ID KAT5_HUMAN Reviewed; 513 AA. AC Q92993; B4E3C7; C9JL99; O95624; Q13430; Q17RW5; Q561W3; Q6GSE8; Q9BWK7; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2003, sequence version 2. DT 27-MAR-2024, entry version 232. DE RecName: Full=Histone acetyltransferase KAT5 {ECO:0000305}; DE EC=2.3.1.48 {ECO:0000269|PubMed:10096020, ECO:0000269|PubMed:12468530, ECO:0000269|PubMed:26438602, ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:29765047, ECO:0000269|PubMed:32822602, ECO:0000269|PubMed:33076429}; DE AltName: Full=60 kDa Tat-interactive protein {ECO:0000303|PubMed:11416127}; DE Short=Tip60 {ECO:0000303|PubMed:10096020, ECO:0000303|PubMed:11416127, ECO:0000303|PubMed:12801643, ECO:0000303|PubMed:29040603}; DE AltName: Full=Histone acetyltransferase HTATIP; DE Short=HIV-1 Tat interactive protein {ECO:0000303|PubMed:8607265}; DE AltName: Full=Lysine acetyltransferase 5; DE AltName: Full=Protein 2-hydroxyisobutyryltransferase KAT5 {ECO:0000305}; DE EC=2.3.1.- {ECO:0000269|PubMed:29192674}; DE AltName: Full=Protein acetyltransferase KAT5 {ECO:0000305}; DE EC=2.3.1.- {ECO:0000269|PubMed:25865756, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:30409912, ECO:0000269|PubMed:30704899, ECO:0000269|PubMed:32034146, ECO:0000269|PubMed:32817552}; DE AltName: Full=Protein crotonyltransferase KAT5 {ECO:0000305}; DE EC=2.3.1.- {ECO:0000269|PubMed:34608293}; DE AltName: Full=cPLA(2)-interacting protein {ECO:0000303|PubMed:11416127}; GN Name=KAT5 {ECO:0000303|PubMed:32817552, ECO:0000312|HGNC:HGNC:5275}; GN Synonyms=HTATIP, TIP60 {ECO:0000303|PubMed:11416127}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH HIV-1 TAT RP (MICROBIAL INFECTION). RC TISSUE=Lymphoblast; RX PubMed=8607265; DOI=10.1006/viro.1996.0071; RA Kamine J., Elangovan B., Subramanian T., Coleman D., Chinnadurai G.; RT "Identification of a cellular protein that specifically interacts with the RT essential cysteine region of the HIV-1 Tat transactivator."; RL Virology 216:357-366(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PLA2G4A, AND RP SUBCELLULAR LOCATION. RC TISSUE=Fibroblast, and Placenta; RX PubMed=11416127; DOI=10.1128/mcb.21.14.4470-4481.2001; RA Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G., Taheri M.R., RA Bonventre J.V.; RT "PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic RT phospholipase A(2), induces apoptosis, and potentiates prostaglandin RT production."; RL Mol. Cell. Biol. 21:4470-4481(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=12801643; DOI=10.1016/s0378-1119(03)00547-x; RA Legube G., Trouche D.; RT "Identification of a larger form of the histone acetyl transferase Tip60."; RL Gene 310:161-168(2003). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cervix, Liver, Placenta, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 19-35; 150-177 AND 297-307, IDENTIFICATION IN NUA4 RP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12963728; DOI=10.1074/jbc.c300389200; RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., RA Conaway R.C., Conaway J.W.; RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60- RT containing histone acetyltransferase complex."; RL J. Biol. Chem. 278:42733-42736(2003). RN [10] RP CATALYTIC ACTIVITY IN VITRO. RX PubMed=10096020; DOI=10.1046/j.1365-2443.1998.00229.x; RA Kimura A., Horikoshi M.; RT "Tip60 acetylates six lysines of a specific class in core histones in RT vitro."; RL Genes Cells 3:789-800(1998). RN [11] RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=10966108; DOI=10.1016/s0092-8674(00)00051-9; RA Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., RA Scully R., Qin J., Nakatani Y.; RT "Involvement of the TIP60 histone acetylase complex in DNA repair and RT apoptosis."; RL Cell 102:463-473(2000). RN [12] RP INTERACTION WITH EDNRA, AND SUBCELLULAR LOCATION. RX PubMed=11262386; DOI=10.1074/jbc.c000909200; RA Lee H.-J., Chun M., Kandror K.V.; RT "Tip60 and HDAC7 interact with the endothelin receptor a and may be RT involved in downstream signaling."; RL J. Biol. Chem. 276:16597-16600(2001). RN [13] RP UBIQUITINATION. RX PubMed=11927554; DOI=10.1093/emboj/21.7.1704; RA Legube G., Linares L.K., Lemercier C., Scheffner M., Khochbin S., RA Trouche D.; RT "Tip60 is targeted to proteasome-mediated degradation by Mdm2 and RT accumulates after UV irradiation."; RL EMBO J. 21:1704-1712(2002). RN [14] RP ROLE IN MYC-DEPENDENT TRANSCRIPTION, AND INTERACTION WITH MYC. RX PubMed=12776177; DOI=10.1038/sj.embor.embor861; RA Frank S.R., Parisi T., Taubert S., Fernandez P., Fuchs M., Chan H.M., RA Livingston D.M., Amati B.; RT "MYC recruits the TIP60 histone acetyltransferase complex to chromatin."; RL EMBO Rep. 4:575-580(2003). RN [15] RP PHOSPHORYLATION AT SER-86 AND SER-90, MUTAGENESIS OF SER-86; SER-90; RP LEU-254; LEU-257 AND GLY-380, AND CATALYTIC ACTIVITY. RX PubMed=12468530; DOI=10.1074/jbc.m211811200; RA Lemercier C., Legube G., Caron C., Louwagie M., Garin J., Trouche D., RA Khochbin S.; RT "Tip60 acetyltransferase activity is controlled by phosphorylation."; RL J. Biol. Chem. 278:4713-4718(2003). RN [16] RP SUBCELLULAR LOCATION, AND INTERACTION WITH HDAC7. RX PubMed=12551922; DOI=10.1074/jbc.m210816200; RA Xiao H., Chung J., Kao H.-Y., Yang Y.-C.; RT "Tip60 is a co-repressor for STAT3."; RL J. Biol. Chem. 278:11197-11204(2003). RN [17] RP REVIEW ON NUA4 COMPLEX. RX PubMed=15196461; DOI=10.1016/j.gde.2004.02.009; RA Doyon Y., Cote J.; RT "The highly conserved and multifunctional NuA4 HAT complex."; RL Curr. Opin. Genet. Dev. 14:147-154(2004). RN [18] RP ROLE IN TP53-DEPENDENT TRANSCRIPTION. RX PubMed=15310756; DOI=10.1074/jbc.m407478200; RA Legube G., Linares L.K., Tyteca S., Caron C., Scheffner M., RA Chevillard-Briet M., Trouche D.; RT "Role of the histone acetyl transferase Tip60 in the p53 pathway."; RL J. Biol. Chem. 279:44825-44833(2004). RN [19] RP INTERACTION WITH JADE1. RX PubMed=15502158; DOI=10.1074/jbc.m410487200; RA Panchenko M.V., Zhou M.I., Cohen H.T.; RT "von Hippel-Lindau partner Jade-1 is a transcriptional co-activator RT associated with histone acetyltransferase activity."; RL J. Biol. Chem. 279:56032-56041(2004). RN [20] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RP NUA4 COMPLEX. RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004; RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.; RT "Structural and functional conservation of the NuA4 histone RT acetyltransferase complex from yeast to humans."; RL Mol. Cell. Biol. 24:1884-1896(2004). RN [21] RP ROLE IN E2F1-DEPENDENT TRANSCRIPTION. RX PubMed=15121871; DOI=10.1128/mcb.24.10.4546-4556.2004; RA Taubert S., Gorrini C., Frank S.R., Parisi T., Fuchs M., Chan H.M., RA Livingston D.M., Amati B.; RT "E2F-dependent histone acetylation and recruitment of the Tip60 RT acetyltransferase complex to chromatin in late G1."; RL Mol. Cell. Biol. 24:4546-4556(2004). RN [22] RP ROLE IN TP53-DEPENDENT TRANSCRIPTION. RX PubMed=15042092; DOI=10.1038/nature02371; RA Berns K., Hijmans E.M., Mullenders J., Brummelkamp T.R., Velds A., RA Heimerikx M., Kerkhoven R.M., Madiredjo M., Nijkamp W., Weigelt B., RA Agami R., Ge W., Cavet G., Linsley P.S., Beijersbergen R.L., Bernards R.; RT "A large-scale RNAi screen in human cells identifies new components of the RT p53 pathway."; RL Nature 428:431-437(2004). RN [23] RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION), AND UBIQUITINATION RP (MICROBIAL INFECTION). RX PubMed=16001085; DOI=10.1038/sj.emboj.7600734; RA Col E., Caron C., Chable-Bessia C., Legube G., Gazzeri S., Komatsu Y., RA Yoshida M., Benkirane M., Trouche D., Khochbin S.; RT "HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic RT stresses."; RL EMBO J. 24:2634-2645(2005). RN [24] RP INTERACTION WITH ATM, AND FUNCTION. RX PubMed=16141325; DOI=10.1073/pnas.0504211102; RA Sun Y., Jiang X., Chen S., Fernandes N., Price B.D.; RT "A role for the Tip60 histone acetyltransferase in the acetylation and RT activation of ATM."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13182-13187(2005). RN [25] RP IDENTIFICATION IN A COMPLEX WITH HINT1. RX PubMed=16835243; DOI=10.1074/jbc.m513452200; RA Weiske J., Huber O.; RT "The histidine triad protein Hint1 triggers apoptosis independent of its RT enzymatic activity."; RL J. Biol. Chem. 281:27356-27366(2006). RN [26] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007; RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., RA Lane W.S., Tan S., Yang X.-J., Cote J.; RT "ING tumor suppressor proteins are critical regulators of chromatin RT acetylation required for genome expression and perpetuation."; RL Mol. Cell 21:51-64(2006). RN [27] RP FUNCTION. RX PubMed=17709392; DOI=10.1128/mcb.00579-07; RA Ikura T., Tashiro S., Kakino A., Shima H., Jacob N., Amunugama R., RA Yoder K., Izumi S., Kuraoka I., Tanaka K., Kimura H., Ikura M., RA Nishikubo S., Ito T., Muto A., Miyagawa K., Takeda S., Fishel R., RA Igarashi K., Kamiya K.; RT "DNA damage-dependent acetylation and ubiquitination of H2AX enhances RT chromatin dynamics."; RL Mol. Cell. Biol. 27:7028-7040(2007). RN [28] RP FUNCTION, INTERACTION WITH FOXP3, AND SUBCELLULAR LOCATION. RX PubMed=17360565; DOI=10.1073/pnas.0700298104; RA Li B., Samanta A., Song X., Iacono K.T., Bembas K., Tao R., Basu S., RA Riley J.L., Hancock W.W., Shen Y., Saouaf S.J., Greene M.I.; RT "FOXP3 interactions with histone acetyltransferase and class II histone RT deacetylases are required for repression."; RL Proc. Natl. Acad. Sci. U.S.A. 104:4571-4576(2007). RN [29] RP FUNCTION, INTERACTION WITH NR1D2, AND SUBCELLULAR LOCATION. RX PubMed=17996965; DOI=10.1016/j.bbamcr.2007.09.004; RA Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.; RT "The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to RT regulate apolipoprotein CIII promoter."; RL Biochim. Biophys. Acta 1783:224-236(2008). RN [30] RP INTERACTION WITH TRIM68. RX PubMed=18451177; DOI=10.1158/0008-5472.can-07-6059; RA Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M., Shinohara N., RA Nonomura K., Hatakeyama S.; RT "TRIM68 regulates ligand-dependent transcription of androgen receptor in RT prostate cancer cells."; RL Cancer Res. 68:3486-3494(2008). RN [31] RP INTERACTION WITH ATF2 AND CUL3, AND PROTEASOMAL DEGRADATION. RX PubMed=18397884; DOI=10.1074/jbc.m802030200; RA Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.; RT "Regulation of TIP60 by ATF2 modulates ATM activation."; RL J. Biol. Chem. 283:17605-17614(2008). RN [32] RP SUMOYLATION AT LYS-430 AND LYS-451, MUTAGENESIS OF LYS-430 AND LYS-451, RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND RP IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX. RX PubMed=17704809; DOI=10.1038/sj.onc.1210710; RA Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z., RA Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M., Liang S., RA Wu Q., Reddy S.E., Hu R., Huang H., Jin C., Yao X.; RT "Functional characterization of TIP60 sumoylation in UV-irradiated DNA RT damage response."; RL Oncogene 27:931-941(2008). RN [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [34] RP FUNCTION, AND INTERACTION WITH TRIM24. RX PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001; RA Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., RA Imamura M., Hatakeyama S.; RT "TRIM24 mediates ligand-dependent activation of androgen receptor and is RT repressed by a bromodomain-containing protein, BRD7, in prostate cancer RT cells."; RL Biochim. Biophys. Acta 1793:1828-1836(2009). RN [35] RP FUNCTION. RX PubMed=19783983; DOI=10.1038/ncb1982; RA Sun Y., Jiang X., Xu Y., Ayrapetov M.K., Moreau L.A., Whetstine J.R., RA Price B.D.; RT "Histone H3 methylation links DNA damage detection to activation of the RT tumour suppressor Tip60."; RL Nat. Cell Biol. 11:1376-1382(2009). RN [36] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [37] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [38] RP ACETYLATION, AND ACTIVITY REGULATION. RX PubMed=20100829; DOI=10.1074/jbc.m109.087585; RA Wang J., Chen J.; RT "SIRT1 regulates autoacetylation and histone acetyltransferase activity of RT TIP60."; RL J. Biol. Chem. 285:11458-11464(2010). RN [39] RP INTERACTION WITH GPR50. RX PubMed=21858214; DOI=10.1371/journal.pone.0023725; RA Li J., Hand L.E., Meng Q.J., Loudon A.S., Bechtold D.A.; RT "GPR50 interacts with TIP60 to modulate glucocorticoid receptor RT signalling."; RL PLoS ONE 6:e23725-e23725(2011). RN [40] RP PHOSPHORYLATION AT SER-86 AND SER-90, AND MUTAGENESIS OF SER-86 AND SER-90. RX PubMed=22539723; DOI=10.1126/science.1217032; RA Lin S.Y., Li T.Y., Liu Q., Zhang C., Li X., Chen Y., Zhang S.M., Lian G., RA Liu Q., Ruan K., Wang Z., Zhang C.S., Chien K.Y., Wu J., Li Q., Han J., RA Lin S.C.; RT "GSK3-TIP60-ULK1 signaling pathway links growth factor deprivation to RT autophagy."; RL Science 336:477-481(2012). RN [41] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-90 AND SER-199, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [42] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EP300 AND FOXP3, RP UBIQUITINATION, ACETYLATION AT LYS-327, AND MUTAGENESIS OF LYS-327 AND RP 377-GLN--GLY-380. RX PubMed=24835996; DOI=10.1016/j.celrep.2014.04.021; RA Xiao Y., Nagai Y., Deng G., Ohtani T., Zhu Z., Zhou Z., Zhang H., Ji M.Q., RA Lough J.W., Samanta A., Hancock W.W., Greene M.I.; RT "Dynamic interactions between TIP60 and p300 regulate FOXP3 function RT through a structural switch defined by a single lysine on TIP60."; RL Cell Rep. 7:1471-1480(2014). RN [43] RP ACETYLATION AT LYS-104; LYS-120; LYS-148; LYS-150; LYS-187 AND LYS-189, RP UBIQUITINATION, AND MUTAGENESIS OF LYS-104; LYS-120; LYS-148; LYS-150; RP LYS-187 AND LYS-189. RX PubMed=25301942; DOI=10.1074/jbc.m114.575266; RA Yi J., Huang X., Yang Y., Zhu W.G., Gu W., Luo J.; RT "Regulation of histone acetyltransferase TIP60 function by histone RT deacetylase 3."; RL J. Biol. Chem. 289:33878-33886(2014). RN [44] RP INTERACTION WITH ZBTB49. RX PubMed=25245946; DOI=10.1093/nar/gku857; RA Jeon B.N., Kim M.K., Yoon J.H., Kim M.Y., An H., Noh H.J., Choi W.I., RA Koh D.I., Hur M.W.; RT "Two ZNF509 (ZBTB49) isoforms induce cell-cycle arrest by activating RT transcription of p21/CDKN1A and RB upon exposure to genotoxic stress."; RL Nucleic Acids Res. 42:11447-11461(2014). RN [45] RP FUNCTION, AND IDENTIFICATION IN THE SWR1-LIKE COMPLEX. RX PubMed=24463511; DOI=10.1038/nature12922; RA Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M., RA Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C., RA Hamiche A.; RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin."; RL Nature 505:648-653(2014). RN [46] RP SUBCELLULAR LOCATION. RX PubMed=25560918; DOI=10.1080/09168451.2014.993914; RA Kim C.H., Kim J.W., Jang S.M., An J.H., Seo S.B., Choi K.H.; RT "The chromodomain-containing histone acetyltransferase TIP60 acts as a code RT reader, recognizing the epigenetic codes for initiating transcription."; RL Biosci. Biotechnol. Biochem. 79:532-538(2015). RN [47] RP FUNCTION, CATALYTIC ACTIVITY, ACETYLATION, AND MUTAGENESIS OF RP 377-GLN--GLY-380. RX PubMed=26291311; DOI=10.1038/cddis.2015.190; RA Jang S.M., Kim J.W., Kim C.H., An J.H., Johnson A., Song P.I., Rhee S., RA Choi K.H.; RT "KAT5-mediated SOX4 acetylation orchestrates chromatin remodeling during RT myoblast differentiation."; RL Cell Death Dis. 6:e1857-e1857(2015). RN [48] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=26438602; DOI=10.1128/mcb.00757-15; RA Ikura M., Furuya K., Matsuda S., Matsuda R., Shima H., Adachi J., RA Matsuda T., Shiraki T., Ikura T.; RT "Acetylation of histone H2AX at Lys 5 by the TIP60 histone RT acetyltransferase complex is essential for the dynamic binding of NBS1 to RT damaged chromatin."; RL Mol. Cell. Biol. 35:4147-4157(2015). RN [49] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH ATF3, RP ACETYLATION, AND UBIQUITINATION. RX PubMed=25865756; DOI=10.1038/ncomms7752; RA Cui H., Guo M., Xu D., Ding Z.C., Zhou G., Ding H.F., Zhang J., Tang Y., RA Yan C.; RT "The stress-responsive gene ATF3 regulates the histone acetyltransferase RT Tip60."; RL Nat. Commun. 6:6752-6752(2015). RN [50] RP INTERACTION WITH NME3. RX PubMed=26945015; DOI=10.1042/bcj20160122; RA Tsao N., Yang Y.C., Deng Y.J., Chang Z.F.; RT "The direct interaction of NME3 with Tip60 in DNA repair."; RL Biochem. J. 473:1237-1245(2016). RN [51] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=27153538; DOI=10.1016/j.molcel.2016.03.031; RA Jacquet K., Fradet-Turcotte A., Avvakumov N., Lambert J.P., Roques C., RA Pandita R.K., Paquet E., Herst P., Gingras A.C., Pandita T.K., Legube G., RA Doyon Y., Durocher D., Cote J.; RT "The TIP60 complex regulates bivalent chromatin recognition by 53BP1 RT through direct H4K20me binding and H2AK15 acetylation."; RL Mol. Cell 62:409-421(2016). RN [52] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT RP SER-90, AND MUTAGENESIS OF SER-90. RX PubMed=26829474; DOI=10.1038/nchembio.2017; RA Mo F., Zhuang X., Liu X., Yao P.Y., Qin B., Su Z., Zang J., Wang Z., RA Zhang J., Dou Z., Tian C., Teng M., Niu L., Hill D.L., Fang G., Ding X., RA Fu C., Yao X.; RT "Acetylation of Aurora B by TIP60 ensures accurate chromosomal RT segregation."; RL Nat. Chem. Biol. 12:226-232(2016). RN [53] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29192674; DOI=10.1038/cr.2017.149; RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J., RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.; RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation RT pathway."; RL Cell Res. 28:111-125(2018). RN [54] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-86 AND SER-90, AND RP MUTAGENESIS OF SER-90. RX PubMed=29335245; DOI=10.15252/embr.201744311; RA Brauns-Schubert P., Schubert F., Wissler M., Weiss M., Schlicher L., RA Bessler S., Safavi M., Miething C., Borner C., Brummer T., Maurer U.; RT "CDK9-mediated phosphorylation controls the interaction of TIP60 with the RT transcriptional machinery."; RL EMBO Rep. 19:244-256(2018). RN [55] RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN NUA4 COMPLEX, ACETYLATION RP AT LYS-104, AND MUTAGENESIS OF LYS-104. RX PubMed=29174981; DOI=10.1016/j.yexcr.2017.11.028; RA Fang X., Lu G., Ha K., Lin H., Du Y., Zuo Q., Fu Y., Zou C., Zhang P.; RT "Acetylation of TIP60 at K104 is essential for metabolic stress-induced RT apoptosis in cells of hepatocellular cancer."; RL Exp. Cell Res. 362:279-286(2018). RN [56] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29040603; DOI=10.1093/jmcb/mjx045; RA Bao X., Liu H., Liu X., Ruan K., Zhang Y., Zhang Z., Hu Q., Liu Y., RA Akram S., Zhang J., Gong Q., Wang W., Yuan X., Li J., Zhao L., Dou Z., RA Tian R., Yao X., Wu J., Shi Y.; RT "Mitosis-specific acetylation tunes Ran effector binding for chromosome RT segregation."; RL J. Mol. Cell Biol. 10:18-32(2018). RN [57] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29765047; DOI=10.1038/s41467-018-04363-w; RA Li T.Y., Song L., Sun Y., Li J., Yi C., Lam S.M., Xu D., Zhou L., Li X., RA Yang Y., Zhang C.S., Xie C., Huang X., Shui G., Lin S.Y., Reue K., RA Lin S.C.; RT "Tip60-mediated lipin 1 acetylation and ER translocation determine RT triacylglycerol synthesis rate."; RL Nat. Commun. 9:1916-1916(2018). RN [58] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30409912; DOI=10.1074/jbc.ra118.003844; RA Zhao G., Cheng Y., Gui P., Cui M., Liu W., Wang W., Wang X., Ali M., RA Dou Z., Niu L., Liu H., Anderson L., Ruan K., Hong J., Yao X.; RT "Dynamic acetylation of the kinetochore-associated protein HEC1 ensures RT accurate microtubule-kinetochore attachment."; RL J. Biol. Chem. 294:576-592(2019). RN [59] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT RP SER-86, AND MUTAGENESIS OF SER-86. RX PubMed=30704899; DOI=10.1016/j.molcel.2018.12.017; RA Cheng X., Ma X., Zhu Q., Song D., Ding X., Li L., Jiang X., Wang X., RA Tian R., Su H., Shen Z., Chen S., Liu T., Gong W., Liu W., Sun Q.; RT "Pacer is a mediator of mTORC1 and GSK3-TIP60 signaling in regulation of RT autophagosome maturation and lipid metabolism."; RL Mol. Cell 73:1-15(2019). RN [60] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=31857589; DOI=10.1038/s41467-019-13718-w; RA You Z., Jiang W.X., Qin L.Y., Gong Z., Wan W., Li J., Wang Y., Zhang H., RA Peng C., Zhou T., Tang C., Liu W.; RT "Requirement for p62 acetylation in the aggregation of ubiquitylated RT proteins under nutrient stress."; RL Nat. Commun. 10:5792-5792(2019). RN [61] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=33076429; DOI=10.3390/cancers12102986; RA Garcia-Gonzalez R., Morejon-Garcia P., Campillo-Marcos I., Salzano M., RA Lazo P.A.; RT "VRK1 phosphorylates Tip60/KAT5 and is required for H4K16 acetylation in RT response to DNA Damage."; RL Cancers 12:0-0(2020). RN [62] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 377-GLN--GLY-380. RX PubMed=32034146; DOI=10.1038/s41467-020-14564-x; RA Wang J., He H., Chen B., Jiang G., Cao L., Jiang H., Zhang G., Chen J., RA Huang J., Yang B., Zhou C., Liu T.; RT "Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and RT activation."; RL Nat. Commun. 11:786-786(2020). RN [63] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 377-GLN--GLY-380. RX PubMed=32817552; DOI=10.1073/pnas.1922330117; RA Song Z.M., Lin H., Yi X.M., Guo W., Hu M.M., Shu H.B.; RT "KAT5 acetylates cGAS to promote innate immune response to DNA virus."; RL Proc. Natl. Acad. Sci. U.S.A. 117:21568-21575(2020). RN [64] RP FUNCTION, INTERACTION WITH PRKDC, SUMOYLATION AT LYS-430, AND MUTAGENESIS RP OF LYS-430. RX PubMed=32832608; DOI=10.1126/sciadv.aba7822; RA Gao S.S., Guan H., Yan S., Hu S., Song M., Guo Z.P., Xie D.F., Liu Y., RA Liu X., Zhang S., Zhou P.K.; RT "TIP60 K430 SUMOylation attenuates its interaction with DNA-PKcs in S-phase RT cells: Facilitating homologous recombination and emerging target for cancer RT therapy."; RL Sci. Adv. 6:eaba7822-eaba7822(2020). RN [65] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACETYLATION, RP INTERACTION WITH APP AND APBB1, AND MUTAGENESIS OF 377-GLN--GLY-380. RX PubMed=33938178; DOI=10.1515/hsz-2020-0279; RA Probst S., Riese F., Kaegi L., Krueger M., Russi N., Nitsch R.M., RA Konietzko U.; RT "Lysine acetyltransferase Tip60 acetylates the APP adaptor Fe65 to increase RT its transcriptional activity."; RL Biol. Chem. 402:481-499(2021). RN [66] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=34077757; DOI=10.1016/j.molcel.2021.05.005; RA Liu R., Lee J.H., Li J., Yu R., Tan L., Xia Y., Zheng Y., Bian X.L., RA Lorenzi P.L., Chen Q., Lu Z.; RT "Choline kinase alpha 2 acts as a protein kinase to promote lipolysis of RT lipid droplets."; RL Mol. Cell 81:2722-2735(2021). RN [67] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=34608293; DOI=10.1038/s41589-021-00875-7; RA Song X., Yang F., Liu X., Xia P., Yin W., Wang Z., Wang Y., Yuan X., RA Dou Z., Jiang K., Ma M., Hu B., Zhang R., Xu C., Zhang Z., Ruan K., RA Tian R., Li L., Liu T., Hill D.L., Zang J., Liu X., Li J., Cheng J., RA Yao X.; RT "Dynamic crotonylation of EB1 by TIP60 ensures accurate spindle positioning RT in mitosis."; RL Nat. Chem. Biol. 17:1314-1323(2021). RN [68] RP INVOLVEMENT IN NEDFASB, VARIANTS NEDFASB HIS-53; SER-369 AND ALA-413, RP CHARACTERIZATION OF VARIANTS NEDFASB HIS-53; SER-369 AND ALA-413, FUNCTION, RP AND CATALYTIC ACTIVITY. RX PubMed=32822602; DOI=10.1016/j.ajhg.2020.08.002; RA Humbert J., Salian S., Makrythanasis P., Lemire G., Rousseau J., RA Ehresmann S., Garcia T., Alasiri R., Bottani A., Hanquinet S., Beaver E., RA Heeley J., Smith A.C.M., Berger S.I., Antonarakis S.E., Yang X.J., Cote J., RA Campeau P.M.; RT "De Novo KAT5 Variants Cause a Syndrome with Recognizable Facial RT Dysmorphisms, Cerebellar Atrophy, Sleep Disturbance, and Epilepsy."; RL Am. J. Hum. Genet. 107:564-574(2020). RN [69] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 227-506 IN COMPLEX WITH ACETYL-COA RP AND ZINC IONS, AND ACETYLATION AT LYS-327. RG Structural genomics consortium (SGC); RT "The crystal structure of acetyltransferase domain of human HIV-1 TAT RT interacting protein in complex with acetylcoenzyme A."; RL Submitted (FEB-2009) to the PDB data bank. RN [70] RP STRUCTURE BY NMR OF 5-78. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of RUH-073, a pseudo chromo domain from human cDNA."; RL Submitted (FEB-2009) to the PDB data bank. RN [71] {ECO:0007744|PDB:4QQG} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-80. RX PubMed=29494751; DOI=10.1002/1873-3468.13021; RA Zhang Y., Lei M., Yang X., Feng Y., Yang Y., Loppnau P., Li Y., Yang Y., RA Min J., Liu Y.; RT "Structural and histone binding studies of the chromo barrel domain of RT TIP60."; RL FEBS Lett. 592:1221-1232(2018). CC -!- FUNCTION: Catalytic subunit of the NuA4 histone acetyltransferase CC complex, a multiprotein complex involved in transcriptional activation CC of select genes principally by acetylation of nucleosomal histones H2A CC and H4 (PubMed:12776177, PubMed:15042092, PubMed:15121871, CC PubMed:15310756, PubMed:14966270, PubMed:16387653, PubMed:19909775, CC PubMed:25865756, PubMed:27153538, PubMed:29335245, PubMed:29174981, CC PubMed:33076429, PubMed:32822602). Histone acetylation alters CC nucleosome-DNA interactions and promotes interaction of the modified CC histones with other proteins which positively regulate transcription CC (PubMed:12776177, PubMed:15042092, PubMed:15121871, PubMed:15310756, CC PubMed:14966270). The NuA4 histone acetyltransferase complex is CC required for the activation of transcriptional programs associated with CC proto-oncogene mediated growth induction, tumor suppressor mediated CC growth arrest and replicative senescence, apoptosis, and DNA repair CC (PubMed:17709392, PubMed:19783983, PubMed:32832608). The NuA4 complex CC plays a direct role in repair of DNA double-strand breaks (DSBs) by CC promoting homologous recombination (HR): the complex inhibits TP53BP1 CC binding to chromatin via MBTD1, which recognizes and binds histone H4 CC trimethylated at 'Lys-20' (H4K20me), and KAT5 that catalyzes CC acetylation of 'Lys-15' of histone H2A (H2AK15ac), thereby blocking the CC ubiquitination mark required for TP53BP1 localization at DNA breaks CC (PubMed:27153538, PubMed:32832608). Also involved in DSB repair by CC mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac), promoting CC NBN/NBS1 assembly at the sites of DNA damage (PubMed:17709392, CC PubMed:26438602). The NuA4 complex plays a key role in hematopoietic CC stem cell maintenance and is required to maintain acetylated CC H2A.Z/H2AZ1 at MYC target genes (By similarity). The NuA4 complex is CC also required for spermatid development by promoting acetylation of CC histones: histone hyperacetylation is required for histone replacement CC during the transition from round to elongating spermatids (By CC similarity). Component of a SWR1-like complex that specifically CC mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome CC (PubMed:24463511). Also acetylates non-histone proteins, such as BMAL1, CC ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, NDC80/HEC1, NR1D2, RAN, SOX4, CC FOXP3, SQSTM1, ULK1 and RUBCNL/Pacer (PubMed:16141325, PubMed:17360565, CC PubMed:17996965, PubMed:24835996, PubMed:26829474, PubMed:29040603, CC PubMed:30409912, PubMed:30704899, PubMed:31857589, PubMed:32034146, CC PubMed:32817552, PubMed:34077757). Directly acetylates and activates CC ATM (PubMed:16141325). Promotes nucleotide excision repair (NER) by CC mediating acetylation of ERCC4/XPF, thereby promoting formation of the CC ERCC4-ERCC1 complex (PubMed:32034146). Relieves NR1D2-mediated CC inhibition of APOC3 expression by acetylating NR1D2 (PubMed:17996965). CC Acts as a regulator of regulatory T-cells (Treg) by catalyzing FOXP3 CC acetylation, thereby promoting FOXP3 transcriptional repressor activity CC (PubMed:17360565, PubMed:24835996). Involved in skeletal myoblast CC differentiation by mediating acetylation of SOX4 (PubMed:26291311). CC Catalyzes acetylation of APBB1/FE65, increasing its transcription CC activator activity (PubMed:33938178). Promotes transcription elongation CC during the activation phase of the circadian cycle by catalyzing CC acetylation of BMAL1, promoting elongation of circadian transcripts (By CC similarity). Together with GSK3 (GSK3A or GSK3B), acts as a regulator CC of autophagy: phosphorylated at Ser-86 by GSK3 under starvation CC conditions, leading to activate acetyltransferase activity and promote CC acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer CC (PubMed:30704899). Acts as a regulator of the cGAS-STING innate CC antiviral response by catalyzing acetylation the N-terminus of CGAS, CC thereby promoting CGAS DNA-binding and activation (PubMed:32817552). CC Also regulates lipid metabolism by mediating acetylation of CHKA or CC LPIN1 (PubMed:34077757). Promotes lipolysis of lipid droplets following CC glucose deprivation by mediating acetylation of isoform 1 of CHKA, CC thereby promoting monomerization of CHKA and its conversion into a CC tyrosine-protein kinase (PubMed:34077757). Acts as a regulator of CC fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation CC of LPIN1, thereby promoting the synthesis of diacylglycerol CC (PubMed:29765047). In addition to protein acetyltransferase, can use CC different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) CC and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to CC mediate protein crotonylation and 2-hydroxyisobutyrylation, CC respectively (PubMed:29192674, PubMed:34608293). Acts as a key CC regulator of chromosome segregation and kinetochore-microtubule CC attachment during mitosis by mediating acetylation or crotonylation of CC target proteins (PubMed:26829474, PubMed:29040603, PubMed:30409912, CC PubMed:34608293). Catalyzes acetylation of AURKB at kinetochores, CC increasing AURKB activity and promoting accurate chromosome segregation CC in mitosis (PubMed:26829474). Acetylates RAN during mitosis, promoting CC microtubule assembly at mitotic chromosomes (PubMed:29040603). CC Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore- CC microtubule attachment (PubMed:30409912). Catalyzes crotonylation of CC MAPRE1/EB1, thereby ensuring accurate spindle positioning in mitosis CC (PubMed:34608293). {ECO:0000250|UniProtKB:Q8CHK4, CC ECO:0000269|PubMed:12776177, ECO:0000269|PubMed:14966270, CC ECO:0000269|PubMed:15042092, ECO:0000269|PubMed:15121871, CC ECO:0000269|PubMed:15310756, ECO:0000269|PubMed:16141325, CC ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:17360565, CC ECO:0000269|PubMed:17709392, ECO:0000269|PubMed:17996965, CC ECO:0000269|PubMed:19783983, ECO:0000269|PubMed:19909775, CC ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:24835996, CC ECO:0000269|PubMed:25865756, ECO:0000269|PubMed:26291311, CC ECO:0000269|PubMed:26438602, ECO:0000269|PubMed:26829474, CC ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:29040603, CC ECO:0000269|PubMed:29174981, ECO:0000269|PubMed:29192674, CC ECO:0000269|PubMed:29335245, ECO:0000269|PubMed:29765047, CC ECO:0000269|PubMed:30409912, ECO:0000269|PubMed:30704899, CC ECO:0000269|PubMed:31857589, ECO:0000269|PubMed:32034146, CC ECO:0000269|PubMed:32817552, ECO:0000269|PubMed:32822602, CC ECO:0000269|PubMed:32832608, ECO:0000269|PubMed:33076429, CC ECO:0000269|PubMed:33938178, ECO:0000269|PubMed:34077757, CC ECO:0000269|PubMed:34608293}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000269|PubMed:10096020, ECO:0000269|PubMed:12468530, CC ECO:0000269|PubMed:25865756, ECO:0000269|PubMed:26438602, CC ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:29174981, CC ECO:0000269|PubMed:32822602, ECO:0000269|PubMed:33076429}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; CC Evidence={ECO:0000269|PubMed:25865756, ECO:0000269|PubMed:26438602, CC ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:29174981, CC ECO:0000269|PubMed:33076429, ECO:0000305|PubMed:32822602}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; CC Evidence={ECO:0000269|PubMed:24835996, ECO:0000269|PubMed:25865756, CC ECO:0000269|PubMed:26291311, ECO:0000269|PubMed:26829474, CC ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:29765047, CC ECO:0000269|PubMed:30409912, ECO:0000269|PubMed:30704899, CC ECO:0000269|PubMed:31857589, ECO:0000269|PubMed:32034146, CC ECO:0000269|PubMed:32817552, ECO:0000269|PubMed:33938178, CC ECO:0000269|PubMed:34077757}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; CC Evidence={ECO:0000269|PubMed:24835996, ECO:0000269|PubMed:26291311, CC ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:29765047, CC ECO:0000269|PubMed:30409912, ECO:0000269|PubMed:31857589, CC ECO:0000269|PubMed:32034146, ECO:0000269|PubMed:32817552, CC ECO:0000269|PubMed:33938178, ECO:0000269|PubMed:34077757}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)- CC (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA- CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, CC ChEBI:CHEBI:137954; Evidence={ECO:0000269|PubMed:34608293}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909; CC Evidence={ECO:0000269|PubMed:34608293}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180, CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780, CC ChEBI:CHEBI:144968; Evidence={ECO:0000269|PubMed:29192674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181; CC Evidence={ECO:0000269|PubMed:29192674}; CC -!- ACTIVITY REGULATION: Acyltransferase and acetyltransferase activities CC are activated by phosphorylation and autoacetylation (PubMed:20100829, CC PubMed:30704899). Autoacetylation activates the histone CC acetyltransferase activity (PubMed:20100829, PubMed:25865756, CC PubMed:30704899). {ECO:0000269|PubMed:20100829, CC ECO:0000269|PubMed:25865756, ECO:0000269|PubMed:30704899}. CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400, CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, CC YEATS4/GAS41, VPS72/YL1 and MEAF6 (PubMed:12963728, PubMed:10966108, CC PubMed:15196461, PubMed:14966270, PubMed:29174981). KAT5/TIP60, EPC1, CC and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. CC The NuA4 complex interacts with MYC (PubMed:12776177). Interacts with CC ATM (PubMed:16141325). Interacts with JADE1 (PubMed:15502158). CC Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7 (PubMed:11416127, CC PubMed:11262386, PubMed:12551922). Interacts with the cytoplasmic tail CC of APP and APBB1/FE65 (PubMed:33938178). Interacts with TRIM24 and CC TRIM68 (PubMed:18451177, PubMed:19909775). Forms a complex with SENP6 CC and UBE2I in response to UV irradiation. Identified in a complex with CC HINT1 (PubMed:16835243). Interacts with ATF2 and CUL3 CC (PubMed:18397884). Interacts with NR1D2 (via N-terminus) CC (PubMed:17996965). Component of a SWR1-like complex (PubMed:24463511). CC Interacts with FOXP3 (PubMed:17360565, PubMed:24835996). Interacts with CC ZBTB49 (PubMed:25245946). Interacts with SRF (By similarity). Interacts CC with ATF3; promoting autoacetylation and deubiquitination by USP7 CC (PubMed:25865756). Interacts with EP300/p300; interaction promotes KAT5 CC autoacetylation (PubMed:24835996). Interacts with PRKDC; interaction is CC impaired following KAT5 sumoylation (PubMed:32832608). Interacts with CC GPR50 (PubMed:21858214). Interacts with NME3; this interaction enables CC recruitment of NME3 at DNA damage sites where it plays a role in the CC repair of DNA (PubMed:26945015). {ECO:0000250|UniProtKB:Q8CHK4, CC ECO:0000269|PubMed:10966108, ECO:0000269|PubMed:11262386, CC ECO:0000269|PubMed:11416127, ECO:0000269|PubMed:12551922, CC ECO:0000269|PubMed:12776177, ECO:0000269|PubMed:12963728, CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15502158, CC ECO:0000269|PubMed:16001085, ECO:0000269|PubMed:16141325, CC ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:17360565, CC ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:18397884, CC ECO:0000269|PubMed:18451177, ECO:0000269|PubMed:19909775, CC ECO:0000269|PubMed:21858214, ECO:0000269|PubMed:24463511, CC ECO:0000269|PubMed:24835996, ECO:0000269|PubMed:25245946, CC ECO:0000269|PubMed:26945015, ECO:0000269|PubMed:29174981, CC ECO:0000269|PubMed:32832608, ECO:0000269|PubMed:33938178, CC ECO:0000269|Ref.69, ECO:0000303|PubMed:15196461}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 TAT. CC {ECO:0000269|PubMed:16001085, ECO:0000269|PubMed:8607265}. CC -!- INTERACTION: CC Q92993; P01023: A2M; NbExp=3; IntAct=EBI-399080, EBI-640741; CC Q92993; Q15027: ACAP1; NbExp=3; IntAct=EBI-399080, EBI-751746; CC Q92993; Q9NPJ3: ACOT13; NbExp=3; IntAct=EBI-399080, EBI-1045357; CC Q92993; Q15699: ALX1; NbExp=3; IntAct=EBI-399080, EBI-750671; CC Q92993; Q8IWZ3-3: ANKHD1; NbExp=3; IntAct=EBI-399080, EBI-25833200; CC Q92993; O00213-2: APBB1; NbExp=3; IntAct=EBI-399080, EBI-13307975; CC Q92993; P05067: APP; NbExp=3; IntAct=EBI-399080, EBI-77613; CC Q92993; O43307: ARHGEF9; NbExp=3; IntAct=EBI-399080, EBI-3447299; CC Q92993; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-399080, EBI-5280499; CC Q92993; Q9Y576: ASB1; NbExp=3; IntAct=EBI-399080, EBI-2323092; CC Q92993; P54253: ATXN1; NbExp=9; IntAct=EBI-399080, EBI-930964; CC Q92993; Q96GD4: AURKB; NbExp=4; IntAct=EBI-399080, EBI-624291; CC Q92993; Q14032: BAAT; NbExp=3; IntAct=EBI-399080, EBI-8994378; CC Q92993; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-399080, EBI-1642333; CC Q92993; Q13072: BAGE; NbExp=3; IntAct=EBI-399080, EBI-25884811; CC Q92993; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-399080, EBI-2548012; CC Q92993; Q6PH81: C16orf87; NbExp=3; IntAct=EBI-399080, EBI-6598617; CC Q92993; Q8NDD1-6: C1orf131; NbExp=3; IntAct=EBI-399080, EBI-17761821; CC Q92993; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-399080, EBI-2559016; CC Q92993; Q9HC52: CBX8; NbExp=2; IntAct=EBI-399080, EBI-712912; CC Q92993; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-399080, EBI-11977221; CC Q92993; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-399080, EBI-10171416; CC Q92993; Q96HJ3-2: CCDC34; NbExp=3; IntAct=EBI-399080, EBI-17641690; CC Q92993; Q96A33: CCDC47; NbExp=3; IntAct=EBI-399080, EBI-720151; CC Q92993; Q9GZT6: CCDC90B; NbExp=3; IntAct=EBI-399080, EBI-713148; CC Q92993; Q7Z7K6: CENPV; NbExp=3; IntAct=EBI-399080, EBI-1210604; CC Q92993; Q9P2H0: CEP126; NbExp=2; IntAct=EBI-399080, EBI-473176; CC Q92993; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-399080, EBI-739624; CC Q92993; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-399080, EBI-742887; CC Q92993; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-399080, EBI-743375; CC Q92993; Q99828: CIB1; NbExp=3; IntAct=EBI-399080, EBI-372594; CC Q92993; P15169: CPN1; NbExp=3; IntAct=EBI-399080, EBI-2116369; CC Q92993; P43234: CTSO; NbExp=3; IntAct=EBI-399080, EBI-2874283; CC Q92993; O95424: DEXI; NbExp=3; IntAct=EBI-399080, EBI-724515; CC Q92993; O43261: DLEU1; NbExp=2; IntAct=EBI-399080, EBI-710057; CC Q92993; Q9NQM4: DNAAF6; NbExp=6; IntAct=EBI-399080, EBI-10239299; CC Q92993; P50570-2: DNM2; NbExp=3; IntAct=EBI-399080, EBI-10968534; CC Q92993; O43598: DNPH1; NbExp=3; IntAct=EBI-399080, EBI-748674; CC Q92993; P21728: DRD1; NbExp=3; IntAct=EBI-399080, EBI-6624459; CC Q92993; Q16254: E2F4; NbExp=3; IntAct=EBI-399080, EBI-448943; CC Q92993; P20042: EIF2S2; NbExp=3; IntAct=EBI-399080, EBI-711977; CC Q92993; P60228: EIF3E; NbExp=3; IntAct=EBI-399080, EBI-347740; CC Q92993; Q9H2F5-2: EPC1; NbExp=3; IntAct=EBI-399080, EBI-11023729; CC Q92993; Q96J88-3: EPSTI1; NbExp=3; IntAct=EBI-399080, EBI-25885343; CC Q92993; P03372-1: ESR1; NbExp=3; IntAct=EBI-399080, EBI-15606245; CC Q92993; Q01844: EWSR1; NbExp=2; IntAct=EBI-399080, EBI-739737; CC Q92993; Q3B820: FAM161A; NbExp=3; IntAct=EBI-399080, EBI-719941; CC Q92993; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-399080, EBI-11977403; CC Q92993; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-399080, EBI-10172181; CC Q92993; Q9BZS1-1: FOXP3; NbExp=2; IntAct=EBI-399080, EBI-9695448; CC Q92993; Q8IVH2-2: FOXP4; NbExp=3; IntAct=EBI-399080, EBI-25885364; CC Q92993; Q96NE9-2: FRMD6; NbExp=3; IntAct=EBI-399080, EBI-13213391; CC Q92993; O14926: FSCN2; NbExp=3; IntAct=EBI-399080, EBI-21017948; CC Q92993; P35637: FUS; NbExp=2; IntAct=EBI-399080, EBI-400434; CC Q92993; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-399080, EBI-618189; CC Q92993; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-399080, EBI-9088619; CC Q92993; O95257: GADD45G; NbExp=2; IntAct=EBI-399080, EBI-448202; CC Q92993; P19440-3: GGT1; NbExp=3; IntAct=EBI-399080, EBI-21558069; CC Q92993; O75420: GIGYF1; NbExp=3; IntAct=EBI-399080, EBI-947774; CC Q92993; Q5VSY0: GKAP1; NbExp=3; IntAct=EBI-399080, EBI-743722; CC Q92993; Q96IK5: GMCL1; NbExp=5; IntAct=EBI-399080, EBI-2548508; CC Q92993; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-399080, EBI-745707; CC Q92993; O95837: GNA14; NbExp=3; IntAct=EBI-399080, EBI-7951023; CC Q92993; Q96F32: GNB5; NbExp=3; IntAct=EBI-399080, EBI-25902214; CC Q92993; Q08379: GOLGA2; NbExp=3; IntAct=EBI-399080, EBI-618309; CC Q92993; O43292-2: GPAA1; NbExp=3; IntAct=EBI-399080, EBI-25884370; CC Q92993; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-399080, EBI-11959863; CC Q92993; P29084: GTF2E2; NbExp=3; IntAct=EBI-399080, EBI-2853321; CC Q92993; P62805: H4C9; NbExp=4; IntAct=EBI-399080, EBI-302023; CC Q92993; O00165: HAX1; NbExp=3; IntAct=EBI-399080, EBI-357001; CC Q92993; Q8N7T0: hCG_1820408; NbExp=3; IntAct=EBI-399080, EBI-25858908; CC Q92993; Q6NT76: HMBOX1; NbExp=6; IntAct=EBI-399080, EBI-2549423; CC Q92993; P52597: HNRNPF; NbExp=3; IntAct=EBI-399080, EBI-352986; CC Q92993; Q92826: HOXB13; NbExp=3; IntAct=EBI-399080, EBI-11317274; CC Q92993; P09017: HOXC4; NbExp=3; IntAct=EBI-399080, EBI-3923226; CC Q92993; Q03933-2: HSF2; NbExp=3; IntAct=EBI-399080, EBI-10223348; CC Q92993; O75031: HSF2BP; NbExp=3; IntAct=EBI-399080, EBI-7116203; CC Q92993; P42858: HTT; NbExp=15; IntAct=EBI-399080, EBI-466029; CC Q92993; Q02363: ID2; NbExp=3; IntAct=EBI-399080, EBI-713450; CC Q92993; Q02535: ID3; NbExp=3; IntAct=EBI-399080, EBI-1387094; CC Q92993; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-399080, EBI-9091197; CC Q92993; Q96FT9-2: IFT43; NbExp=3; IntAct=EBI-399080, EBI-11944538; CC Q92993; P78318: IGBP1; NbExp=3; IntAct=EBI-399080, EBI-1055954; CC Q92993; P17936: IGFBP3; NbExp=3; IntAct=EBI-399080, EBI-715709; CC Q92993; Q9UKT9: IKZF3; NbExp=6; IntAct=EBI-399080, EBI-747204; CC Q92993; P26951: IL3RA; NbExp=3; IntAct=EBI-399080, EBI-1757512; CC Q92993; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-399080, EBI-743960; CC Q92993; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-399080, EBI-11954971; CC Q92993; Q9Y4X4: KLF12; NbExp=3; IntAct=EBI-399080, EBI-750750; CC Q92993; O00505: KPNA3; NbExp=3; IntAct=EBI-399080, EBI-358297; CC Q92993; O00629: KPNA4; NbExp=3; IntAct=EBI-399080, EBI-396343; CC Q92993; O15131: KPNA5; NbExp=3; IntAct=EBI-399080, EBI-540602; CC Q92993; O60684: KPNA6; NbExp=3; IntAct=EBI-399080, EBI-359923; CC Q92993; Q5JUW0-3: KRBOX4; NbExp=3; IntAct=EBI-399080, EBI-12893625; CC Q92993; Q6A162: KRT40; NbExp=3; IntAct=EBI-399080, EBI-10171697; CC Q92993; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-399080, EBI-10172052; CC Q92993; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-399080, EBI-9996449; CC Q92993; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-399080, EBI-25835523; CC Q92993; Q9Y234: LIPT1; NbExp=3; IntAct=EBI-399080, EBI-727376; CC Q92993; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-399080, EBI-2341787; CC Q92993; P51884: LUM; NbExp=3; IntAct=EBI-399080, EBI-725780; CC Q92993; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-399080, EBI-1216080; CC Q92993; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-399080, EBI-741037; CC Q92993; Q96GV9: MACIR; NbExp=3; IntAct=EBI-399080, EBI-2350695; CC Q92993; Q9H213: MAGEH1; NbExp=3; IntAct=EBI-399080, EBI-473834; CC Q92993; P80192: MAP3K9; NbExp=3; IntAct=EBI-399080, EBI-3951604; CC Q92993; Q15759: MAPK11; NbExp=3; IntAct=EBI-399080, EBI-298304; CC Q92993; P23508: MCC; NbExp=3; IntAct=EBI-399080, EBI-307531; CC Q92993; Q99750: MDFI; NbExp=3; IntAct=EBI-399080, EBI-724076; CC Q92993; A0JLT2-2: MED19; NbExp=3; IntAct=EBI-399080, EBI-13288755; CC Q92993; P50222: MEOX2; NbExp=3; IntAct=EBI-399080, EBI-748397; CC Q92993; P41218: MNDA; NbExp=3; IntAct=EBI-399080, EBI-2829677; CC Q92993; Q8N983-3: MRPL43; NbExp=3; IntAct=EBI-399080, EBI-11109389; CC Q92993; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-399080, EBI-742948; CC Q92993; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-399080, EBI-11522433; CC Q92993; Q16718: NDUFA5; NbExp=3; IntAct=EBI-399080, EBI-746417; CC Q92993; P49821: NDUFV1; NbExp=3; IntAct=EBI-399080, EBI-748312; CC Q92993; Q9Y2I6: NINL; NbExp=3; IntAct=EBI-399080, EBI-719716; CC Q92993; Q9HC29: NOD2; NbExp=2; IntAct=EBI-399080, EBI-7445625; CC Q92993; P11926: ODC1; NbExp=6; IntAct=EBI-399080, EBI-1044287; CC Q92993; Q2M1J6: OXA1L; NbExp=3; IntAct=EBI-399080, EBI-9978021; CC Q92993; Q16342: PDCD2; NbExp=3; IntAct=EBI-399080, EBI-359462; CC Q92993; Q9BRX2: PELO; NbExp=3; IntAct=EBI-399080, EBI-1043580; CC Q92993; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-399080, EBI-713786; CC Q92993; Q9Y6X2: PIAS3; NbExp=3; IntAct=EBI-399080, EBI-2803703; CC Q92993; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-399080, EBI-79165; CC Q92993; Q86T03: PIP4P1; NbExp=3; IntAct=EBI-399080, EBI-6164623; CC Q92993; Q6P1J6-2: PLB1; NbExp=3; IntAct=EBI-399080, EBI-10694821; CC Q92993; D3DTS7: PMP22; NbExp=3; IntAct=EBI-399080, EBI-25882629; CC Q92993; Q9UNA4: POLI; NbExp=3; IntAct=EBI-399080, EBI-741774; CC Q92993; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-399080, EBI-710402; CC Q92993; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-399080, EBI-11320284; CC Q92993; P07225: PROS1; NbExp=3; IntAct=EBI-399080, EBI-2803380; CC Q92993; Q86WR7-2: PROSER2; NbExp=3; IntAct=EBI-399080, EBI-13089670; CC Q92993; P29074: PTPN4; NbExp=2; IntAct=EBI-399080, EBI-710431; CC Q92993; Q3YEC7-3: RABL6; NbExp=3; IntAct=EBI-399080, EBI-25885259; CC Q92993; Q96I51: RCC1L; NbExp=3; IntAct=EBI-399080, EBI-2117080; CC Q92993; O94844: RHOBTB1; NbExp=3; IntAct=EBI-399080, EBI-6426999; CC Q92993; Q9UJD0: RIMS3; NbExp=3; IntAct=EBI-399080, EBI-3909436; CC Q92993; Q9NWS8-3: RMND1; NbExp=3; IntAct=EBI-399080, EBI-25884400; CC Q92993; Q9Y508: RNF114; NbExp=3; IntAct=EBI-399080, EBI-723587; CC Q92993; Q9ULK6-3: RNF150; NbExp=3; IntAct=EBI-399080, EBI-36513929; CC Q92993; P62913-2: RPL11; NbExp=3; IntAct=EBI-399080, EBI-11027771; CC Q92993; P18077: RPL35A; NbExp=3; IntAct=EBI-399080, EBI-353383; CC Q92993; Q9Y265: RUVBL1; NbExp=5; IntAct=EBI-399080, EBI-353675; CC Q92993; Q96FV2: SCRN2; NbExp=3; IntAct=EBI-399080, EBI-11306862; CC Q92993; Q99643: SDHC; NbExp=3; IntAct=EBI-399080, EBI-1224539; CC Q92993; Q14141: SEPTIN6; NbExp=3; IntAct=EBI-399080, EBI-745901; CC Q92993; Q14140: SERTAD2; NbExp=3; IntAct=EBI-399080, EBI-2822051; CC Q92993; Q01105-2: SET; NbExp=3; IntAct=EBI-399080, EBI-7481343; CC Q92993; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-399080, EBI-12037847; CC Q92993; Q13573: SNW1; NbExp=3; IntAct=EBI-399080, EBI-632715; CC Q92993; Q9Y5X0: SNX10; NbExp=3; IntAct=EBI-399080, EBI-10329478; CC Q92993; Q8WV41: SNX33; NbExp=3; IntAct=EBI-399080, EBI-2481535; CC Q92993; Q92673: SORL1; NbExp=3; IntAct=EBI-399080, EBI-1171329; CC Q92993; P56693: SOX10; NbExp=3; IntAct=EBI-399080, EBI-1167533; CC Q92993; P35711: SOX5; NbExp=3; IntAct=EBI-399080, EBI-3505701; CC Q92993; Q9UM82: SPATA2; NbExp=3; IntAct=EBI-399080, EBI-744066; CC Q92993; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-399080, EBI-5235340; CC Q92993; Q01130: SRSF2; NbExp=3; IntAct=EBI-399080, EBI-627047; CC Q92993; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-399080, EBI-2212028; CC Q92993; Q13586: STIM1; NbExp=3; IntAct=EBI-399080, EBI-448878; CC Q92993; Q9NZ72: STMN3; NbExp=3; IntAct=EBI-399080, EBI-725557; CC Q92993; Q13033-2: STRN3; NbExp=3; IntAct=EBI-399080, EBI-1053876; CC Q92993; O75558: STX11; NbExp=6; IntAct=EBI-399080, EBI-714135; CC Q92993; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-399080, EBI-6872807; CC Q92993; O43761: SYNGR3; NbExp=3; IntAct=EBI-399080, EBI-11321949; CC Q92993; Q92804: TAF15; NbExp=2; IntAct=EBI-399080, EBI-2255091; CC Q92993; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-399080, EBI-529518; CC Q92993; P15884: TCF4; NbExp=3; IntAct=EBI-399080, EBI-533224; CC Q92993; Q92481: TFAP2B; NbExp=3; IntAct=EBI-399080, EBI-725275; CC Q92993; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-399080, EBI-1105213; CC Q92993; P04183: TK1; NbExp=3; IntAct=EBI-399080, EBI-712550; CC Q92993; Q3YBM2: TMEM176B; NbExp=3; IntAct=EBI-399080, EBI-2821479; CC Q92993; Q969K7: TMEM54; NbExp=3; IntAct=EBI-399080, EBI-3922833; CC Q92993; Q9H8H3: TMT1A; NbExp=3; IntAct=EBI-399080, EBI-1390168; CC Q92993; O14656-2: TOR1A; NbExp=3; IntAct=EBI-399080, EBI-25847109; CC Q92993; P04637: TP53; NbExp=3; IntAct=EBI-399080, EBI-366083; CC Q92993; P36406: TRIM23; NbExp=3; IntAct=EBI-399080, EBI-740098; CC Q92993; P14373: TRIM27; NbExp=3; IntAct=EBI-399080, EBI-719493; CC Q92993; O94972: TRIM37; NbExp=3; IntAct=EBI-399080, EBI-741602; CC Q92993; Q9UJA5: TRMT6; NbExp=3; IntAct=EBI-399080, EBI-934061; CC Q92993; Q99598: TSNAX; NbExp=3; IntAct=EBI-399080, EBI-742638; CC Q92993; Q9NNX1: TUFT1; NbExp=3; IntAct=EBI-399080, EBI-2557363; CC Q92993; Q15672: TWIST1; NbExp=2; IntAct=EBI-399080, EBI-1797287; CC Q92993; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-399080, EBI-1380492; CC Q92993; P62837: UBE2D2; NbExp=3; IntAct=EBI-399080, EBI-347677; CC Q92993; Q96BW1: UPRT; NbExp=3; IntAct=EBI-399080, EBI-742943; CC Q92993; Q8NB14: USP38; NbExp=3; IntAct=EBI-399080, EBI-2512509; CC Q92993; Q15836: VAMP3; NbExp=3; IntAct=EBI-399080, EBI-722343; CC Q92993; O95498: VNN2; NbExp=3; IntAct=EBI-399080, EBI-21494555; CC Q92993; Q99986: VRK1; NbExp=6; IntAct=EBI-399080, EBI-1769146; CC Q92993; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-399080, EBI-12040603; CC Q92993; Q9BW85: YJU2; NbExp=3; IntAct=EBI-399080, EBI-10300345; CC Q92993; Q9Y2K1: ZBTB1; NbExp=3; IntAct=EBI-399080, EBI-2682961; CC Q92993; O43829: ZBTB14; NbExp=3; IntAct=EBI-399080, EBI-10176632; CC Q92993; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-399080, EBI-2515601; CC Q92993; Q96BR9: ZBTB8A; NbExp=4; IntAct=EBI-399080, EBI-742740; CC Q92993; Q53FD0-2: ZC2HC1C; NbExp=6; IntAct=EBI-399080, EBI-14104088; CC Q92993; Q9BQ24: ZFYVE21; NbExp=3; IntAct=EBI-399080, EBI-2849569; CC Q92993; Q15776: ZKSCAN8; NbExp=3; IntAct=EBI-399080, EBI-2602314; CC Q92993; Q14202: ZMYM3; NbExp=3; IntAct=EBI-399080, EBI-2556139; CC Q92993; Q05CR2: ZNF248; NbExp=3; IntAct=EBI-399080, EBI-25835471; CC Q92993; Q9UL40: ZNF346; NbExp=3; IntAct=EBI-399080, EBI-2462313; CC Q92993; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-399080, EBI-740727; CC Q92993; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-399080, EBI-12010736; CC Q92993; Q8NB15: ZNF511; NbExp=3; IntAct=EBI-399080, EBI-10269136; CC Q92993; Q8N8E2: ZNF513; NbExp=3; IntAct=EBI-399080, EBI-10279993; CC Q92993; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-399080, EBI-11035148; CC Q92993; Q9BU19: ZNF692; NbExp=3; IntAct=EBI-399080, EBI-12076976; CC Q92993; Q8NAM6: ZSCAN4; NbExp=3; IntAct=EBI-399080, EBI-7252920; CC Q92993; O15535: ZSCAN9; NbExp=3; IntAct=EBI-399080, EBI-751531; CC Q92993; Q9HBH6; NbExp=3; IntAct=EBI-399080, EBI-25901704; CC Q92993; P10085: Myod1; Xeno; NbExp=5; IntAct=EBI-399080, EBI-4405734; CC Q92993-2; P01023: A2M; NbExp=3; IntAct=EBI-20795332, EBI-640741; CC Q92993-2; P05067: APP; NbExp=3; IntAct=EBI-20795332, EBI-77613; CC Q92993-2; P54253: ATXN1; NbExp=3; IntAct=EBI-20795332, EBI-930964; CC Q92993-2; P23560-2: BDNF; NbExp=3; IntAct=EBI-20795332, EBI-12275524; CC Q92993-2; P35520: CBS; NbExp=3; IntAct=EBI-20795332, EBI-740135; CC Q92993-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-20795332, EBI-10976677; CC Q92993-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-20795332, EBI-10968534; CC Q92993-2; P04406: GAPDH; NbExp=3; IntAct=EBI-20795332, EBI-354056; CC Q92993-2; P07900: HSP90AA1; NbExp=3; IntAct=EBI-20795332, EBI-296047; CC Q92993-2; Q14114-3: LRP8; NbExp=3; IntAct=EBI-20795332, EBI-25832196; CC Q92993-2; P51608: MECP2; NbExp=3; IntAct=EBI-20795332, EBI-1189067; CC Q92993-2; P00491: PNP; NbExp=3; IntAct=EBI-20795332, EBI-712238; CC Q92993-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-20795332, EBI-5235340; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11262386, CC ECO:0000269|PubMed:11416127, ECO:0000269|PubMed:12551922, CC ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17704809, CC ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:25301942, CC ECO:0000269|PubMed:33938178}. Chromosome {ECO:0000269|PubMed:25560918, CC ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:29335245, CC ECO:0000269|PubMed:33076429}. Cytoplasm {ECO:0000269|PubMed:25301942}. CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:26829474}. CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:34608293}. CC Nucleus, nucleolus {ECO:0000269|PubMed:16387653}. Cytoplasm, CC perinuclear region {ECO:0000269|PubMed:11262386}. Note=Upon stimulation CC with EDN1, it is exported from the nucleus to the perinuclear region CC and UV irradiation induces translocation into punctuate subnuclear CC structures named nuclear bodies (PubMed:11262386). Transiently CC localizes to kinetochores in early mitosis (PubMed:26829474). Localizes CC to spindle poles when chromosomes align during metaphase CC (PubMed:34608293). Localizes in the cytoplasm and nucleus of round CC spermatids (By similarity). {ECO:0000250|UniProtKB:Q8CHK4, CC ECO:0000269|PubMed:11262386, ECO:0000269|PubMed:26829474, CC ECO:0000269|PubMed:34608293}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=2; CC IsoId=Q92993-1; Sequence=Displayed; CC Name=1; Synonyms=PLIP {ECO:0000303|PubMed:11416127}; CC IsoId=Q92993-2; Sequence=VSP_007438; CC Name=3; CC IsoId=Q92993-3; Sequence=VSP_009104; CC Name=4; CC IsoId=Q92993-4; Sequence=VSP_009104, VSP_007438; CC -!- PTM: Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase CC (PubMed:12468530, PubMed:26829474, PubMed:29335245). The phosphorylated CC form has a higher activity (PubMed:12468530, PubMed:29335245). CC Phosphorylation at Ser-90 by CDK1 or CDK9 is a prerequisite for CC phosphorylation at Ser-86 by GSK3 (PubMed:26829474, PubMed:30704899). CC Phosphorylation at Ser-86 by GSK3 (GSK3A or GSK3B) activates CC acetyltransferase and acyltransferase activities (PubMed:30704899). CC Phosphorylation at Ser-90 by CDK9 promotes KAT5 recruitment to CC chromatin (PubMed:29335245). Phosphorylation by VRK1 following DNA CC damage promotes KAT5 association with chromatin and histone CC acetyltransferase activity (PubMed:33076429). CC {ECO:0000269|PubMed:12468530, ECO:0000269|PubMed:26829474, CC ECO:0000269|PubMed:29335245, ECO:0000269|PubMed:30704899, CC ECO:0000269|PubMed:33076429}. CC -!- PTM: Autoacetylated (PubMed:20100829, PubMed:24835996, PubMed:25301942, CC PubMed:26291311, PubMed:33938178). Autoacetylation is required for CC histone acetyltransferase activity (PubMed:20100829, PubMed:25865756). CC Autoacetylation at Lys-327 is facilitated by interaction with CC EP300/p300: it prevents ubiquitination and subsequent degradation by CC the proteasome and promotes acetylation of target proteins CC (PubMed:24835996). Deacetylated by HDAC3 and SIRT1 (PubMed:20100829, CC PubMed:25301942). Deacetylation by HDAC3 promotes its ubiquitination CC and cytoplasmic localization (PubMed:25301942). CC {ECO:0000269|PubMed:20100829, ECO:0000269|PubMed:24835996, CC ECO:0000269|PubMed:25301942, ECO:0000269|PubMed:25865756, CC ECO:0000269|PubMed:26291311, ECO:0000269|PubMed:33938178}. CC -!- PTM: Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of CC its histone acetyltransferase activity in UV-induced DNA damage CC response, as well as its translocation to nuclear bodies CC (PubMed:17704809). Sumoylation with SUMO2 by PIAS4 at Lys-430 promotes CC repair of DNA double-strand breaks (DSBs) via homologous recombination CC (HR) (PubMed:32832608). Sumoylation by PIAS4 impairs interaction with CC PRKDC, inhibiting non-homologous end joining (NHEJ)-mediated repair of CC DSBs, thereby facilitating HR (PubMed:32832608). Desumoylated by SENP3 CC (PubMed:32832608). {ECO:0000269|PubMed:17704809, CC ECO:0000269|PubMed:32832608}. CC -!- PTM: Ubiquitinated by MDM2, leading to its proteasome-dependent CC degradation (PubMed:11927554, PubMed:24835996). Ubiquitination is CC prevented by autoacetylation at Lys-327 (PubMed:24835996). CC Ubiquitinated following deacetylation by HDAC3, leading to cytoplasmic CC localization (PubMed:25301942). Deubiquitinated by USP7 following CC interaction with ATF3, promoting its stabilization (PubMed:25865756). CC {ECO:0000269|PubMed:11927554, ECO:0000269|PubMed:24835996, CC ECO:0000269|PubMed:25301942, ECO:0000269|PubMed:25865756}. CC -!- PTM: (Microbial infection) In case of HIV-1 infection, interaction with CC the viral Tat protein leads to KAT5 polyubiquitination and targets it CC to degradation. {ECO:0000269|PubMed:16001085}. CC -!- DISEASE: Neurodevelopmental disorder with dysmorphic facies, sleep CC disturbance, and brain abnormalities (NEDFASB) [MIM:619103]: A CC neurodevelopmental disorder characterized by severe global CC developmental delay, intellectual disability, poor or absent language, CC behavioral abnormalities, severe sleep disturbance, seizures, cerebral CC malformations, and craniofacial dysmorphism. Progressive cerebellar CC atrophy is also observed. Additional features may include genitourinary CC tract anomalies, hearing loss, and mild distal skeletal defects. CC {ECO:0000269|PubMed:32822602}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}. CC -!- CAUTION: The role of the Tudor-knot domain, also named chromo barrel or CC chromodomain, is unclear. Based on its similarity with some chromo CC domains, it was first reported to bind histone H3 trimethylated on CC 'Lys-4' and/or 'Lys-9' (H3K4me3 and/or H3K9me3, respectively) CC (PubMed:19783983, PubMed:25560918). However, another group was not able CC to see any binding to methylated histones (PubMed:29494751). The 3D CC structure of the domain suggests that the inability to bind histones is CC caused by occlusion of the putative peptide-binding site by a basic CC amino acid side chain within a unique beta hairpin (PubMed:29494751). CC {ECO:0000269|PubMed:19783983, ECO:0000269|PubMed:25560918, CC ECO:0000269|PubMed:29494751, ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB02683.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/htatip/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40893/HTATIP"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U74667; AAB18236.1; -; mRNA. DR EMBL; U40989; AAB02683.1; ALT_INIT; mRNA. DR EMBL; U67734; AAD00163.1; -; mRNA. DR EMBL; AY214165; AAO21130.1; -; Genomic_DNA. DR EMBL; AK304664; BAG65439.1; -; mRNA. DR EMBL; AP001266; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74427.1; -; Genomic_DNA. DR EMBL; CH471076; EAW74429.1; -; Genomic_DNA. DR EMBL; BC000166; AAH00166.3; -; mRNA. DR EMBL; BC064912; AAH64912.1; -; mRNA. DR EMBL; BC093032; AAH93032.1; -; mRNA. DR EMBL; BC143296; AAI43297.1; -; mRNA. DR EMBL; BC117167; AAI17168.1; -; mRNA. DR CCDS; CCDS31610.1; -. [Q92993-1] DR CCDS; CCDS55771.1; -. [Q92993-4] DR CCDS; CCDS8109.1; -. [Q92993-2] DR CCDS; CCDS8110.1; -. [Q92993-3] DR RefSeq; NP_001193762.1; NM_001206833.1. [Q92993-4] DR RefSeq; NP_006379.2; NM_006388.3. [Q92993-1] DR RefSeq; NP_874368.1; NM_182709.2. [Q92993-2] DR RefSeq; NP_874369.1; NM_182710.2. [Q92993-3] DR PDB; 2EKO; NMR; -; A=5-78. DR PDB; 2OU2; X-ray; 2.30 A; A=227-506. DR PDB; 4QQG; X-ray; 2.80 A; A/B/C/D/E/F/G=1-80. DR PDBsum; 2EKO; -. DR PDBsum; 2OU2; -. DR PDBsum; 4QQG; -. DR AlphaFoldDB; Q92993; -. DR SMR; Q92993; -. DR BioGRID; 115779; 336. DR ComplexPortal; CPX-709; Piccolo NuA4 histone acetyltransferase complex. DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex. DR CORUM; Q92993; -. DR DIP; DIP-5998N; -. DR IntAct; Q92993; 315. DR MINT; Q92993; -. DR STRING; 9606.ENSP00000340330; -. DR BindingDB; Q92993; -. DR ChEMBL; CHEMBL5750; -. DR DrugBank; DB01992; Coenzyme A. DR DrugBank; DB02039; S-Acetyl-Cysteine. DR GuidetoPHARMACOLOGY; 2664; -. DR iPTMnet; Q92993; -. DR PhosphoSitePlus; Q92993; -. DR BioMuta; KAT5; -. DR DMDM; 30923328; -. DR CPTAC; CPTAC-2605; -. DR CPTAC; CPTAC-2606; -. DR EPD; Q92993; -. DR jPOST; Q92993; -. DR MassIVE; Q92993; -. DR MaxQB; Q92993; -. DR PaxDb; 9606-ENSP00000340330; -. DR PeptideAtlas; Q92993; -. DR ProteomicsDB; 75654; -. [Q92993-1] DR ProteomicsDB; 75655; -. [Q92993-2] DR ProteomicsDB; 75656; -. [Q92993-3] DR ProteomicsDB; 75657; -. [Q92993-4] DR Pumba; Q92993; -. DR Antibodypedia; 1823; 821 antibodies from 38 providers. DR DNASU; 10524; -. DR Ensembl; ENST00000341318.9; ENSP00000340330.4; ENSG00000172977.13. [Q92993-3] DR Ensembl; ENST00000352980.8; ENSP00000344955.4; ENSG00000172977.13. [Q92993-2] DR Ensembl; ENST00000377046.7; ENSP00000366245.3; ENSG00000172977.13. [Q92993-1] DR Ensembl; ENST00000530446.5; ENSP00000434765.1; ENSG00000172977.13. [Q92993-4] DR GeneID; 10524; -. DR KEGG; hsa:10524; -. DR MANE-Select; ENST00000341318.9; ENSP00000340330.4; NM_182710.3; NP_874369.1. [Q92993-3] DR UCSC; uc001ofi.4; human. [Q92993-1] DR AGR; HGNC:5275; -. DR CTD; 10524; -. DR DisGeNET; 10524; -. DR GeneCards; KAT5; -. DR HGNC; HGNC:5275; KAT5. DR HPA; ENSG00000172977; Low tissue specificity. DR MalaCards; KAT5; -. DR MIM; 601409; gene. DR MIM; 619103; phenotype. DR neXtProt; NX_Q92993; -. DR OpenTargets; ENSG00000172977; -. DR PharmGKB; PA162392746; -. DR VEuPathDB; HostDB:ENSG00000172977; -. DR eggNOG; KOG2747; Eukaryota. DR GeneTree; ENSGT00940000162343; -. DR HOGENOM; CLU_011815_2_0_1; -. DR InParanoid; Q92993; -. DR OMA; QYQRHGY; -. DR OrthoDB; 118560at2759; -. DR PhylomeDB; Q92993; -. DR TreeFam; TF317619; -. DR BRENDA; 2.3.1.48; 2681. DR PathwayCommons; Q92993; -. DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR). DR Reactome; R-HSA-5693548; Sensing of DNA Double Strand Breaks. DR Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA). DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates. DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ). DR Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange. DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR Reactome; R-HSA-9701192; Defective homologous recombination repair (HRR) due to BRCA1 loss of function. DR Reactome; R-HSA-9704331; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function. DR Reactome; R-HSA-9704646; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function. DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51. DR Reactome; R-HSA-9709603; Impaired BRCA2 binding to PALB2. DR Reactome; R-HSA-9733709; Cardiogenesis. DR SignaLink; Q92993; -. DR SIGNOR; Q92993; -. DR BioGRID-ORCS; 10524; 540 hits in 1180 CRISPR screens. DR ChiTaRS; KAT5; human. DR EvolutionaryTrace; Q92993; -. DR GeneWiki; KAT5; -. DR GenomeRNAi; 10524; -. DR Pharos; Q92993; Tchem. DR PRO; PR:Q92993; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q92993; Protein. DR Bgee; ENSG00000172977; Expressed in right uterine tube and 198 other cell types or tissues. DR ExpressionAtlas; Q92993; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProt. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB. DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB. DR GO; GO:0072487; C:MSL complex; IBA:GO_Central. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032777; C:piccolo histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0035861; C:site of double-strand break; IDA:UniProt. DR GO; GO:0000812; C:Swr1 complex; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl. DR GO; GO:0016407; F:acetyltransferase activity; TAS:Reactome. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043998; F:histone H2A acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043999; F:histone H2AK5 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0010485; F:histone H4 acetyltransferase activity; IDA:GO_Central. DR GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA. DR GO; GO:0140065; F:peptide butyryltransferase activity; IDA:UniProtKB. DR GO; GO:0140064; F:peptide crotonyltransferase activity; IDA:UniProtKB. DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl. DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB. DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0090398; P:cellular senescence; TAS:Reactome. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB. DR GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; IDA:UniProt. DR GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:1905691; P:lipid droplet disassembly; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProt. DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0021915; P:neural tube development; IEA:Ensembl. DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl. DR GO; GO:0006289; P:nucleotide-excision repair; IDA:UniProtKB. DR GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:UniProtKB. DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IDA:UniProtKB. DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB. DR GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:0045089; P:positive regulation of innate immune response; IDA:UniProt. DR GO; GO:0062033; P:positive regulation of mitotic sister chromatid segregation; IDA:UniProtKB. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:UniProtKB. DR GO; GO:1901985; P:positive regulation of protein acetylation; IDA:UniProtKB. DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; NAS:ComplexPortal. DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal. DR GO; GO:2000779; P:regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISS:UniProtKB. DR GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB. DR GO; GO:0035092; P:sperm DNA condensation; IEA:Ensembl. DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB. DR CDD; cd18985; CBD_TIP60_like; 1. DR CDD; cd04301; NAT_SF; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR IDEAL; IID00492; -. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR002717; HAT_MYST-type. DR InterPro; IPR025995; Tudor-knot. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR040706; Zf-MYST. DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1. DR Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF11717; Tudor-knot; 1. DR Pfam; PF17772; zf-MYST; 1. DR SMART; SM00298; CHROMO; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR PROSITE; PS51726; MYST_HAT; 1. DR Genevisible; Q92993; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Acyltransferase; KW Alternative splicing; Centromere; Chromatin regulator; Chromosome; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant; KW DNA damage; DNA repair; Growth regulation; Host-virus interaction; KW Immunity; Innate immunity; Intellectual disability; Isopeptide bond; KW Kinetochore; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Transferase; Ubl conjugation; KW Zinc; Zinc-finger. FT CHAIN 1..513 FT /note="Histone acetyltransferase KAT5" FT /id="PRO_0000051580" FT DOMAIN 8..65 FT /note="Tudor-knot" FT /evidence="ECO:0000255" FT DOMAIN 227..504 FT /note="MYST-type HAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063" FT ZN_FING 260..285 FT /note="C2HC MYST-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063, FT ECO:0000305|Ref.69" FT REGION 69..106 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 122..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 368..513 FT /note="Interaction with ATF2" FT /evidence="ECO:0000269|PubMed:18397884" FT ACT_SITE 403 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" FT BINDING 370..372 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|Ref.69" FT BINDING 377..383 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|Ref.69" FT BINDING 407 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|Ref.69" FT BINDING 416 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" FT MOD_RES 52 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 86 FT /note="Phosphoserine; by GSK3" FT /evidence="ECO:0000269|PubMed:12468530, FT ECO:0000269|PubMed:22539723, ECO:0000269|PubMed:29335245, FT ECO:0000269|PubMed:30704899, ECO:0007744|PubMed:23186163" FT MOD_RES 90 FT /note="Phosphoserine; by CDK1 and CDK9" FT /evidence="ECO:0000269|PubMed:12468530, FT ECO:0000269|PubMed:22539723, ECO:0000269|PubMed:26829474, FT ECO:0000269|PubMed:29335245, ECO:0007744|PubMed:23186163" FT MOD_RES 104 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:25301942, FT ECO:0000269|PubMed:29174981" FT MOD_RES 120 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:25301942" FT MOD_RES 148 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:25301942" FT MOD_RES 150 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:25301942" FT MOD_RES 187 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:25301942" FT MOD_RES 189 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:25301942" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 327 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:24835996, ECO:0000269|Ref.69" FT CROSSLNK 430 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000269|PubMed:17704809" FT CROSSLNK 430 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000269|PubMed:32832608" FT CROSSLNK 451 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:17704809" FT VAR_SEQ 4 FT /note="V -> VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ (in isoform FT 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:12801643, FT ECO:0000303|PubMed:14702039" FT /id="VSP_009104" FT VAR_SEQ 96..147 FT /note="Missing (in isoform 1 and isoform 4)" FT /evidence="ECO:0000303|PubMed:11416127, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_007438" FT VARIANT 53 FT /note="R -> H (in NEDFASB; decreased histone FT acetyltransferase activity; dbSNP:rs1857071943)" FT /evidence="ECO:0000269|PubMed:32822602" FT /id="VAR_085192" FT VARIANT 78 FT /note="P -> T (in dbSNP:rs11541271)" FT /id="VAR_059456" FT VARIANT 369 FT /note="C -> S (in NEDFASB; decreased histone FT acetyltransferase activity; dbSNP:rs1857215256)" FT /evidence="ECO:0000269|PubMed:32822602" FT /id="VAR_085193" FT VARIANT 413 FT /note="S -> A (in NEDFASB; decreased histone FT acetyltransferase activity; dbSNP:rs1857290083)" FT /evidence="ECO:0000269|PubMed:32822602" FT /id="VAR_085194" FT MUTAGEN 86 FT /note="S->A: Reduced phosphorylation. Abolishes FT phosphorylation; when associated with A-90. Reduced histone FT acetyltransferase activity. Abolished phosphorylation by FT GSK3 and decreased acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:12468530, FT ECO:0000269|PubMed:22539723, ECO:0000269|PubMed:30704899" FT MUTAGEN 90 FT /note="S->A: Reduced phosphorylation, leading to reduced FT protein acetyltransferase activity. Abolishes FT phosphorylation; when associated with A-86. Reduced histone FT acetyltransferase activity. Abolished phosphorylation by FT GSK3 at S-86." FT /evidence="ECO:0000269|PubMed:12468530, FT ECO:0000269|PubMed:22539723, ECO:0000269|PubMed:26829474, FT ECO:0000269|PubMed:29335245" FT MUTAGEN 90 FT /note="S->D: Mimics phosphorylation, promoting protein FT acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:26829474" FT MUTAGEN 104 FT /note="K->R: Impaired acetylation, leading to reduced FT histone acetyltransferase activity. In K6R; abolished FT autoacetylation; when associated with R-120, R-148, R-150, FT R-187 and R-189." FT /evidence="ECO:0000269|PubMed:25301942, FT ECO:0000269|PubMed:29174981" FT MUTAGEN 120 FT /note="K->R: In K6R; abolished autoacetylation; when FT associated with R-104, R-148, R-150, R-187 and R-189." FT /evidence="ECO:0000269|PubMed:25301942" FT MUTAGEN 148 FT /note="K->R: In K6R; abolished autoacetylation; when FT associated with R-104, R-120, R-150, R-187 and R-189." FT /evidence="ECO:0000269|PubMed:25301942" FT MUTAGEN 150 FT /note="K->R: In K6R; abolished autoacetylation; when FT associated with R-104, R-120, R-148, R-187 and R-189." FT /evidence="ECO:0000269|PubMed:25301942" FT MUTAGEN 187 FT /note="K->R: In K6R; abolished autoacetylation; when FT associated with R-104, R-120, R-148, R-150 and R-189." FT /evidence="ECO:0000269|PubMed:25301942" FT MUTAGEN 189 FT /note="K->R: In K6R; abolished autoacetylation; when FT associated with R-104, R-120, R-148, R-150 and R-187." FT /evidence="ECO:0000269|PubMed:25301942" FT MUTAGEN 254 FT /note="L->A: Does not affect phosphorylation; when FT associated with A-257." FT /evidence="ECO:0000269|PubMed:12468530" FT MUTAGEN 257 FT /note="L->A: Does not affect phosphorylation; when FT associated with A-254." FT /evidence="ECO:0000269|PubMed:12468530" FT MUTAGEN 327 FT /note="K->Q: Mimics acetylation; promoting interaction with FT FOXP3 and subsequent acetylation." FT /evidence="ECO:0000269|PubMed:24835996" FT MUTAGEN 327 FT /note="K->R: Decreased autoacetylation; leading to FT decreased acetyltransferase activity and ability to FT acetylate FOXP3." FT /evidence="ECO:0000269|PubMed:24835996" FT MUTAGEN 377..380 FT /note="QRRG->ERRE: In KAT5(QG/EE) mutant; abolished FT acetyltransferase activity. Impaired ability to activate FT CGAS." FT /evidence="ECO:0000269|PubMed:24835996, FT ECO:0000269|PubMed:26291311, ECO:0000269|PubMed:32034146, FT ECO:0000269|PubMed:32817552, ECO:0000269|PubMed:33938178" FT MUTAGEN 380 FT /note="G->A: Loss of function. Does not affect FT phosphorylation." FT /evidence="ECO:0000269|PubMed:12468530" FT MUTAGEN 430 FT /note="K->R: Abrogates sumoylation. Abolished sumoylation FT by PIAS4, promoting interaction with PRKDC, leading to FT decreased repair of DNA double-strand breaks (DSBs) via FT homologous recombination (HR)." FT /evidence="ECO:0000269|PubMed:17704809, FT ECO:0000269|PubMed:32832608" FT MUTAGEN 451 FT /note="K->R: Abrogates sumoylation." FT /evidence="ECO:0000269|PubMed:17704809" FT CONFLICT 382 FT /note="G -> R (in Ref. 1; AAB18236/AAB02683)" FT /evidence="ECO:0000305" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:4QQG" FT STRAND 12..15 FT /evidence="ECO:0007829|PDB:4QQG" FT STRAND 28..35 FT /evidence="ECO:0007829|PDB:4QQG" FT STRAND 37..40 FT /evidence="ECO:0007829|PDB:4QQG" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:4QQG" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:4QQG" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:4QQG" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:4QQG" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:2EKO" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:2OU2" FT HELIX 252..254 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:2OU2" FT TURN 264..266 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 269..271 FT /evidence="ECO:0007829|PDB:2OU2" FT HELIX 273..282 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 289..296 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 299..305 FT /evidence="ECO:0007829|PDB:2OU2" FT TURN 306..308 FT /evidence="ECO:0007829|PDB:2OU2" FT HELIX 310..321 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 336..345 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 348..360 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 365..368 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 370..372 FT /evidence="ECO:0007829|PDB:2OU2" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:2OU2" FT HELIX 381..395 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 400..402 FT /evidence="ECO:0007829|PDB:2OU2" FT HELIX 408..425 FT /evidence="ECO:0007829|PDB:2OU2" FT HELIX 441..448 FT /evidence="ECO:0007829|PDB:2OU2" FT HELIX 452..461 FT /evidence="ECO:0007829|PDB:2OU2" FT STRAND 469..474 FT /evidence="ECO:0007829|PDB:2OU2" FT HELIX 497..499 FT /evidence="ECO:0007829|PDB:2OU2" FT CONFLICT Q92993-3:32 FT /note="V -> A (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" SQ SEQUENCE 513 AA; 58582 MW; 63724F5E10B957D5 CRC64; MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ ASGKTLPIPV QITLRFNLPK EREAIPGGEP DQPLSSSSCL QPNHRSTKRK VEVVSPATPV PSETAPASVF PQNGAARRAV AAQPGRKRKS NCLGTDEDSQ DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH RLKPWYFSPY PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH IVGYFSKEKE STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG TPEKPLSDLG LLSYRSYWSQ TILEILMGLK SESGERPQIT INEISEITSI KKEDVISTLQ YLNLINYYKG QYILTLSEDI VDGHERAMLK RLLRIDSKCL HFTPKDWSKR GKW //