ID KAT5_HUMAN Reviewed; 513 AA. AC Q92993; B4E3C7; C9JL99; O95624; Q13430; Q17RW5; Q561W3; Q6GSE8; AC Q9BWK7; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2003, sequence version 2. DT 31-JAN-2018, entry version 191. DE RecName: Full=Histone acetyltransferase KAT5; DE EC=2.3.1.48 {ECO:0000269|PubMed:10096020, ECO:0000269|PubMed:12468530, ECO:0000269|PubMed:29040603}; DE AltName: Full=60 kDa Tat-interactive protein; 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; DE AltName: Full=Lysine acetyltransferase 5; DE AltName: Full=cPLA(2)-interacting protein; GN Name=KAT5; Synonyms=HTATIP, TIP60; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT the 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., RA Taheri M.R., Bonventre J.V.; RT "PLIP, a novel splice variant of Tip60, interacts with group IV RT cytosolic phospholipase A(2), induces apoptosis, and potentiates RT prostaglandin 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 RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT TRRAP/TIP60-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., RA Horikoshi M., 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. 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. 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 RT 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 RP THE 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., RA Bernards R.; RT "A large-scale RNAi screen in human cells identifies new components of RT the 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 RT genotoxic 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 RT its 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, 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 RT histone deacetylases are required for repression."; RL Proc. Natl. Acad. Sci. U.S.A. 104:4571-4576(2007). RN [28] 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., RA 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 [29] 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., RA Shinohara N., Nonomura K., Hatakeyama S.; RT "TRIM68 regulates ligand-dependent transcription of androgen receptor RT in prostate cancer cells."; RL Cancer Res. 68:3486-3494(2008). RN [30] 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 [31] RP SUMOYLATION AT LYS-430 AND LYS-451, MUTAGENESIS OF LYS-430 AND RP LYS-451, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, RP AND 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., RA Liang S., 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 [32] 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 [33] 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., RA Tanaka J., Imamura M., Hatakeyama S.; RT "TRIM24 mediates ligand-dependent activation of androgen receptor and RT is repressed by a bromodomain-containing protein, BRD7, in prostate RT cancer cells."; RL Biochim. Biophys. Acta 1793:1828-1836(2009). RN [34] 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 [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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 [36] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-90 AND SER-199, RP AND 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 [37] 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 RT stress."; RL Nucleic Acids Res. 42:11447-11461(2014). RN [38] 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., RA Marek M., Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., RA Romier C., Hamiche A.; RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin."; RL Nature 505:648-653(2014). RN [39] 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 RT chromosome segregation."; RL J. Mol. Cell Biol. 0:0-0(2017). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 227-506 IN COMPLEX WITH RP ACETYL-COA 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 [41] 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 RT cDNA."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Catalytic subunit of the NuA4 histone acetyltransferase CC complex which is involved in transcriptional activation of select CC genes principally by acetylation of nucleosomal histones H4 and CC H2A. This modification may both alter nucleosome-DNA interactions CC and promote interaction of the modified histones with other CC proteins which positively regulate transcription. This complex may CC be required for the activation of transcriptional programs CC associated with oncogene and proto-oncogene mediated growth CC induction, tumor suppressor mediated growth arrest and replicative CC senescence, apoptosis, and DNA repair. NuA4 may also play a direct CC role in DNA repair when recruited to sites of DNA damage. Directly CC acetylates and activates ATM. Component of a SWR1-like complex CC that specifically mediates the removal of histone H2A.Z/H2AFZ from CC the nucleosome. Relieves NR1D2-mediated inhibition of APOC3 CC expression by acetylating NR1D2. Promotes FOXP3 acetylation and CC positively regulates its transcriptional repressor activity CC (PubMed:17360565). Acetylates RAN at 'Lys-134' (PubMed:29040603). 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:17996965, ECO:0000269|PubMed:19909775, CC ECO:0000269|PubMed:24463511, ECO:0000303|PubMed:15196461}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA + CC [protein]-N(6)-acetyl-L-lysine. {ECO:0000269|PubMed:10096020, CC ECO:0000269|PubMed:12468530, ECO:0000269|PubMed:29040603}. CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex CC which contains the catalytic subunit KAT5/TIP60 and the subunits CC EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, CC RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, CC MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6 (PubMed:12963728, CC PubMed:10966108, PubMed:15196461, PubMed:14966270). HTATTIP/TIP60, CC EPC1, and ING3 together constitute a minimal HAT complex termed CC Piccolo NuA4. The NuA4 complex interacts with MYC. 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 CC tail of APP and APBB1/FE65 (By similarity). Interacts with TRIM24 CC and TRIM68 (PubMed:18451177, PubMed:19909775). Forms a complex CC with SENP6 and UBE2I in response to UV irradiation. Identified in CC a complex with HINT1 (PubMed:16835243). Interacts with ATF2 and CC CUL3 (PubMed:18397884). Interacts with NR1D2 (via N-terminus) CC (PubMed:17996965). Component of a SWR1-like complex CC (PubMed:24463511). Interacts with FOXP3 (PubMed:17360565). CC Interacts with ZBTB49 (PubMed:25245946). CC {ECO:0000250|UniProtKB:Q99MK2, ECO:0000269|PubMed:10966108, CC ECO:0000269|PubMed:11262386, ECO:0000269|PubMed:11416127, CC ECO:0000269|PubMed:12551922, 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:24463511, ECO:0000269|PubMed:25245946, CC ECO:0000269|Ref.40, 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 P54253:ATXN1; NbExp=3; IntAct=EBI-399080, EBI-930964; CC Q96GD4:AURKB; NbExp=4; IntAct=EBI-399080, EBI-624291; CC Q9HC52:CBX8; NbExp=2; IntAct=EBI-399080, EBI-712912; CC Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-399080, EBI-10171416; CC Q9P2H0:CEP126; NbExp=2; IntAct=EBI-399080, EBI-473176; CC O43261:DLEU1; NbExp=2; IntAct=EBI-399080, EBI-710057; CC P03372-1:ESR1; NbExp=3; IntAct=EBI-399080, EBI-15606245; CC Q01844:EWSR1; NbExp=2; IntAct=EBI-399080, EBI-739737; CC Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-399080, EBI-10172181; CC Q9BZS1-1:FOXP3; NbExp=2; IntAct=EBI-399080, EBI-9695448; CC P35637:FUS; NbExp=2; IntAct=EBI-399080, EBI-400434; CC O95257:GADD45G; NbExp=2; IntAct=EBI-399080, EBI-448202; CC Q5VSY0:GKAP1; NbExp=4; IntAct=EBI-399080, EBI-743722; CC Q96IK5:GMCL1; NbExp=4; IntAct=EBI-399080, EBI-2548508; CC Q8NEA9:GMCL1P1; NbExp=3; IntAct=EBI-399080, EBI-745707; CC Q08379:GOLGA2; NbExp=3; IntAct=EBI-399080, EBI-618309; CC Q6NT76:HMBOX1; NbExp=5; IntAct=EBI-399080, EBI-2549423; CC Q9UKT9:IKZF3; NbExp=5; IntAct=EBI-399080, EBI-747204; CC Q6A162:KRT40; NbExp=3; IntAct=EBI-399080, EBI-10171697; CC P60411:KRTAP10-9; NbExp=3; IntAct=EBI-399080, EBI-10172052; CC Q17RB8:LONRF1; NbExp=3; IntAct=EBI-399080, EBI-2341787; CC Q9BRK4:LZTS2; NbExp=5; IntAct=EBI-399080, EBI-741037; CC Q99750:MDFI; NbExp=3; IntAct=EBI-399080, EBI-724076; CC P50222:MEOX2; NbExp=3; IntAct=EBI-399080, EBI-748397; CC Q5JR59:MTUS2; NbExp=3; IntAct=EBI-399080, EBI-742948; CC P10085:Myod1 (xeno); NbExp=5; IntAct=EBI-399080, EBI-4405734; CC Q9Y2I6:NINL; NbExp=3; IntAct=EBI-399080, EBI-719716; CC Q9HC29:NOD2; NbExp=2; IntAct=EBI-399080, EBI-7445625; CC P11926:ODC1; NbExp=7; IntAct=EBI-399080, EBI-1044287; CC Q8IXK0:PHC2; NbExp=3; IntAct=EBI-399080, EBI-713786; CC Q9NQM4:PIH1D3; NbExp=5; IntAct=EBI-399080, EBI-10239299; CC P29074:PTPN4; NbExp=2; IntAct=EBI-399080, EBI-710431; CC Q9Y265:RUVBL1; NbExp=5; IntAct=EBI-399080, EBI-353675; CC P35711:SOX5; NbExp=3; IntAct=EBI-399080, EBI-3505701; CC Q01130:SRSF2; NbExp=3; IntAct=EBI-399080, EBI-627047; CC Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-399080, EBI-2212028; CC O75558:STX11; NbExp=7; IntAct=EBI-399080, EBI-714135; CC Q92804:TAF15; NbExp=2; IntAct=EBI-399080, EBI-2255091; CC O75069-4:TMCC2; NbExp=3; IntAct=EBI-399080, EBI-10177480; CC P04637:TP53; NbExp=3; IntAct=EBI-399080, EBI-366083; CC P36406:TRIM23; NbExp=3; IntAct=EBI-399080, EBI-740098; CC P14373:TRIM27; NbExp=3; IntAct=EBI-399080, EBI-719493; CC O94972:TRIM37; NbExp=3; IntAct=EBI-399080, EBI-741602; CC Q9NNX1:TUFT1; NbExp=3; IntAct=EBI-399080, EBI-2557363; CC Q15672:TWIST1; NbExp=2; IntAct=EBI-399080, EBI-1797287; CC O43829:ZBTB14; NbExp=3; IntAct=EBI-399080, EBI-10176632; CC Q96BR9:ZBTB8A; NbExp=4; IntAct=EBI-399080, EBI-742740; CC Q8N8E2:ZNF513; NbExp=3; IntAct=EBI-399080, EBI-10279993; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17360565}. CC Nucleus, nucleolus. Cytoplasm, perinuclear region. Note=Upon CC stimulation with EDN1, it is exported from the nucleus to the CC perinuclear region and UV irradiation induces translocation into CC punctuate subnuclear structures named nuclear bodies. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=2; CC IsoId=Q92993-1; Sequence=Displayed; CC Name=1; Synonyms=PLIP; CC IsoId=Q92993-2; Sequence=VSP_007438; CC Name=3; CC IsoId=Q92993-3; Sequence=VSP_009104; CC Note=Ref.3 (no nucleotide entry) sequence is in conflict in CC position: 32:V->A. {ECO:0000305}; CC Name=4; CC IsoId=Q92993-4; Sequence=VSP_009104, VSP_007438; CC Note=No experimental confirmation available.; CC -!- PTM: (Microbial infection) In case of HIV-1 infection, interaction CC with the viral Tat protein leads to KAT5 polyubiquitination and CC targets it to degradation. {ECO:0000269|PubMed:16001085}. CC -!- PTM: Sumoylated by UBE2I at Lys-430 and Lys-451, leading to CC increase of its histone acetyltransferase activity in UV-induced CC DNA damage response, as well as its translocation to nuclear CC bodies. {ECO:0000269|PubMed:17704809}. CC -!- PTM: Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M CC phase. The phosphorylated form has a higher HAT activity. CC {ECO:0000269|PubMed:12468530}. CC -!- PTM: Ubiquitinated by MDM2, leading to its proteasome-dependent CC degradation. {ECO:0000269|PubMed:11927554}. CC -!- PTM: Autoacetylation at Lys-327 is required for proper function. CC {ECO:0000250|UniProtKB:Q9H7Z6}. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB02683.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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 CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/HTATIPID40893ch11q13.html"; 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 UniGene; Hs.397010; -. 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 ProteinModelPortal; Q92993; -. DR SMR; Q92993; -. DR BioGrid; 115779; 228. DR CORUM; Q92993; -. DR DIP; DIP-5998N; -. DR IntAct; Q92993; 148. DR MINT; MINT-94861; -. 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 EPD; Q92993; -. DR MaxQB; Q92993; -. DR PaxDb; Q92993; -. DR PeptideAtlas; Q92993; -. DR PRIDE; Q92993; -. DR DNASU; 10524; -. DR Ensembl; ENST00000341318; ENSP00000340330; ENSG00000172977. [Q92993-3] DR Ensembl; ENST00000352980; ENSP00000344955; ENSG00000172977. [Q92993-2] DR Ensembl; ENST00000377046; ENSP00000366245; ENSG00000172977. [Q92993-1] DR Ensembl; ENST00000530446; ENSP00000434765; ENSG00000172977. [Q92993-4] DR GeneID; 10524; -. DR KEGG; hsa:10524; -. DR UCSC; uc001ofi.4; human. [Q92993-1] DR CTD; 10524; -. DR DisGeNET; 10524; -. DR EuPathDB; HostDB:ENSG00000172977.12; -. DR GeneCards; KAT5; -. DR HGNC; HGNC:5275; KAT5. DR HPA; HPA016953; -. DR MIM; 601409; gene. DR neXtProt; NX_Q92993; -. DR OpenTargets; ENSG00000172977; -. DR PharmGKB; PA162392746; -. DR eggNOG; KOG2747; Eukaryota. DR eggNOG; COG5027; LUCA. DR GeneTree; ENSGT00550000074503; -. DR HOGENOM; HOG000182457; -. DR InParanoid; Q92993; -. DR KO; K11304; -. DR OMA; ITHADVM; -. DR OrthoDB; EOG091G0B73; -. DR PhylomeDB; Q92993; -. DR TreeFam; TF317619; -. 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 SignaLink; Q92993; -. DR SIGNOR; Q92993; -. DR ChiTaRS; KAT5; human. DR EvolutionaryTrace; Q92993; -. DR GeneWiki; KAT5; -. DR GenomeRNAi; 10524; -. DR PRO; PR:Q92993; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000172977; -. DR CleanEx; HS_KAT5; -. DR ExpressionAtlas; Q92993; baseline and differential. DR Genevisible; Q92993; HS. 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: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 factor complex; IEA:Ensembl. DR GO; GO:0016407; F:acetyltransferase activity; TAS:Reactome. DR GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB. DR GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome. DR GO; GO:0071392; P:cellular response to estradiol stimulus; 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:0000729; P:DNA double-strand break processing; TAS:Reactome. DR GO; GO:0006260; P:DNA replication; TAS:Reactome. DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome. DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome. DR GO; GO:0016573; P:histone acetylation; 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 from RNA polymerase II promoter; IMP:BHF-UCL. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL. DR GO; GO:1901985; P:positive regulation of protein acetylation; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW. DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome. DR GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB. DR GO; GO:0000732; P:strand displacement; TAS:Reactome. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR CDD; cd00024; CHROMO; 1. 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 Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF11717; Tudor-knot; 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; Chromatin regulator; Complete proteome; KW Cytoplasm; Direct protein sequencing; Growth regulation; KW Host-virus interaction; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Polymorphism; Reference proteome; Transcription; KW Transcription regulation; Transferase; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1 513 Histone acetyltransferase KAT5. FT /FTId=PRO_0000051580. FT DOMAIN 227 504 MYST-type HAT. {ECO:0000255|PROSITE- FT ProRule:PRU01063}. FT ZN_FING 260 285 C2HC MYST-type. {ECO:0000255|PROSITE- FT ProRule:PRU01063, ECO:0000305|Ref.40}. FT REGION 368 513 Interaction with ATF2. FT {ECO:0000269|PubMed:18397884}. FT REGION 370 372 Acetyl-CoA binding. {ECO:0000269|Ref.40}. FT REGION 377 383 Acetyl-CoA binding. {ECO:0000269|Ref.40}. FT ACT_SITE 403 403 Proton donor/acceptor. FT {ECO:0000250|UniProtKB:Q9H7Z6}. FT BINDING 407 407 Acetyl-CoA. {ECO:0000269|Ref.40}. FT BINDING 416 416 Acetyl-CoA. FT {ECO:0000250|UniProtKB:Q9H7Z6}. FT MOD_RES 52 52 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 86 86 Phosphoserine. FT {ECO:0000244|PubMed:23186163, FT ECO:0000269|PubMed:12468530}. FT MOD_RES 90 90 Phosphoserine; by CDK1. FT {ECO:0000244|PubMed:23186163, FT ECO:0000269|PubMed:12468530}. FT MOD_RES 199 199 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 327 327 N6-acetyllysine; by autocatalysis. FT {ECO:0000269|Ref.40}. FT CROSSLNK 430 430 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT {ECO:0000269|PubMed:17704809}. FT CROSSLNK 451 451 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT {ECO:0000269|PubMed:17704809}. FT VAR_SEQ 4 4 V -> VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ FT (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:12801643, FT ECO:0000303|PubMed:14702039}. FT /FTId=VSP_009104. FT VAR_SEQ 96 147 Missing (in isoform 1 and isoform 4). FT {ECO:0000303|PubMed:11416127, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_007438. FT VARIANT 78 78 P -> T (in dbSNP:rs11541271). FT /FTId=VAR_059456. FT MUTAGEN 86 86 S->A: Reduces phosphorylation. Abolishes FT phosphorylation; when associated with A- FT 90. Reduced HAT activity. FT {ECO:0000269|PubMed:12468530}. FT MUTAGEN 90 90 S->A: Reduces phosphorylation. Abolishes FT phosphorylation; when associated with A- FT 86. Reduced HAT activity. FT {ECO:0000269|PubMed:12468530}. FT MUTAGEN 254 254 L->A: Does not affect phosphorylation; FT when associated with A-257. FT {ECO:0000269|PubMed:12468530}. FT MUTAGEN 257 257 L->A: Does not affect phosphorylation; FT when associated with A-254. FT {ECO:0000269|PubMed:12468530}. FT MUTAGEN 380 380 G->A: Loss of function. Does not affect FT phosphorylation. FT {ECO:0000269|PubMed:12468530}. FT MUTAGEN 430 430 K->R: Abrogates sumoylation. FT {ECO:0000269|PubMed:17704809}. FT MUTAGEN 451 451 K->R: Abrogates sumoylation. FT {ECO:0000269|PubMed:17704809}. FT CONFLICT 382 382 G -> R (in Ref. 1; AAB18236/AAB02683). FT {ECO:0000305}. FT HELIX 4 6 {ECO:0000244|PDB:4QQG}. FT STRAND 12 15 {ECO:0000244|PDB:4QQG}. FT STRAND 28 35 {ECO:0000244|PDB:4QQG}. FT STRAND 37 40 {ECO:0000244|PDB:4QQG}. FT STRAND 42 47 {ECO:0000244|PDB:4QQG}. FT HELIX 52 54 {ECO:0000244|PDB:4QQG}. FT STRAND 56 58 {ECO:0000244|PDB:4QQG}. FT HELIX 60 62 {ECO:0000244|PDB:4QQG}. FT HELIX 65 67 {ECO:0000244|PDB:2EKO}. FT STRAND 235 237 {ECO:0000244|PDB:2OU2}. FT STRAND 240 242 {ECO:0000244|PDB:2OU2}. FT HELIX 252 254 {ECO:0000244|PDB:2OU2}. FT STRAND 260 262 {ECO:0000244|PDB:2OU2}. FT TURN 264 266 {ECO:0000244|PDB:2OU2}. FT STRAND 269 271 {ECO:0000244|PDB:2OU2}. FT HELIX 273 282 {ECO:0000244|PDB:2OU2}. FT STRAND 289 296 {ECO:0000244|PDB:2OU2}. FT STRAND 299 305 {ECO:0000244|PDB:2OU2}. FT TURN 306 308 {ECO:0000244|PDB:2OU2}. FT HELIX 310 321 {ECO:0000244|PDB:2OU2}. FT STRAND 336 345 {ECO:0000244|PDB:2OU2}. FT STRAND 348 360 {ECO:0000244|PDB:2OU2}. FT STRAND 365 368 {ECO:0000244|PDB:2OU2}. FT STRAND 370 372 {ECO:0000244|PDB:2OU2}. FT HELIX 374 376 {ECO:0000244|PDB:2OU2}. FT HELIX 381 395 {ECO:0000244|PDB:2OU2}. FT STRAND 400 402 {ECO:0000244|PDB:2OU2}. FT HELIX 408 425 {ECO:0000244|PDB:2OU2}. FT HELIX 441 448 {ECO:0000244|PDB:2OU2}. FT HELIX 452 461 {ECO:0000244|PDB:2OU2}. FT STRAND 469 474 {ECO:0000244|PDB:2OU2}. FT HELIX 497 499 {ECO:0000244|PDB:2OU2}. 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 //