{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q92993","secondaryAccessions":["B4E3C7","C9JL99","O95624","Q13430","Q17RW5","Q561W3","Q6GSE8","Q9BWK7"],"uniProtkbId":"KAT5_HUMAN","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-05-16","entryVersion":242,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Histone acetyltransferase KAT5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10096020"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12468530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26438602"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27153538"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29765047"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32822602"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33076429"}],"value":"2.3.1.48"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11416127"}],"value":"60 kDa Tat-interactive protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10096020"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11416127"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12801643"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29040603"}],"value":"Tip60"}]},{"fullName":{"value":"Histone acetyltransferase HTATIP"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8607265"}],"value":"HIV-1 Tat interactive protein"}]},{"fullName":{"value":"Lysine acetyltransferase 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein 2-hydroxyisobutyryltransferase KAT5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29192674"}],"value":"2.3.1.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein acetyltransferase KAT5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25865756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26829474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29040603"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409912"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30704899"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32034146"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817552"}],"value":"2.3.1.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein crotonyltransferase KAT5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34608293"}],"value":"2.3.1.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein lactyltransferase KAT5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38961290"}],"value":"2.3.1.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11416127"}],"value":"cPLA(2)-interacting protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32817552"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:5275"}],"value":"KAT5"},"synonyms":[{"value":"HTATIP"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11416127"}],"value":"TIP60"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8CHK4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12776177"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14966270"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15042092"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15121871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15310756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16141325"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387653"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17189187"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17360565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17709392"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17996965"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19783983"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19909775"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24463511"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24835996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25865756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26291311"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26438602"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26829474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27153538"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29040603"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29174981"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29192674"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29335245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29765047"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409912"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30704899"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31857589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32034146"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817552"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32822602"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32832608"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33076429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33938178"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34077757"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34608293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38961290"}],"value":"Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4 (PubMed:12776177, PubMed:14966270, PubMed:15042092, PubMed:15121871, PubMed:15310756, PubMed:16387653, PubMed:19909775, PubMed:25865756, PubMed:27153538, PubMed:29174981, PubMed:29335245, PubMed:32822602, PubMed:33076429). Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histones with other proteins which positively regulate transcription (PubMed:12776177, PubMed:14966270, PubMed:15042092, PubMed:15121871, PubMed:15310756). The NuA4 histone acetyltransferase complex is required for the activation of transcriptional programs associated with proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (PubMed:17709392, PubMed:19783983, PubMed:32832608). The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR): the complex inhibits TP53BP1 binding to chromatin via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys-20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of histone H2A (H2AK15ac), thereby blocking the ubiquitination mark required for TP53BP1 localization at DNA breaks (PubMed:27153538, PubMed:32832608). Also involved in DSB repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac), promoting NBN/NBS1 assembly at the sites of DNA damage (PubMed:17709392, PubMed:26438602). The NuA4 complex plays a key role in hematopoietic stem cell maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC target genes (By similarity). The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone hyperacetylation is required for histone replacement during the transition from round to elongating spermatids (By similarity). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (PubMed:24463511). Also acetylates non-histone proteins, such as BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, TP53/p53, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, SQSTM1, ULK1 and RUBCNL/Pacer (PubMed:16141325, PubMed:17189187, PubMed:17360565, PubMed:17996965, PubMed:24835996, PubMed:26829474, PubMed:29040603, PubMed:30409912, PubMed:30704899, PubMed:31857589, PubMed:32034146, PubMed:32817552, PubMed:34077757). Directly acetylates and activates ATM (PubMed:16141325). Promotes nucleotide excision repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting formation of the ERCC4-ERCC1 complex (PubMed:32034146). Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2 (PubMed:17996965). Acts as a regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation, thereby promoting FOXP3 transcriptional repressor activity (PubMed:17360565, PubMed:24835996). Involved in skeletal myoblast differentiation by mediating acetylation of SOX4 (PubMed:26291311). Catalyzes acetylation of APBB1/FE65, increasing its transcription activator activity (PubMed:33938178). Promotes transcription elongation during the activation phase of the circadian cycle by catalyzing acetylation of BMAL1, promoting elongation of circadian transcripts (By similarity). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Acts as a regulator of the cGAS-STING innate antiviral response by catalyzing acetylation the N-terminus of CGAS, thereby promoting CGAS DNA-binding and activation (PubMed:32817552). Also regulates lipid metabolism by mediating acetylation of CHKA or LPIN1 (PubMed:34077757). Promotes lipolysis of lipid droplets following glucose deprivation by mediating acetylation of isoform 1 of CHKA, thereby promoting monomerization of CHKA and its conversion into a tyrosine-protein kinase (PubMed:34077757). Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of LPIN1, thereby promoting the synthesis of diacylglycerol (PubMed:29765047). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), S-lactoyl-CoA (lactyl-CoA) and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to mediate protein crotonylation, lactylation and 2-hydroxyisobutyrylation, respectively (PubMed:29192674, PubMed:34608293, PubMed:38961290). Acts as a key regulator of chromosome segregation and kinetochore-microtubule attachment during mitosis by mediating acetylation or crotonylation of target proteins (PubMed:26829474, PubMed:29040603, PubMed:30409912, PubMed:34608293). Catalyzes acetylation of AURKB at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis (PubMed:26829474). Acetylates RAN during mitosis, promoting microtubule assembly at mitotic chromosomes (PubMed:29040603). Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore-microtubule attachment (PubMed:30409912). Catalyzes crotonylation of MAPRE1/EB1, thereby ensuring accurate spindle positioning in mitosis (PubMed:34608293). Catalyzes lactylation of NBN/NBS1 in response to DNA damage, thereby promoting DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed:38961290)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37478852"}],"value":"(Microbial infection) Catalyzes the acetylation of flavivirus NS3 protein to modulate their RNA-binding and -unwinding activities leading to facilitate viral replication"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10096020"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12468530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25865756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26438602"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27153538"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29174981"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32822602"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33076429"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21993"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25865756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26438602"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27153538"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29174981"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33076429"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32822602"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17189187"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24835996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25865756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26291311"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26829474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29040603"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29765047"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409912"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30704899"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31857589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32034146"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817552"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33938178"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34077757"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45949"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17189187"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24835996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26291311"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26829474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29765047"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409912"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31857589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32034146"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32817552"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33938178"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34077757"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53908"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:13707"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:137954"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34608293"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53909"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34608293"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24180"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15921"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:131780"},{"database":"ChEBI","id":"CHEBI:144968"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29192674"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24181"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29192674"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-lactoyl-CoA + L-lysyl-[protein] = N(6)-[(S)-lactoyl]-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:61996"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:19466"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:231527"},{"database":"ChEBI","id":"CHEBI:231528"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38961290"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:61997"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38961290"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20100829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25865756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30704899"}],"value":"Acyltransferase and acetyltransferase activities are activated by phosphorylation and autoacetylation (PubMed:20100829, PubMed:30704899). Autoacetylation activates the histone acetyltransferase activity (PubMed:20100829, PubMed:25865756, PubMed:30704899)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8CHK4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10966108"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11262386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11416127"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12551922"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12776177"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12963728"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14966270"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15502158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16001085"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16141325"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16835243"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17360565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17996965"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18397884"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18451177"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19308289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19909775"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21858214"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24463511"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24835996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25245946"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26945015"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29174981"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32832608"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33938178"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.73"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15196461"}],"value":"Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6 (PubMed:10966108, PubMed:12963728, PubMed:14966270, PubMed:15196461, PubMed:29174981). KAT5/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. The NuA4 complex interacts with MYC (PubMed:12776177). Interacts with ATM (PubMed:16141325). Interacts with JADE1 (PubMed:15502158). Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7 (PubMed:11262386, PubMed:11416127, PubMed:12551922). Interacts with the cytoplasmic tail of APP and APBB1/FE65 (PubMed:33938178). Interacts with TRIM24 and TRIM68 (PubMed:18451177, PubMed:19909775). Forms a complex with SENP6 and UBE2I in response to UV irradiation. Identified in a complex with HINT1 (PubMed:16835243). Interacts with ATF2 and CUL3 (PubMed:18397884). Interacts with NR1D2 (via N-terminus) (PubMed:17996965). Component of a SWR1-like complex (PubMed:24463511). Interacts with FOXP3 (PubMed:17360565, PubMed:24835996). Interacts with ZBTB49 (PubMed:25245946). Interacts with SRF (By similarity). Interacts with ATF3; promoting autoacetylation and deubiquitination by USP7 (PubMed:25865756). Interacts with EP300/p300; interaction promotes KAT5 autoacetylation (PubMed:24835996). Interacts with PRKDC; interaction is impaired following KAT5 sumoylation (PubMed:32832608). Interacts with GPR50 (PubMed:21858214). Interacts with NME3; this interaction enables recruitment of NME3 at DNA damage sites where it plays a role in the repair of DNA (PubMed:26945015). Interacts with PDCD5; the interaction is direct and leads to stabilization of the KAT5 protein (PubMed:19308289)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16001085"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8607265"}],"value":"(Microbial infection) Interacts with HIV-1 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Transiently localizes to kinetochores in early mitosis (PubMed:26829474). Localizes to spindle poles when chromosomes align during metaphase (PubMed:34608293). Localizes in the cytoplasm and nucleus of round spermatids (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11262386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11416127"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12551922"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17360565"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17704809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17996965"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19308289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33938178"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25560918"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27153538"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29335245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33076429"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26829474"}],"value":"Chromosome, centromere, kinetochore","id":"SL-0149"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34608293"}],"value":"Cytoplasm, cytoskeleton, spindle pole","id":"SL-0448"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387653"}],"value":"Nucleus, nucleolus","id":"SL-0188"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11262386"}],"value":"Cytoplasm, perinuclear region","id":"SL-0198"}}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37478852"}],"value":"(Microbial infection) Relocalizes from the nucleus to zika virus replication complexes in the cytoplasm"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37478852"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"2"},"isoformIds":["Q92993-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11416127"}],"value":"PLIP"}],"isoformIds":["Q92993-2"],"sequenceIds":["VSP_007438"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q92993-3"],"sequenceIds":["VSP_009104"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"isoformIds":["Q92993-4"],"sequenceIds":["VSP_009104","VSP_007438"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12468530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26829474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29335245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30704899"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33076429"}],"value":"Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase (PubMed:12468530, PubMed:26829474, PubMed:29335245). The phosphorylated form has a higher activity (PubMed:12468530, PubMed:29335245). Phosphorylation at Ser-90 by CDK1 or CDK9 is a prerequisite for phosphorylation at Ser-86 by GSK3 (PubMed:26829474, PubMed:30704899). Phosphorylation at Ser-86 by GSK3 (GSK3A or GSK3B) activates acetyltransferase and acyltransferase activities (PubMed:30704899). Phosphorylation at Ser-90 by CDK9 promotes KAT5 recruitment to chromatin (PubMed:29335245). Phosphorylation by VRK1 following DNA damage promotes KAT5 association with chromatin and histone acetyltransferase activity (PubMed:33076429)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20100829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24835996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25865756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26291311"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33938178"}],"value":"Autoacetylated (PubMed:20100829, PubMed:24835996, PubMed:25301942, PubMed:26291311, PubMed:33938178). Autoacetylation is required for histone acetyltransferase activity (PubMed:20100829, PubMed:25865756). Autoacetylation at Lys-327 is facilitated by interaction with EP300/p300: it prevents ubiquitination and subsequent degradation by the proteasome and promotes acetylation of target proteins (PubMed:24835996). Deacetylated by HDAC3 and SIRT1 (PubMed:20100829, PubMed:25301942). Deacetylation by HDAC3 promotes its ubiquitination and cytoplasmic localization (PubMed:25301942)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17704809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32832608"}],"value":"Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies (PubMed:17704809). Sumoylation with SUMO2 by PIAS4 at Lys-430 promotes repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed:32832608). Sumoylation by PIAS4 impairs interaction with PRKDC, inhibiting non-homologous end joining (NHEJ)-mediated repair of DSBs, thereby facilitating HR (PubMed:32832608). Desumoylated by SENP3 (PubMed:32832608)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11927554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24835996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25865756"}],"value":"Ubiquitinated by MDM2, leading to its proteasome-dependent degradation (PubMed:11927554, PubMed:24835996). Ubiquitination is prevented by autoacetylation at Lys-327 (PubMed:24835996). Ubiquitinated following deacetylation by HDAC3, leading to cytoplasmic localization (PubMed:25301942). Deubiquitinated by USP7 following interaction with ATF3, promoting its stabilization (PubMed:25865756)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16001085"}],"value":"(Microbial infection) In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Neurodevelopmental disorder with dysmorphic facies, sleep disturbance, and brain abnormalities","diseaseAccession":"DI-05983","acronym":"NEDFASB","description":"A neurodevelopmental disorder characterized by severe global developmental delay, intellectual disability, poor or absent language, behavioral abnormalities, severe sleep disturbance, seizures, cerebral malformations, and craniofacial dysmorphism. Progressive cerebellar atrophy is also observed. Additional features may include genitourinary tract anomalies, hearing loss, and mild distal skeletal defects.","diseaseCrossReference":{"database":"MIM","id":"619103"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32822602"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the MYST (SAS/MOZ) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19783983"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25560918"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29494751"},{"evidenceCode":"ECO:0000305"}],"value":"The role of the Tudor-knot domain, also named chromo barrel or chromodomain, is unclear. Based on its similarity with some chromo domains, it was first reported to bind histone H3 trimethylated on 'Lys-4' and/or 'Lys-9' (H3K4me3 and/or H3K9me3, respectively) (PubMed:19783983, PubMed:25560918). However, another group was not able to see any binding to methylated histones (PubMed:29494751). The 3D structure of the domain suggests that the inability to bind histones is caused by occlusion of the putative peptide-binding site by a basic amino acid side chain within a unique beta hairpin (PubMed:29494751)"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAB02683.1","note":"Truncated N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/40893/HTATIP","ftp":false}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Histone acetyltransferase KAT5","featureId":"PRO_0000051580"},{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"Tudor-knot","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Domain","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":504,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01063"}]},{"type":"Zinc finger","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"C2HC MYST-type","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01063"},{"evidenceCode":"ECO:0000305","source":"Reference","id":"Ref.73"}]},{"type":"Region","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":368,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Interaction with ATF2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18397884"}]},{"type":"Compositional bias","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9H7Z6"}]},{"type":"Binding site","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.73"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.73"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.73"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":416,"modifier":"EXACT"},"end":{"value":416,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9H7Z6"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Modified residue","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19608861"}]},{"type":"Modified residue","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"Phosphoserine; by GSK3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12468530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22539723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29335245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30704899"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"Phosphoserine; by CDK1 and CDK9","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12468530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22539723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26829474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29335245"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29174981"}]},{"type":"Modified residue","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}]},{"type":"Modified residue","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}]},{"type":"Modified residue","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}]},{"type":"Modified residue","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}]},{"type":"Modified residue","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}]},{"type":"Modified residue","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24835996"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.73"}]},{"type":"Cross-link","location":{"start":{"value":430,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17704809"}]},{"type":"Cross-link","location":{"start":{"value":430,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32832608"}]},{"type":"Cross-link","location":{"start":{"value":451,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17704809"}]},{"type":"Alternative sequence","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":4,"modifier":"EXACT"}},"description":"in isoform 3 and isoform 4","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12801643"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14702039"}],"featureId":"VSP_009104","alternativeSequence":{"originalSequence":"V","alternativeSequences":["VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ"]}},{"type":"Alternative sequence","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"in isoform 1 and isoform 4","evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11416127"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14702039"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15489334"}],"featureId":"VSP_007438","alternativeSequence":{}},{"type":"Natural variant","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"in NEDFASB; decreased histone acetyltransferase activity; dbSNP:rs1857071943","featureCrossReferences":[{"database":"dbSNP","id":"rs1857071943"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32822602"}],"featureId":"VAR_085192","alternativeSequence":{"originalSequence":"R","alternativeSequences":["H"]}},{"type":"Natural variant","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"in dbSNP:rs11541271","featureCrossReferences":[{"database":"dbSNP","id":"rs11541271"}],"featureId":"VAR_059456","alternativeSequence":{"originalSequence":"P","alternativeSequences":["T"]}},{"type":"Natural variant","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"in NEDFASB; decreased histone acetyltransferase activity; dbSNP:rs1857215256","featureCrossReferences":[{"database":"dbSNP","id":"rs1857215256"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32822602"}],"featureId":"VAR_085193","alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Natural variant","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"in NEDFASB; 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Abolishes phosphorylation; when associated with A-90. Reduced histone acetyltransferase activity. Abolished phosphorylation by GSK3 and decreased acetyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12468530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22539723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30704899"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"Reduced phosphorylation, leading to reduced protein acetyltransferase activity. Abolishes phosphorylation; when associated with A-86. Reduced histone acetyltransferase activity. 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In K6R; abolished autoacetylation; when associated with R-120, R-148, R-150, R-187 and R-189.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29174981"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"In K6R; abolished autoacetylation; when associated with R-104, R-148, R-150, R-187 and R-189.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"In K6R; abolished autoacetylation; when associated with R-104, R-120, R-150, R-187 and R-189.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"In K6R; abolished autoacetylation; when associated with R-104, R-120, R-148, R-187 and R-189.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"In K6R; abolished autoacetylation; when associated with R-104, R-120, R-148, R-150 and R-189.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"In K6R; abolished autoacetylation; when associated with R-104, R-120, R-148, R-150 and R-187.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25301942"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Does not affect phosphorylation; when associated with A-257.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12468530"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"Does not affect phosphorylation; when associated with A-254.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12468530"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"Mimics acetylation; promoting interaction with FOXP3 and subsequent acetylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24835996"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"Decreased autoacetylation; leading to decreased acetyltransferase activity and ability to acetylate FOXP3.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24835996"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"In KAT5(QG/EE) mutant; abolished acetyltransferase activity. 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