KAT7_HUMAN
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 03-AUG-2022, entry version 192.
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, ECO:0000303|PubMed:10930412},
GN HBOa {ECO:0000303|Ref.3}, MYST2 {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}.
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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; 125.
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; 70.
DR MINT; O95251; -.
DR STRING; 9606.ENSP00000259021; -.
DR BindingDB; O95251; -.
DR ChEMBL; CHEMBL3774299; -.
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; O95251; -.
DR PeptideAtlas; O95251; -.
DR PRIDE; O95251; -.
DR ProteomicsDB; 17693; -.
DR ProteomicsDB; 33968; -.
DR ProteomicsDB; 50746; -. [O95251-1]
DR ProteomicsDB; 50747; -. [O95251-2]
DR ProteomicsDB; 50748; -. [O95251-3]
DR Antibodypedia; 17983; 387 antibodies from 39 providers.
DR DNASU; 11143; -.
DR Ensembl; ENST00000259021.9; ENSP00000259021.4; ENSG00000136504.13. [O95251-1]
DR Ensembl; ENST00000424009.6; ENSP00000398961.2; ENSG00000136504.13. [O95251-4]
DR Ensembl; ENST00000454930.6; ENSP00000413415.2; ENSG00000136504.13. [O95251-5]
DR Ensembl; ENST00000509773.5; ENSP00000424577.1; ENSG00000136504.13. [O95251-2]
DR Ensembl; ENST00000510819.5; ENSP00000423385.1; ENSG00000136504.13. [O95251-3]
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 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; EDRMLSH; -.
DR OrthoDB; 629545at2759; -.
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; 159 hits in 1111 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 199 other tissues.
DR ExpressionAtlas; O95251; baseline and differential.
DR Genevisible; O95251; HS.
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:UniProtKB.
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:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0016570; P:histone modification; IDA:ComplexPortal.
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 transcription, DNA-templated; 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:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IDA:UniProtKB.
DR GO; GO:0090240; P:positive regulation of histone H4 acetylation; IMP:CAFA.
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; IMP:CAFA.
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:2000819; P:regulation of nucleotide-excision repair; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
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 Gene3D; 1.10.10.10; -; 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 Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF103637; SSF103637; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
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
