ID KAT7_HUMAN Reviewed; 611 AA. AC O95251; B3KN74; B4DF85; B4DFB4; B4DFE0; B4DGY4; E7ER15; G5E9K7; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=Histone acetyltransferase KAT7 {ECO:0000305}; DE EC=2.3.1.48 {ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:17954561, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:26620551, ECO:0000269|PubMed:31827282}; DE AltName: Full=Histone acetyltransferase binding to ORC1 {ECO:0000303|PubMed:10438470, ECO:0000303|PubMed:10930412}; DE AltName: Full=Lysine acetyltransferase 7 {ECO:0000303|PubMed:31767635}; DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2 {ECO:0000303|Ref.4}; DE Short=MYST-2 {ECO:0000303|Ref.4}; GN Name=KAT7 {ECO:0000303|PubMed:31767635, ECO:0000312|HGNC:HGNC:17016}; GN Synonyms=HBO1 {ECO:0000303|PubMed:10438470, GN ECO:0000303|PubMed:10930412}, HBOa {ECO:0000303|Ref.3}, MYST2 GN {ECO:0000303|Ref.4}; 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 1), INTERACTION WITH ORC1, FUNCTION, RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RC TISSUE=Epithelium; RX PubMed=10438470; DOI=10.1074/jbc.274.33.23027; RA Iizuka M., Stillman B.; RT "Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the RT human initiator protein."; RL J. Biol. Chem. 274:23027-23034(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR RP LOCATION, AND INTERACTION WITH AR. RC TISSUE=Prostate; RX PubMed=10930412; DOI=10.1074/jbc.m004838200; RA Sharma M., Zarnegar M., Li X., Lim B., Sun Z.; RT "Androgen receptor interacts with a novel MYST protein, HBO1."; RL J. Biol. Chem. 275:35200-35208(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Jian J., Guangtao L., Guangwei D., Yan Z., Jianhe C., Jiangang Y., RA Boqin Q.; RT "Cloning and identifying histone acetyltransferase HBOa."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Borrow J., Housman D.E.; RT "Structure and function of the human MYST family: MOZ2, MYST1 and MYST2."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5). RC TISSUE=Brain, Cerebellum, and Thyroid; 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=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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 INTERACTION WITH MCM2 AND ORC1, DOMAIN, SUBCELLULAR LOCATION, FUNCTION, AND RP MUTAGENESIS OF CYS-371. RX PubMed=11278932; DOI=10.1074/jbc.m011556200; RA Burke T.W., Cook J.G., Asano M., Nevins J.R.; RT "Replication factors MCM2 and ORC1 interact with the histone RT acetyltransferase HBO1."; RL J. Biol. Chem. 276:15397-15408(2001). RN [10] RP FUNCTION. RX PubMed=16997280; DOI=10.1016/j.bbrc.2006.09.030; RA Contzler R., Regamey A., Favre B., Roger T., Hohl D., Huber M.; RT "Histone acetyltransferase HBO1 inhibits NF-kappaB activity by coactivator RT sequestration."; RL Biochem. Biophys. Res. Commun. 350:208-213(2006). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [12] RP FUNCTION IN HISTONE ACETYLATION, IDENTIFICATION IN THE HBO1 COMPLEX, RP INTERACTION WITH MCM2, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [15] RP INTERACTION WITH CDT1, AND SUBCELLULAR LOCATION. RX PubMed=18832067; DOI=10.1101/gad.1674108; RA Miotto B., Struhl K.; RT "HBO1 histone acetylase is a coactivator of the replication licensing RT factor Cdt1."; RL Genes Dev. 22:2633-2638(2008). RN [16] RP CATALYTIC ACTIVITY, INTERACTION WITH TP53, AND MUTAGENESIS OF GLY-485. RX PubMed=17954561; DOI=10.1128/mcb.00662-07; RA Iizuka M., Sarmento O.F., Sekiya T., Scrable H., Allis C.D., Smith M.M.; RT "Hbo1 Links p53-dependent stress signaling to DNA replication licensing."; RL Mol. Cell. Biol. 28:140-153(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57; THR-85; THR-88 RP AND SER-102, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [18] RP PHOSPHORYLATION AT SER-57 BY PLK1, PHOSPHORYLATION AT THR-85 AND THR-88 BY RP CDK1, AND MUTAGENESIS OF SER-57. RX PubMed=18250300; DOI=10.1073/pnas.0712063105; RA Wu Z.Q., Liu X.; RT "Role for Plk1 phosphorylation of Hbo1 in regulation of replication RT licensing."; RL Proc. Natl. Acad. Sci. U.S.A. 105:1919-1924(2008). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] RP FUNCTION, IDENTIFICATION IN THE HBO1 COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=19187766; DOI=10.1016/j.molcel.2009.01.007; RA Saksouk N., Avvakumov N., Champagne K.S., Hung T., Doyon Y., Cayrou C., RA Paquet E., Ullah M., Landry A.J., Cote V., Yang X.J., Gozani O., RA Kutateladze T.G., Cote J.; RT "HBO1 HAT complexes target chromatin throughout gene coding regions via RT multiple PHD finger interactions with histone H3 tail."; RL Mol. Cell 33:257-265(2009). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-85; THR-88 AND RP SER-102, AND 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 [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, 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 [23] RP FUNCTION, ACTIVITY REGULATION, IDENTIFICATION IN THE HBO1 COMPLEX, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-485. RX PubMed=20129055; DOI=10.1016/j.molcel.2009.12.012; RA Miotto B., Struhl K.; RT "HBO1 histone acetylase activity is essential for DNA replication licensing RT and inhibited by Geminin."; RL Mol. Cell 37:57-66(2010). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-506, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [25] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE HBO1 COMPLEX. RX PubMed=21753189; DOI=10.1182/blood-2011-01-331892; RA Mishima Y., Miyagi S., Saraya A., Negishi M., Endoh M., Endo T.A., RA Toyoda T., Shinga J., Katsumoto T., Chiba T., Yamaguchi N., Kitabayashi I., RA Koseki H., Iwama A.; RT "The Hbo1-Brd1/Brpf2 complex is responsible for global acetylation of H3K14 RT and required for fetal liver erythropoiesis."; RL Blood 118:2443-2453(2011). RN [26] RP FUNCTION. RX PubMed=21856198; DOI=10.1016/j.molcel.2011.06.021; RA Miotto B., Struhl K.; RT "JNK1 phosphorylation of Cdt1 inhibits recruitment of HBO1 histone RT acetylase and blocks replication licensing in response to stress."; RL Mol. Cell 44:62-71(2011). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-88; SER-102; SER-124; RP SER-162 AND SER-164, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [28] RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE HBO1 COMPLEX, AND RP SUBCELLULAR LOCATION. RX PubMed=24065767; DOI=10.1101/gad.223396.113; RA Lalonde M.E., Avvakumov N., Glass K.C., Joncas F.H., Saksouk N., RA Holliday M., Paquet E., Yan K., Tong Q., Klein B.J., Tan S., Yang X.J., RA Kutateladze T.G., Cote J.; RT "Exchange of associated factors directs a switch in HBO1 acetyltransferase RT histone tail specificity."; RL Genes Dev. 27:2009-2024(2013). RN [29] RP MUTAGENESIS OF LYS-338, AND UBIQUITINATION AT LYS-338. RX PubMed=23319590; DOI=10.1074/jbc.m112.426882; RA Zou C., Chen Y., Smith R.M., Snavely C., Li J., Coon T.A., Chen B.B., RA Zhao Y., Mallampalli R.K.; RT "SCF(Fbxw15) mediates histone acetyltransferase binding to origin RT recognition complex (HBO1) ubiquitin-proteasomal degradation to regulate RT cell proliferation."; RL J. Biol. Chem. 288:6306-6316(2013). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-50; SER-57; SER-64; RP SER-102; SER-111; SER-162; SER-164; SER-178 AND SER-506, AND IDENTIFICATION RP 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 [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [32] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MIS18BP1. RX PubMed=27270040; DOI=10.1016/j.devcel.2016.05.006; RA Ohzeki J., Shono N., Otake K., Martins N.M., Kugou K., Kimura H., RA Nagase T., Larionov V., Earnshaw W.C., Masumoto H.; RT "KAT7/HBO1/MYST2 regulates CENP-A chromatin assembly by antagonizing RT Suv39h1-mediated centromere inactivation."; RL Dev. Cell 37:413-427(2016). RN [33] RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE HBO1 COMPLEX. RX PubMed=26620551; DOI=10.15252/embj.201591293; RA Feng Y., Vlassis A., Roques C., Lalonde M.E., Gonzalez-Aguilera C., RA Lambert J.P., Lee S.B., Zhao X., Alabert C., Johansen J.V., Paquet E., RA Yang X.J., Gingras A.C., Cote J., Groth A.; RT "BRPF3-HBO1 regulates replication origin activation and histone H3K14 RT acetylation."; RL EMBO J. 35:176-192(2016). RN [34] RP PHOSPHORYLATION AT SER-50 AND SER-53, UBIQUITINATION, AND MUTAGENESIS OF RP 50-SER--SER-53. RX PubMed=26572825; DOI=10.1128/mcb.00809-15; RA Matsunuma R., Niida H., Ohhata T., Kitagawa K., Sakai S., Uchida C., RA Shiotani B., Matsumoto M., Nakayama K.I., Ogura H., Shiiya N., Kitagawa M.; RT "UV damage-induced phosphorylation of HBO1 triggers CRL4DDB2-mediated RT degradation to regulate cell proliferation."; RL Mol. Cell. Biol. 36:394-406(2016). RN [35] RP FUNCTION, PHOSPHORYLATION AT SER-50 AND SER-53, AND SUBCELLULAR LOCATION. RX PubMed=28719581; DOI=10.1038/ncomms16102; RA Niida H., Matsunuma R., Horiguchi R., Uchida C., Nakazawa Y., Motegi A., RA Nishimoto K., Sakai S., Ohhata T., Kitagawa K., Moriwaki S., Nishitani H., RA Ui A., Ogi T., Kitagawa M.; RT "Phosphorylated HBO1 at UV irradiated sites is essential for nucleotide RT excision repair."; RL Nat. Commun. 8:16102-16102(2017). RN [36] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-323, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [37] RP INTERACTION WITH JADE1. RX PubMed=29382722; DOI=10.1074/jbc.ra117.000677; RA Han J., Lachance C., Ricketts M.D., McCullough C.E., Gerace M., Black B.E., RA Cote J., Marmorstein R.; RT "The scaffolding protein JADE1 physically links the acetyltransferase RT subunit HBO1 with its histone H3-H4 substrate."; RL J. Biol. Chem. 293:4498-4509(2018). RN [38] RP FUNCTION. RX PubMed=31767635; DOI=10.1128/mcb.00506-19; RA Kueh A.J., Eccles S., Tang L., Garnham A.L., May R.E., Herold M.J., RA Smyth G.K., Voss A.K., Thomas T.; RT "HBO1(KAT7) does not have an essential role in cell proliferation, DNA RT replication or histone 4 acetylation in human cells."; RL Mol. Cell. Biol. 0:0-0(2019). RN [39] {ECO:0007744|PDB:5GK9} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 336-611 IN COMPLEX WITH BRD1; RP ZINC AND ACETYL-COA. RX PubMed=28334966; DOI=10.1093/nar/gkx142; RA Tao Y., Zhong C., Zhu J., Xu S., Ding J.; RT "Structural and mechanistic insights into regulation of HBO1 histone RT acetyltransferase activity by BRPF2."; RL Nucleic Acids Res. 45:5707-5719(2017). RN [40] {ECO:0007744|PDB:6MAJ, ECO:0007744|PDB:6MAK} RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 336-609 IN COMPLEX WITH BRD1; RP ZINC; WM-3835 INHIBITOR AND ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, RP ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-508. RX PubMed=31827282; DOI=10.1038/s41586-019-1835-6; RA MacPherson L., Anokye J., Yeung M.M., Lam E.Y.N., Chan Y.C., Weng C.F., RA Yeh P., Knezevic K., Butler M.S., Hoegl A., Chan K.L., Burr M.L., RA Gearing L.J., Willson T., Liu J., Choi J., Yang Y., Bilardi R.A., Falk H., RA Nguyen N., Stupple P.A., Peat T.S., Zhang M., de Silva M., RA Carrasco-Pozo C., Avery V.M., Khoo P.S., Dolezal O., Dennis M.L., RA Nuttall S., Surjadi R., Newman J., Ren B., Leaver D.J., Sun Y., Baell J.B., RA Dovey O., Vassiliou G.S., Grebien F., Dawson S.J., Street I.P., RA Monahan B.J., Burns C.J., Choudhary C., Blewitt M.E., Voss A.K., Thomas T., RA Dawson M.A.; RT "HBO1 is required for the maintenance of leukaemia stem cells."; RL Nature 577:266-270(2020). CC -!- FUNCTION: Catalytic subunit of histone acetyltransferase HBO1 CC complexes, which specifically mediate acetylation of histone H3 at CC 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene CC transcription, protein ubiquitination, immune regulation, stem cell CC pluripotent and self-renewal maintenance and embryonic development CC (PubMed:16387653, PubMed:21753189, PubMed:24065767, PubMed:26620551, CC PubMed:31767635, PubMed:31827282). Some complexes also catalyze CC acetylation of histone H4 at 'Lys-5', 'Lys-8' and 'Lys-12' (H4K5ac, CC H4K8ac and H4K12ac, respectively), regulating DNA replication CC initiation, regulating DNA replication initiation (PubMed:10438470, CC PubMed:19187766, PubMed:20129055, PubMed:24065767). Specificity of the CC HBO1 complexes is determined by the scaffold subunit: complexes CC containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 CC specificity towards H3K14ac, while complexes containing JADE (JADE1, CC JADE2 and JADE3) scaffold direct KAT7/HBO1 specificity towards histone CC H4 (PubMed:19187766, PubMed:20129055, PubMed:24065767, CC PubMed:26620551). H3K14ac promotes transcriptional elongation by CC facilitating the processivity of RNA polymerase II (PubMed:31827282). CC Acts as a key regulator of hematopoiesis by forming a complex with CC BRD1/BRPF2, directing KAT7/HBO1 specificity towards H3K14ac and CC promoting erythroid differentiation (PubMed:21753189). H3K14ac is also CC required for T-cell development (By similarity). KAT7/HBO1-mediated CC acetylation facilitates two consecutive steps, licensing and CC activation, in DNA replication initiation: H3K14ac facilitates the CC activation of replication origins, and histone H4 acetylation (H4K5ac, CC H4K8ac and H4K12ac) facilitates chromatin loading of MCM complexes, CC promoting DNA replication licensing (PubMed:10438470, PubMed:11278932, CC PubMed:18832067, PubMed:19187766, PubMed:20129055, PubMed:21856198, CC PubMed:24065767, PubMed:26620551). Acts as a positive regulator of CC centromeric CENPA assembly: recruited to centromeres and mediates CC histone acetylation, thereby preventing centromere inactivation CC mediated by SUV39H1, possibly by increasing histone turnover/exchange CC (PubMed:27270040). Involved in nucleotide excision repair: CC phosphorylation by ATR in response to ultraviolet irradiation promotes CC its localization to DNA damage sites, where it mediates histone CC acetylation to facilitate recruitment of XPC at the damaged DNA sites CC (PubMed:28719581). Acts as an inhibitor of NF-kappa-B independently of CC its histone acetyltransferase activity (PubMed:16997280). CC {ECO:0000250|UniProtKB:Q5SVQ0, ECO:0000269|PubMed:10438470, CC ECO:0000269|PubMed:11278932, ECO:0000269|PubMed:16387653, CC ECO:0000269|PubMed:16997280, ECO:0000269|PubMed:18832067, CC ECO:0000269|PubMed:19187766, ECO:0000269|PubMed:20129055, CC ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:21856198, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:26620551, CC ECO:0000269|PubMed:27270040, ECO:0000269|PubMed:28719581, CC ECO:0000269|PubMed:31767635, ECO:0000269|PubMed:31827282}. CC -!- FUNCTION: Plays a central role in the maintenance of leukemia stem CC cells in acute myeloid leukemia (AML) (PubMed:31827282). Acts by CC mediating acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby CC facilitating the processivity of RNA polymerase II to maintain the high CC expression of key genes, such as HOXA9 and HOXA10 that help to sustain CC the functional properties of leukemia stem cells (PubMed:31827282). CC {ECO:0000269|PubMed:31827282}. 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:10438470, ECO:0000269|PubMed:17954561, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:26620551, CC ECO:0000269|PubMed:31827282}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; CC Evidence={ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:17954561, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:26620551, CC ECO:0000269|PubMed:31827282}; CC -!- ACTIVITY REGULATION: Histone acetyltransferase activity is inhibited by CC GMNN in the context of a complex with CDT1, inhibiting histone H4 CC acetylation and DNA replication licensing (PubMed:20129055). CC Selectively inhibited by WM-3835 (N'-(4-fluoro-5-methyl-[1,1'- CC biphenyl]-3-carbonyl)-3- hydroxybenzenesulfonohydrazide) inhibitor CC (PubMed:31827282). {ECO:0000269|PubMed:20129055, CC ECO:0000269|PubMed:31827282}. CC -!- SUBUNIT: Component of the HBO1 complex composed of KAT7/HBO1, MEAF6, CC ING4 or ING5, and one scaffold subunit: complexes containing BRPF CC scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity CC towards H3K14ac, while complexes containing JADE scaffold (JADE1, JADE2 CC and JADE3) mediate acetylation of histone H4 (PubMed:16387653, CC PubMed:19187766, PubMed:20129055, PubMed:21753189, PubMed:24065767, CC PubMed:26620551, PubMed:29382722). Interacts with MCM2 and ORC1 CC (PubMed:10438470, PubMed:11278932, PubMed:16387653). Interacts with the CC androgen receptor (AR); in the presence of dihydrotestosterone CC (PubMed:10930412). Interacts with CDT1 (PubMed:18832067). Interacts CC with MAP2K1 and CUL1 (By similarity). Interacts with p53/TP53; leading CC to inhibit histone acetyltransferase activity (PubMed:17954561). CC Interacts with MIS18BP1 (PubMed:27270040). CC {ECO:0000250|UniProtKB:Q5SVQ0, ECO:0000269|PubMed:10438470, CC ECO:0000269|PubMed:10930412, ECO:0000269|PubMed:11278932, CC ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:17954561, CC ECO:0000269|PubMed:18832067, ECO:0000269|PubMed:19187766, CC ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:21753189, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:26620551, CC ECO:0000269|PubMed:27270040, ECO:0000269|PubMed:29382722}. CC -!- INTERACTION: CC O95251; P10275: AR; NbExp=5; IntAct=EBI-473199, EBI-608057; CC O95251; Q99728: BARD1; NbExp=2; IntAct=EBI-473199, EBI-473181; CC O95251; Q9P2H0: CEP126; NbExp=2; IntAct=EBI-473199, EBI-473176; CC O95251; Q6IE81: JADE1; NbExp=2; IntAct=EBI-473199, EBI-954672; CC O95251; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-473199, EBI-348259; CC O95251; P53350: PLK1; NbExp=6; IntAct=EBI-473199, EBI-476768; CC O95251; P08670: VIM; NbExp=4; IntAct=EBI-473199, EBI-353844; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10930412, CC ECO:0000269|PubMed:11278932, ECO:0000269|PubMed:16387653, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:28719581}. Chromosome CC {ECO:0000269|PubMed:18832067, ECO:0000269|PubMed:19187766, CC ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:21753189, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:28719581}. Chromosome, CC centromere {ECO:0000269|PubMed:27270040}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q5SVQ0}. Note=Associates with replication CC origins specifically during the G1 phase of the cell cycle CC (PubMed:18832067, PubMed:20129055). Localizes to transcription start CC sites (PubMed:21753189, PubMed:24065767). Localizes to ultraviolet- CC induced DNA damage sites following phosphorylation by ATR CC (PubMed:28719581). Localizes to centromeres in G1 phase CC (PubMed:27270040). {ECO:0000269|PubMed:18832067, CC ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:21753189, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:27270040, CC ECO:0000269|PubMed:28719581}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=O95251-1; Sequence=Displayed; CC Name=2; CC IsoId=O95251-2; Sequence=VSP_042553, VSP_042554; CC Name=3; CC IsoId=O95251-3; Sequence=VSP_042552, VSP_042553, VSP_042554; CC Name=4; CC IsoId=O95251-4; Sequence=VSP_042554; CC Name=5; CC IsoId=O95251-5; Sequence=VSP_042552, VSP_042553; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in CC testis. {ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:10930412}. CC -!- DOMAIN: The C2HC MYST-type zinc finger is required for interaction with CC MCM2 and ORC1. {ECO:0000269|PubMed:11278932}. CC -!- DOMAIN: The N-terminus is involved in transcriptional repression, while CC the C-terminus mediates AR-interaction. {ECO:0000269|PubMed:10930412}. CC -!- PTM: Phosphorylated at Ser-50 and Ser-53 by ATR in response to DNA CC damage, promoting its ubiquitination by the CRL4(DDB2) complex and CC subsequent degradation (PubMed:26572825). Phosphorylation at Ser-50 and CC Ser-53 by ATR in response to ultraviolet-induced DNA, promotes CC localization to DNA damage sites (PubMed:28719581). Phosphorylation at CC Ser-57 by PLK1 during mitosis seems important for prereplicative CC complex formation and DNA replication licensing, and requires prior CC phosphorylation at Thr-85 and Thr-88 by CDK1 (PubMed:18250300). CC Phosphorylated by MAP2K1, which accelerates its degradation (By CC similarity). {ECO:0000250|UniProtKB:Q5SVQ0, CC ECO:0000269|PubMed:18250300, ECO:0000269|PubMed:26572825, CC ECO:0000269|PubMed:28719581}. CC -!- PTM: Ubiquitinated at Lys-338, leading to proteasomal degradation CC (PubMed:23319590). Ubiquitinated by the CRL4(DDB2) complex following CC phosphorylation by ATR, leading to its subsequent degradation CC (PubMed:26572825). {ECO:0000269|PubMed:23319590, CC ECO:0000269|PubMed:26572825}. CC -!- PTM: Autoacetylation at Lys-432 is required for proper function. CC {ECO:0000250|UniProtKB:Q9H7Z6}. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}. 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; AF074606; AAC99368.1; -; mRNA. DR EMBL; AF140360; AAD42348.1; -; mRNA. DR EMBL; AF217502; AAL56649.1; -; mRNA. DR EMBL; AK023890; BAG51236.1; -; mRNA. DR EMBL; AK293976; BAG57346.1; -; mRNA. DR EMBL; AK294014; BAG57375.1; -; mRNA. DR EMBL; AK294052; BAG57401.1; -; mRNA. DR EMBL; AK294836; BAG57945.1; -; mRNA. DR EMBL; AC015795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027801; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471109; EAW94658.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94659.1; -; Genomic_DNA. DR EMBL; BC032640; AAH32640.1; -; mRNA. DR CCDS; CCDS11554.1; -. [O95251-1] DR CCDS; CCDS56035.1; -. [O95251-4] DR CCDS; CCDS56036.1; -. [O95251-2] DR CCDS; CCDS56037.1; -. [O95251-5] DR CCDS; CCDS56038.1; -. [O95251-3] DR RefSeq; NP_001186084.1; NM_001199155.1. [O95251-4] DR RefSeq; NP_001186085.1; NM_001199156.1. [O95251-5] DR RefSeq; NP_001186086.1; NM_001199157.1. [O95251-2] DR RefSeq; NP_001186087.1; NM_001199158.1. [O95251-3] DR RefSeq; NP_008998.1; NM_007067.4. [O95251-1] DR PDB; 5GK9; X-ray; 2.40 A; A=336-611. DR PDB; 6MAJ; X-ray; 2.14 A; A=336-609. DR PDB; 6MAK; X-ray; 2.13 A; A=336-609. DR PDB; 7D0O; X-ray; 2.51 A; A=336-611. DR PDB; 7D0P; X-ray; 1.80 A; A=336-611. DR PDB; 7D0Q; X-ray; 2.21 A; A=336-611. DR PDB; 7D0R; X-ray; 1.95 A; A=336-611. DR PDB; 7D0S; X-ray; 2.30 A; A=336-611. DR PDBsum; 5GK9; -. DR PDBsum; 6MAJ; -. DR PDBsum; 6MAK; -. DR PDBsum; 7D0O; -. DR PDBsum; 7D0P; -. DR PDBsum; 7D0Q; -. DR PDBsum; 7D0R; -. DR PDBsum; 7D0S; -. DR AlphaFoldDB; O95251; -. DR SMR; O95251; -. DR BioGRID; 116315; 151. DR ComplexPortal; CPX-718; HBO1-4.1 histone acetyltransferase complex. DR ComplexPortal; CPX-719; HBO1-4.2 histone acetyltransferase complex. DR ComplexPortal; CPX-720; HBO1-4.3 histone acetyltransferase complex. DR ComplexPortal; CPX-721; HBO1-5.1 histone acetyltransferase complex. DR ComplexPortal; CPX-722; HBO1-5.2 histone acetyltransferase complex. DR ComplexPortal; CPX-723; HBO1-5.3 histone acetyltransferase complex. DR CORUM; O95251; -. DR DIP; DIP-29697N; -. DR IntAct; O95251; 71. DR MINT; O95251; -. DR STRING; 9606.ENSP00000259021; -. DR BindingDB; O95251; -. DR ChEMBL; CHEMBL3774299; -. DR GlyGen; O95251; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; O95251; -. DR MetOSite; O95251; -. DR PhosphoSitePlus; O95251; -. DR SwissPalm; O95251; -. DR BioMuta; KAT7; -. DR EPD; O95251; -. DR jPOST; O95251; -. DR MassIVE; O95251; -. DR MaxQB; O95251; -. DR PaxDb; 9606-ENSP00000259021; -. DR PeptideAtlas; O95251; -. DR ProteomicsDB; 17693; -. DR ProteomicsDB; 33968; -. DR ProteomicsDB; 50746; -. [O95251-1] DR ProteomicsDB; 50747; -. [O95251-2] DR ProteomicsDB; 50748; -. [O95251-3] DR Pumba; O95251; -. DR Antibodypedia; 17983; 438 antibodies from 39 providers. DR DNASU; 11143; -. DR Ensembl; ENST00000259021.9; ENSP00000259021.4; ENSG00000136504.15. [O95251-1] DR Ensembl; ENST00000424009.6; ENSP00000398961.2; ENSG00000136504.15. [O95251-4] DR Ensembl; ENST00000454930.6; ENSP00000413415.2; ENSG00000136504.15. [O95251-5] DR Ensembl; ENST00000509773.5; ENSP00000424577.1; ENSG00000136504.15. [O95251-2] DR Ensembl; ENST00000510819.5; ENSP00000423385.1; ENSG00000136504.15. [O95251-3] DR Ensembl; ENST00000706506.1; ENSP00000516419.1; ENSG00000136504.15. [O95251-4] DR GeneID; 11143; -. DR KEGG; hsa:11143; -. DR MANE-Select; ENST00000259021.9; ENSP00000259021.4; NM_007067.5; NP_008998.1. DR UCSC; uc002ipl.3; human. [O95251-1] DR AGR; HGNC:17016; -. DR CTD; 11143; -. DR DisGeNET; 11143; -. DR GeneCards; KAT7; -. DR HGNC; HGNC:17016; KAT7. DR HPA; ENSG00000136504; Low tissue specificity. DR MIM; 609880; gene. DR neXtProt; NX_O95251; -. DR OpenTargets; ENSG00000136504; -. DR PharmGKB; PA134886407; -. DR VEuPathDB; HostDB:ENSG00000136504; -. DR eggNOG; KOG2747; Eukaryota. DR GeneTree; ENSGT00940000157744; -. DR HOGENOM; CLU_011815_6_1_1; -. DR InParanoid; O95251; -. DR OMA; NSLXVRA; -. DR OrthoDB; 118560at2759; -. DR PhylomeDB; O95251; -. DR TreeFam; TF317619; -. DR BRENDA; 2.3.1.48; 2681. DR PathwayCommons; O95251; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR SignaLink; O95251; -. DR SIGNOR; O95251; -. DR BioGRID-ORCS; 11143; 168 hits in 1199 CRISPR screens. DR ChiTaRS; KAT7; human. DR GeneWiki; MYST2; -. DR GenomeRNAi; 11143; -. DR Pharos; O95251; Tbio. DR PRO; PR:O95251; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O95251; Protein. DR Bgee; ENSG00000136504; Expressed in sural nerve and 200 other cell types or tissues. DR ExpressionAtlas; O95251; baseline and differential. DR GO; GO:0005694; C:chromosome; IDA:UniProtKB. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0036409; C:histone H3-K14 acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB. DR GO; GO:0003688; F:DNA replication origin binding; IMP:CAFA. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0036408; F:histone H3K14 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043994; F:histone H3K23 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0044016; F:histone H3K4 acetyltransferase activity; IMP:GO_Central. DR GO; GO:0010485; F:histone H4 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043997; F:histone H4K12 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043995; F:histone H4K5 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043996; F:histone H4K8 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0140889; P:DNA replication-dependent chromatin disassembly; IDA:UniProtKB. DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB. DR GO; GO:0001779; P:natural killer cell differentiation; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB. DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISS:UniProtKB. DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IDA:UniProtKB. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0051726; P:regulation of cell cycle; IDA:ComplexPortal. DR GO; GO:0001558; P:regulation of cell growth; IDA:ComplexPortal. DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IDA:ComplexPortal. DR GO; GO:0006275; P:regulation of DNA replication; IDA:ComplexPortal. DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IDA:UniProtKB. DR GO; GO:0072716; P:response to actinomycin D; IMP:CAFA. DR GO; GO:0072739; P:response to anisomycin; IMP:CAFA. DR GO; GO:0072720; P:response to dithiothreitol; IMP:CAFA. DR GO; GO:0072710; P:response to hydroxyurea; IMP:CAFA. DR GO; GO:0072708; P:response to sorbitol; IMP:CAFA. DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IDA:CAFA. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IMP:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 4.10.320.30; -; 1. DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR002717; HAT_MYST-type. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR040706; Zf-MYST. DR InterPro; IPR002515; Znf_C2H2C. DR InterPro; IPR036060; Znf_C2H2C_sf. DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10615:SF210; HISTONE ACETYLTRANSFERASE KAT7; 1. DR Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF01530; zf-C2HC; 1. DR Pfam; PF17772; zf-MYST; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF103637; CCHHC domain; 1. DR PROSITE; PS51726; MYST_HAT; 1. DR PROSITE; PS51802; ZF_CCHHC; 1. DR Genevisible; O95251; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing; KW Centromere; Chromatin regulator; Chromosome; Cytoplasm; DNA damage; KW DNA repair; DNA replication; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..611 FT /note="Histone acetyltransferase KAT7" FT /id="PRO_0000051569" FT DOMAIN 332..607 FT /note="MYST-type HAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063" FT ZN_FING 176..219 FT /note="CCHHC-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143" FT ZN_FING 365..390 FT /note="C2HC MYST-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063" FT REGION 1..173 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..38 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 39..106 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 107..123 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 124..151 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 153..173 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 508 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000305|PubMed:31827282" FT BINDING 368 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:28334966, FT ECO:0000269|PubMed:31827282, ECO:0007744|PDB:5GK9, FT ECO:0007744|PDB:6MAJ, ECO:0007744|PDB:6MAK" FT BINDING 371 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:28334966, FT ECO:0000269|PubMed:31827282, ECO:0007744|PDB:5GK9, FT ECO:0007744|PDB:6MAJ, ECO:0007744|PDB:6MAK" FT BINDING 384 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:28334966, FT ECO:0000269|PubMed:31827282, ECO:0007744|PDB:5GK9, FT ECO:0007744|PDB:6MAJ, ECO:0007744|PDB:6MAK" FT BINDING 388 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:28334966, FT ECO:0000269|PubMed:31827282, ECO:0007744|PDB:5GK9, FT ECO:0007744|PDB:6MAJ, ECO:0007744|PDB:6MAK" FT BINDING 475..477 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:28334966, FT ECO:0000269|PubMed:31827282, ECO:0007744|PDB:5GK9, FT ECO:0007744|PDB:6MAK" FT BINDING 483..488 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:28334966, FT ECO:0000269|PubMed:31827282, ECO:0007744|PDB:5GK9, FT ECO:0007744|PDB:6MAK" FT BINDING 512 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:28334966, FT ECO:0000269|PubMed:31827282, ECO:0007744|PDB:5GK9, FT ECO:0007744|PDB:6MAK" FT BINDING 521 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:28334966, FT ECO:0000269|PubMed:31827282, ECO:0007744|PDB:5GK9, FT ECO:0007744|PDB:6MAK" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 50 FT /note="Phosphoserine; by ATR" FT /evidence="ECO:0000269|PubMed:26572825, FT ECO:0000269|PubMed:28719581, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 53 FT /note="Phosphoserine; by ATR" FT /evidence="ECO:0000269|PubMed:26572825, FT ECO:0000269|PubMed:28719581" FT MOD_RES 57 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000269|PubMed:18250300, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 85 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:18250300, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332" FT MOD_RES 88 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:18250300, FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 104 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5SVQ0" FT MOD_RES 111 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 124 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 128 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5SVQ0" FT MOD_RES 158 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 178 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 199 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 277 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q5SVQ0" FT MOD_RES 432 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" FT MOD_RES 506 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 323 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 338 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:23319590" FT VAR_SEQ 55..113 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042552" FT VAR_SEQ 114..193 FT /note="Missing (in isoform 2, isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042553" FT VAR_SEQ 222..251 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042554" FT MUTAGEN 50..53 FT /note="SQSS->AQSA: Impaired phosphorylation by ATR, leading FT to decreased ubiquitination and increased stability in FT response to DNA damage." FT /evidence="ECO:0000269|PubMed:26572825" FT MUTAGEN 57 FT /note="S->A: Leads to cell cycle arrest in the G1/S phase." FT /evidence="ECO:0000269|PubMed:18250300" FT MUTAGEN 338 FT /note="K->R: Decreases ubiquitination." FT /evidence="ECO:0000269|PubMed:23319590" FT MUTAGEN 371 FT /note="C->A: No interaction with MCM2 and ORC1." FT /evidence="ECO:0000269|PubMed:11278932" FT MUTAGEN 485 FT /note="G->A: Abolishes histone acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:17954561, FT ECO:0000269|PubMed:20129055" FT MUTAGEN 508 FT /note="E->A: Abolished histone acetyltransferase activity." FT /evidence="ECO:0000269|PubMed:31827282" FT CONFLICT 38..44 FT /note="Missing (in Ref. 5; BAG57945)" FT /evidence="ECO:0000305" FT CONFLICT 41 FT /note="R -> Q (in Ref. 5; BAG57346)" FT /evidence="ECO:0000305" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 345..348 FT /evidence="ECO:0007829|PDB:7D0P" FT HELIX 357..360 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 362..367 FT /evidence="ECO:0007829|PDB:7D0P" FT TURN 369..371 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 374..376 FT /evidence="ECO:0007829|PDB:7D0P" FT HELIX 378..387 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 394..401 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 404..410 FT /evidence="ECO:0007829|PDB:7D0P" FT TURN 411..414 FT /evidence="ECO:0007829|PDB:7D0P" FT HELIX 415..426 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 441..450 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 453..465 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 470..477 FT /evidence="ECO:0007829|PDB:7D0P" FT HELIX 479..481 FT /evidence="ECO:0007829|PDB:7D0P" FT TURN 482..485 FT /evidence="ECO:0007829|PDB:6MAJ" FT HELIX 486..501 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 505..507 FT /evidence="ECO:0007829|PDB:7D0P" FT HELIX 513..533 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 536..539 FT /evidence="ECO:0007829|PDB:7D0P" FT HELIX 541..548 FT /evidence="ECO:0007829|PDB:7D0P" FT HELIX 552..561 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 565..568 FT /evidence="ECO:0007829|PDB:7D0P" FT STRAND 571..575 FT /evidence="ECO:0007829|PDB:7D0P" FT HELIX 578..593 FT /evidence="ECO:0007829|PDB:7D0P" FT HELIX 600..602 FT /evidence="ECO:0007829|PDB:7D0P" SQ SEQUENCE 611 AA; 70642 MW; 8368E7C4F07D8D7C CRC64; MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS QSSQDSSPVR NLQSFGTEEP AYSTRRVTRS QQQPTPVTPK KYPLRQTRSS GSETEQVVDF SDRETKNTAD HDESPPRTPT GNAPSSESDI DISSPNVSHD ESIAKDMSLK DSGSDLSHRP KRRRFHESYN FNMKCPTPGC NSLGHLTGKH ERHFSISGCP LYHNLSADEC KVRAQSRDKQ IEERMLSHRQ DDNNRHATRH QAPTERQLRY KEKVAELRKK RNSGLSKEQK EKYMEHRQTY GNTREPLLEN LTSEYDLDLF RRAQARASED LEKLRLQGQI TEGSNMIKTI AFGRYELDTW YHSPYPEEYA RLGRLYMCEF CLKYMKSQTI LRRHMAKCVW KHPPGDEIYR KGSISVFEVD GKKNKIYCQN LCLLAKLFLD HKTLYYDVEP FLFYVMTEAD NTGCHLIGYF SKEKNSFLNY NVSCILTMPQ YMRQGYGKML IDFSYLLSKV EEKVGSPERP LSDLGLISYR SYWKEVLLRY LHNFQGKEIS IKEISQETAV NPVDIVSTLQ ALQMLKYWKG KHLVLKRQDL IDEWIAKEAK RSNSNKTMDP SCLKWTPPKG T //