActId":"EBI-5462248"},"numberOfExperiments":6,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19303003"}],"value":"Nucleolar in interphase and redistributes to the perichromosomal layer and to the midbody during telophase"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_03211"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12429849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14592445"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19303003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24786082"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25653167"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30165671"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34516797"}],"value":"Nucleus, nucleolus","id":"SL-0188"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_03211"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19303003"}],"value":"Midbody","id":"SL-0469"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q9H0A0-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q9H0A0-2"],"sequenceIds":["VSP_054018"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17180247"}],"value":"Transcriptionally activated by genotoxic agents; possible role in DNA damage and induction of cellular resistance to genotoxic agents"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27993683"}],"value":"Acetylation at Lys-426 is required to activation of rRNA transcription (PubMed:27993683). May be autoacetylated; however ability to autoacetylate in vivo requires additional evidence (PubMed:27993683)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_03211"}],"value":"Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14592445"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17631499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19303003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26882543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27993683"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30165671"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30449621"}],"value":"A number of papers have reported some protein lysine acetyltransferase activity in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). However, most experiments have been performed in vitro using a protein construct lacking the RNA-binding region at the terminus (PubMed:14592445, PubMed:17631499, PubMed:19303003). Recent evidence suggests that NAT10 mainly acts as a RNA cytidine acetyltransferase in vivo (PubMed:30449621)"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAO49126.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAB21800.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1025,"modifier":"EXACT"}},"description":"RNA cytidine 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