KAT5_HUMAN
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 03-AUG-2022, entry version 223.
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 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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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 [54]
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 [55]
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 [56]
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 [57]
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 [58]
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 [59]
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 [60]
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 [61]
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 [62]
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 [63]
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 [64]
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 [65]
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 [66]
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 [67]
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 [68] {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
CC ARNTL/BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, NDC80/HEC1,
CC NR1D2, RAN, SOX4, FOXP3, ULK1 and RUBCNL/Pacer (PubMed:16141325,
CC PubMed:17360565, PubMed:17996965, PubMed:24835996, PubMed:26829474,
CC PubMed:29040603, PubMed:30409912, PubMed:30704899, 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 ARNTL/BMAL1, promoting elongation of circadian
CC transcripts (By similarity). Together with GSK3 (GSK3A or GSK3B), acts
CC as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under
CC starvation conditions, leading to activate acetyltransferase activity
CC and promote acetylation of key autophagy regulators, such as ULK1 and
CC RUBCNL/Pacer (PubMed:30704899). Acts as a regulator of the cGAS-STING
CC innate antiviral response by catalyzing acetylation the N-terminus of
CC CGAS, thereby promoting CGAS DNA-binding and activation
CC (PubMed:32817552). Also regulates lipid metabolism by mediating
CC acetylation of CHKA or LPIN1 (PubMed:34077757). Promotes lipolysis of
CC lipid droplets following glucose deprivation by mediating acetylation
CC of isoform 1 of CHKA, thereby promoting monomerization of CHKA and its
CC conversion into a tyrosine-protein kinase (PubMed:34077757). Acts as a
CC regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing
CC acetylation 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:32034146, ECO:0000269|PubMed:32817552,
CC ECO:0000269|PubMed:32822602, ECO:0000269|PubMed:32832608,
CC ECO:0000269|PubMed:33076429, ECO:0000269|PubMed:33938178,
CC ECO:0000269|PubMed:34077757, 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:32034146, ECO:0000269|PubMed:32817552,
CC ECO:0000269|PubMed:33938178, 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:32034146,
CC ECO:0000269|PubMed:32817552, ECO:0000269|PubMed:33938178,
CC 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).
CC {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000269|PubMed:10966108,
CC ECO:0000269|PubMed:11262386, ECO:0000269|PubMed:11416127,
CC ECO:0000269|PubMed:12551922, ECO:0000269|PubMed:12776177,
CC ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14966270,
CC ECO:0000269|PubMed:15502158, ECO:0000269|PubMed:16001085,
CC ECO:0000269|PubMed:16141325, ECO:0000269|PubMed:16835243,
CC ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17996965,
CC ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:18451177,
CC ECO:0000269|PubMed:19909775, ECO:0000269|PubMed:24463511,
CC ECO:0000269|PubMed:24835996, ECO:0000269|PubMed:25245946,
CC ECO:0000269|PubMed:29174981, ECO:0000269|PubMed:32832608,
CC ECO:0000269|PubMed:33938178, ECO:0000269|Ref.66,
CC 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; 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; Q9H8H3: METTL7A; NbExp=3; IntAct=EBI-399080, EBI-1390168;
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-23640835;
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; 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="http://atlasgeneticsoncology.org/Genes/HTATIPID40893ch11q13.html";
CC ---------------------------------------------------------------------------
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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; 324.
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; Q92993; -.
DR PeptideAtlas; Q92993; -.
DR PRIDE; Q92993; -.
DR ProteomicsDB; 75654; -. [Q92993-1]
DR ProteomicsDB; 75655; -. [Q92993-2]
DR ProteomicsDB; 75656; -. [Q92993-3]
DR ProteomicsDB; 75657; -. [Q92993-4]
DR Antibodypedia; 1823; 739 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 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; SMTQNQT; -.
DR OrthoDB; 629545at2759; -.
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 HDR through Homologous Recombination (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 SignaLink; Q92993; -.
DR SIGNOR; Q92993; -.
DR BioGRID-ORCS; 10524; 522 hits in 1101 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 196 other tissues.
DR ExpressionAtlas; Q92993; baseline and differential.
DR Genevisible; Q92993; HS.
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: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 NuA4 histone acetyltransferase complex; IDA:UniProtKB.
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:0043998; F:H2A histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043999; F:histone acetyltransferase activity (H2A-K5 specific); IDA:UniProtKB.
DR GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
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:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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: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:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:ComplexPortal.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:ComplexPortal.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1905691; P:lipid droplet disassembly; IDA:UniProtKB.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA: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:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR GO; GO:1900051; P:positive regulation of histone exchange; ISS:UniProtKB.
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:0045893; P:positive regulation of transcription, DNA-templated; 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; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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:0007286; P:spermatid development; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 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; IPR037995; KAT5/Tip60.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615:SF183; PTHR10615:SF183; 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; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
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.66"
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.66"
FT BINDING 377..383
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|Ref.66"
FT BINDING 407
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|Ref.66"
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.66"
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)"
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)"
FT /evidence="ECO:0000269|PubMed:32822602"
FT /id="VAR_085193"
FT VARIANT 413
FT /note="S -> A (in NEDFASB; decreased histone
FT acetyltransferase activity)"
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
