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Database: UniProt
Entry: Q9H7Z6
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ID   KAT8_HUMAN              Reviewed;         458 AA.
AC   Q9H7Z6; A8K4Z1; G5E9P2; Q659G0; Q7LC17; Q8IY59; Q8WYB4; Q8WZ14; Q9HAC5;
AC   Q9NR35;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   29-SEP-2021, entry version 178.
DE   RecName: Full=Histone acetyltransferase KAT8;
DE            EC=2.3.1.48 {ECO:0000269|PubMed:10786633, ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026, ECO:0000269|Ref.23, ECO:0000305|PubMed:16543150};
DE   AltName: Full=Lysine acetyltransferase 8;
DE   AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1;
DE            Short=MYST-1;
DE            Short=hMOF;
GN   Name=KAT8; Synonyms=MOF, MYST1; ORFNames=PP7073;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-458 (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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-458 (ISOFORM 1), CATALYTIC ACTIVITY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Heart;
RX   PubMed=10786633; DOI=10.1016/s0167-4781(99)00211-0;
RA   Neal K.C., Pannuti A., Smith E.R., Lucchesi J.C.;
RT   "A new human member of the MYST family of histone acetyl transferases with
RT   high sequence similarity to Drosophila MOF.";
RL   Biochim. Biophys. Acta 1490:170-174(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-458 (ISOFORM 1).
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-458 (ISOFORM 2).
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [9]
RP   INTERACTION WITH MORF4L1, AND FUNCTION.
RX   PubMed=12397079; DOI=10.1074/jbc.m203839200;
RA   Pardo P.S., Leung J.K., Lucchesi J.C., Pereira-Smith O.M.;
RT   "MRG15, a novel chromodomain protein, is present in two distinct
RT   multiprotein complexes involved in transcriptional activation.";
RL   J. Biol. Chem. 277:50860-50866(2002).
RN   [10]
RP   IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX   PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA   Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA   Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT   "Physical association and coordinate function of the H3 K4
RT   methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL   Cell 121:873-885(2005).
RN   [11]
RP   INTERACTION WITH ATM, AND FUNCTION.
RX   PubMed=15923642; DOI=10.1128/mcb.25.12.5292-5305.2005;
RA   Gupta A., Sharma G.G., Young C.S.H., Agarwal M., Smith E.R., Paull T.T.,
RA   Lucchesi J.C., Khanna K.K., Ludwig T., Pandita T.K.;
RT   "Involvement of human MOF in ATM function.";
RL   Mol. Cell. Biol. 25:5292-5305(2005).
RN   [12]
RP   FUNCTION, IDENTIFICATION OF MSL COMPLEX COMPONENTS, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=16227571; DOI=10.1128/mcb.25.21.9175-9188.2005;
RA   Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.;
RT   "A human protein complex homologous to the Drosophila MSL complex is
RT   responsible for the majority of histone H4 acetylation at lysine 16.";
RL   Mol. Cell. Biol. 25:9175-9188(2005).
RN   [13]
RP   ERRATUM OF PUBMED:16227571.
RA   Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.;
RL   Mol. Cell. Biol. 26:387-387(2006).
RN   [14]
RP   FUNCTION, IDENTIFICATION IN THE MSL COMPLEX, IDENTIFICATION IN THE NSL
RP   COMPLEX, AND INTERACTION WITH KANSL1.
RX   PubMed=16543150; DOI=10.1016/j.molcel.2006.02.007;
RA   Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M.,
RA   Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M.,
RA   Stunnenberg H.G., Saumweber H., Akhtar A.;
RT   "Nuclear pore components are involved in the transcriptional regulation of
RT   dosage compensation in Drosophila.";
RL   Mol. Cell 21:811-823(2006).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-113, 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   [17]
RP   FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=20018852; DOI=10.1074/jbc.c109.087981;
RA   Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
RA   Washburn M.P., Conaway J.W., Conaway R.C.;
RT   "Subunit composition and substrate specificity of a MOF-containing histone
RT   acetyltransferase distinct from the male-specific lethal (MSL) complex.";
RL   J. Biol. Chem. 285:4268-4272(2010).
RN   [18]
RP   INTERACTION WITH KANSL1.
RX   PubMed=20620954; DOI=10.1016/j.molcel.2010.05.021;
RA   Raja S.J., Charapitsa I., Conrad T., Vaquerizas J.M., Gebhardt P., Holz H.,
RA   Kadlec J., Fraterman S., Luscombe N.M., Akhtar A.;
RT   "The nonspecific lethal complex is a transcriptional regulator in
RT   Drosophila.";
RL   Mol. Cell 38:827-841(2010).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND IDENTIFICATION BY
RP   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   [21]
RP   INTERACTION WITH MSL3.
RX   PubMed=30224647; DOI=10.1038/s41588-018-0220-y;
RG   DDD Study;
RA   Basilicata M.F., Bruel A.L., Semplicio G., Valsecchi C.I.K., Aktas T.,
RA   Duffourd Y., Rumpf T., Morton J., Bache I., Szymanski W.G., Gilissen C.,
RA   Vanakker O., Ounap K., Mittler G., van der Burgt I., El Chehadeh S.,
RA   Cho M.T., Pfundt R., Tan T.Y., Kirchhoff M., Menten B., Vergult S.,
RA   Lindstrom K., Reis A., Johnson D.S., Fryer A., McKay V., Fisher R.B.,
RA   Thauvin-Robinet C., Francis D., Roscioli T., Pajusalu S., Radtke K.,
RA   Ganesh J., Brunner H.G., Wilson M., Faivre L., Kalscheuer V.M.,
RA   Thevenon J., Akhtar A.;
RT   "De novo mutations in MSL3 cause an X-linked syndrome marked by impaired
RT   histone H4 lysine 16 acetylation.";
RL   Nat. Genet. 50:1442-1451(2018).
RN   [22]
RP   INVOLVEMENT IN LIGOWS, VARIANTS LIGOWS CYS-90; GLN-98; GLN-99; VAL-165;
RP   175-LYS--LYS-458 DEL; GLU-175; ASN-181 AND CYS-325, CHARACTERIZATION OF
RP   VARIANTS LIGOWS CYS-90; GLN-98; GLN-99; VAL-165; 175-LYS--LYS-458 DEL;
RP   GLU-175; ASN-181 AND CYS-325, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=31794431; DOI=10.1172/jci131145;
RA   Li L., Ghorbani M., Weisz-Hubshman M., Rousseau J., Thiffault I.,
RA   Schnur R.E., Breen C., Oegema R., Weiss M.M., Waisfisz Q., Welner S.,
RA   Kingston H., Hills J.A., Boon E.M., Basel-Salmon L., Konen O.,
RA   Goldberg-Stern H., Bazak L., Tzur S., Jin J., Bi X., Bruccoleri M.,
RA   McWalter K., Cho M.T., Scarano M., Schaefer G.B., Brooks S.S., Hughes S.S.,
RA   van Gassen K.L.I., van Hagen J.M., Pandita T.K., Agrawal P.B.,
RA   Campeau P.M., Yang X.J.;
RT   "Lysine acetyltransferase 8 is involved in cerebral development and
RT   syndromic intellectual disability.";
RL   J. Clin. Invest. 130:1431-1445(2020).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 174-449 IN COMPLEX WITH
RP   ACETYL-COA AND ZINC, AND ACETYLATION AT LYS-274.
RG   Structural genomics consortium (SGC);
RT   "MYST histone acetyltransferase 1.";
RL   Submitted (MAY-2007) to the PDB data bank.
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 174-449 IN COMPLEX WITH ZINC
RP   IONS, AND ACETYLATION AT LYS-274.
RX   PubMed=21691301; DOI=10.1038/cr.2011.105;
RA   Sun B., Guo S., Tang Q., Li C., Zeng R., Xiong Z., Zhong C., Ding J.;
RT   "Regulation of the histone acetyltransferase activity of hMOF via
RT   autoacetylation of Lys274.";
RL   Cell Res. 21:1262-1266(2011).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 174-458 IN COMPLEX WITH MSL1;
RP   ZINC ION AND ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE,
RP   IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT LYS-274, INTERACTION
RP   WITH KANSL1; MSL1 AND MSL3, AND MUTAGENESIS OF LYS-274; CYS-316 AND
RP   GLU-350.
RX   PubMed=21217699; DOI=10.1038/nsmb.1960;
RA   Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S.,
RA   Akhtar A.;
RT   "Structural basis for MOF and MSL3 recruitment into the dosage compensation
RT   complex by MSL1.";
RL   Nat. Struct. Mol. Biol. 18:142-149(2011).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 170-458 IN COMPLEX WITH MSL1,
RP   ACETYLATION AT LYS-274, FUNCTION IN MSL AND NSL COMPLEX, FUNCTION,
RP   CATALYTIC ACTIVITY, AND INTERACTION WITH KANSL1; MSL1 AND MSL3.
RX   PubMed=22547026; DOI=10.1038/cr.2012.72;
RA   Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.;
RT   "Structural insight into the regulation of MOF in the male-specific lethal
RT   complex and the non-specific lethal complex.";
RL   Cell Res. 22:1078-1081(2012).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 177-458 IN COMPLEX WITH ZINC,
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, ACETYLATION AT LYS-274,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-274.
RX   PubMed=22020126; DOI=10.1038/emboj.2011.382;
RA   Yuan H., Rossetto D., Mellert H., Dang W., Srinivasan M., Johnson J.,
RA   Hodawadekar S., Ding E.C., Speicher K., Abshiru N., Perry R., Wu J.,
RA   Yang C., Zheng Y.G., Speicher D.W., Thibault P., Verreault A.,
RA   Johnson F.B., Berger S.L., Sternglanz R., McMahon S.B., Cote J.,
RA   Marmorstein R.;
RT   "MYST protein acetyltransferase activity requires active site lysine
RT   autoacetylation.";
RL   EMBO J. 31:58-70(2012).
CC   -!- FUNCTION: Histone acetyltransferase which may be involved in
CC       transcriptional activation (PubMed:12397079, PubMed:22020126). May
CC       influence the function of ATM (PubMed:15923642). As part of the MSL
CC       complex it is involved in acetylation of nucleosomal histone H4
CC       producing specifically H4K16ac (PubMed:16227571, PubMed:16543150,
CC       PubMed:21217699, PubMed:22547026, PubMed:22020126). As part of the NSL
CC       complex it may be involved in acetylation of nucleosomal histone H4 on
CC       several lysine residues (PubMed:20018852, PubMed:22547026). That
CC       activity is less specific than the one of the MSL complex
CC       (PubMed:20018852, PubMed:22547026). Can also acetylate TP53/p53 at
CC       'Lys-120'. {ECO:0000269|PubMed:12397079, ECO:0000269|PubMed:15923642,
CC       ECO:0000269|PubMed:16227571, ECO:0000269|PubMed:16543150,
CC       ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:21217699,
CC       ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026,
CC       ECO:0000269|PubMed:31794431}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000269|PubMed:10786633, ECO:0000269|PubMed:21217699,
CC         ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026,
CC         ECO:0000269|PubMed:31794431, ECO:0000305|PubMed:16543150};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC         Evidence={ECO:0000305|PubMed:10786633};
CC   -!- SUBUNIT: Component of a multisubunit histone acetyltransferase complex
CC       (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1
CC       (PubMed:16227571, PubMed:16543150). Interacts with MSL1; the
CC       interaction is direct (PubMed:21217699, PubMed:22547026). Component of
CC       the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3,
CC       MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:16543150,
CC       PubMed:20018852). Component of some MLL1/MLL complex, at least composed
CC       of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as
CC       well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
CC       KANSL1, LAS1L, MAX, MCRS1, MGA, MOF/KAT8, PELP1, PHF20, PRP31, RING2,
CC       RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC       TEX10 (PubMed:15960975). Interacts with the chromodomain of
CC       MORF4L1/MRG15 (PubMed:12397079). Interacts with ATM through the
CC       chromodomain (PubMed:15923642). Interacts with KANSL1; the interaction
CC       is direct (PubMed:16543150, PubMed:20620954, PubMed:21217699,
CC       PubMed:22547026). Interacts with MSL3 (PubMed:21217699,
CC       PubMed:22547026, PubMed:30224647). Interacts with NELFD (By
CC       similarity). {ECO:0000250|UniProtKB:Q9D1P2,
CC       ECO:0000269|PubMed:12397079, ECO:0000269|PubMed:15923642,
CC       ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16227571,
CC       ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:20018852,
CC       ECO:0000269|PubMed:20620954, ECO:0000269|PubMed:21217699,
CC       ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22547026,
CC       ECO:0000269|PubMed:30224647, ECO:0000269|PubMed:31794431}.
CC   -!- INTERACTION:
CC       Q9H7Z6; Q03164: KMT2A; NbExp=3; IntAct=EBI-896414, EBI-591370;
CC       Q9H7Z6; Q99496: RNF2; NbExp=2; IntAct=EBI-896414, EBI-722416;
CC       Q9H7Z6; P04637: TP53; NbExp=2; IntAct=EBI-896414, EBI-366083;
CC       Q9H7Z6; P02309: HHF2; Xeno; NbExp=2; IntAct=EBI-896414, EBI-8113;
CC       Q9H7Z6-1; Q68DK7-1: MSL1; NbExp=2; IntAct=EBI-26435386, EBI-26435399;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10786633,
CC       ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:31794431}. Chromosome
CC       {ECO:0000305|PubMed:10786633}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H7Z6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H7Z6-2; Sequence=VSP_014579;
CC   -!- PTM: Autoacetylation at Lys-274 is required for binding histone H4 with
CC       high affinity and for proper function. {ECO:0000269|PubMed:22020126}.
CC   -!- DISEASE: Li-Ghorbani-Weisz-Hubshman syndrome (LIGOWS) [MIM:618974]: An
CC       autosomal dominant disorder characterized by global developmental
CC       delay, mild to moderate intellectual disability, speech and language
CC       impairment, and variable facial dysmorphism. Some patients have
CC       seizures and autistic features. Brain imaging abnormalities are
CC       observed in some patients and include decreased white matter volume,
CC       enlarged ventricles, thin corpus callosum, and gray matter nodular
CC       heterotopia. {ECO:0000269|PubMed:31794431}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL55762.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC       Sequence=AAL56648.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK021872; BAB13924.1; -; mRNA.
DR   EMBL; AK024102; BAB14827.1; -; mRNA.
DR   EMBL; AK291106; BAF83795.1; -; mRNA.
DR   EMBL; AC009088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC135050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471192; EAW52157.1; -; Genomic_DNA.
DR   EMBL; CH471192; EAW52158.1; -; Genomic_DNA.
DR   EMBL; BC037773; AAH37773.1; -; mRNA.
DR   EMBL; AF217501; AAL56648.1; ALT_FRAME; mRNA.
DR   EMBL; AF260665; AAF72665.2; -; mRNA.
DR   EMBL; AF289578; AAL55762.1; ALT_SEQ; mRNA.
DR   EMBL; AL050395; CAH56416.1; -; mRNA.
DR   CCDS; CCDS10706.1; -. [Q9H7Z6-1]
DR   CCDS; CCDS45468.1; -. [Q9H7Z6-2]
DR   RefSeq; NP_115564.2; NM_032188.2. [Q9H7Z6-1]
DR   RefSeq; NP_892003.2; NM_182958.2. [Q9H7Z6-2]
DR   PDB; 2GIV; X-ray; 1.94 A; A=174-449.
DR   PDB; 2PQ8; X-ray; 1.45 A; A=174-449.
DR   PDB; 2Y0M; X-ray; 2.70 A; A=174-458.
DR   PDB; 3QAH; X-ray; 2.10 A; A=174-449.
DR   PDB; 3TOA; X-ray; 3.00 A; A=177-458.
DR   PDB; 3TOB; X-ray; 2.70 A; A=177-458.
DR   PDB; 4DNC; X-ray; 2.05 A; A/B=170-458.
DR   PDB; 5H43; X-ray; 2.30 A; B=140-149, C=128-142.
DR   PDB; 5J8C; X-ray; 2.17 A; A=177-458.
DR   PDB; 5J8F; X-ray; 2.60 A; A=177-458.
DR   PDB; 5WCI; X-ray; 1.78 A; A=174-449.
DR   PDB; 6BA2; X-ray; 1.85 A; A=174-449.
DR   PDB; 6BA4; X-ray; 1.95 A; A=174-449.
DR   PDB; 6CT2; X-ray; 2.13 A; A=174-449.
DR   PDB; 6OIN; X-ray; 1.70 A; A=176-448.
DR   PDB; 6OIO; X-ray; 1.70 A; A=176-448.
DR   PDB; 6OIP; X-ray; 1.80 A; A=176-448.
DR   PDB; 6OIQ; X-ray; 1.75 A; A=176-448.
DR   PDB; 6OIR; X-ray; 2.03 A; A=176-448.
DR   PDB; 6OWH; X-ray; 2.00 A; A=176-448.
DR   PDB; 6OWI; X-ray; 1.75 A; A=176-448.
DR   PDB; 6PD8; X-ray; 2.74 A; A=177-448.
DR   PDB; 6PD9; X-ray; 2.80 A; A=177-448.
DR   PDB; 6PDA; X-ray; 2.45 A; A=177-448.
DR   PDB; 6PDB; X-ray; 2.42 A; A=177-448.
DR   PDB; 6PDC; X-ray; 1.96 A; A=177-448.
DR   PDB; 6PDD; X-ray; 2.15 A; A=177-448.
DR   PDB; 6PDE; X-ray; 2.22 A; A=177-448.
DR   PDB; 6PDF; X-ray; 2.22 A; A=177-448.
DR   PDB; 6PDG; X-ray; 1.92 A; A=177-448.
DR   PDB; 7CMR; X-ray; 2.20 A; A=1-458.
DR   PDBsum; 2GIV; -.
DR   PDBsum; 2PQ8; -.
DR   PDBsum; 2Y0M; -.
DR   PDBsum; 3QAH; -.
DR   PDBsum; 3TOA; -.
DR   PDBsum; 3TOB; -.
DR   PDBsum; 4DNC; -.
DR   PDBsum; 5H43; -.
DR   PDBsum; 5J8C; -.
DR   PDBsum; 5J8F; -.
DR   PDBsum; 5WCI; -.
DR   PDBsum; 6BA2; -.
DR   PDBsum; 6BA4; -.
DR   PDBsum; 6CT2; -.
DR   PDBsum; 6OIN; -.
DR   PDBsum; 6OIO; -.
DR   PDBsum; 6OIP; -.
DR   PDBsum; 6OIQ; -.
DR   PDBsum; 6OIR; -.
DR   PDBsum; 6OWH; -.
DR   PDBsum; 6OWI; -.
DR   PDBsum; 6PD8; -.
DR   PDBsum; 6PD9; -.
DR   PDBsum; 6PDA; -.
DR   PDBsum; 6PDB; -.
DR   PDBsum; 6PDC; -.
DR   PDBsum; 6PDD; -.
DR   PDBsum; 6PDE; -.
DR   PDBsum; 6PDF; -.
DR   PDBsum; 6PDG; -.
DR   PDBsum; 7CMR; -.
DR   BMRB; Q9H7Z6; -.
DR   SMR; Q9H7Z6; -.
DR   BioGRID; 123914; 61.
DR   ComplexPortal; CPX-809; NSL histone acetyltransferase complex.
DR   ComplexPortal; CPX-815; MSL histone acetyltransferase complex.
DR   CORUM; Q9H7Z6; -.
DR   IntAct; Q9H7Z6; 21.
DR   MINT; Q9H7Z6; -.
DR   STRING; 9606.ENSP00000406037; -.
DR   BindingDB; Q9H7Z6; -.
DR   ChEMBL; CHEMBL1932912; -.
DR   GuidetoPHARMACOLOGY; 2668; -.
DR   iPTMnet; Q9H7Z6; -.
DR   PhosphoSitePlus; Q9H7Z6; -.
DR   BioMuta; KAT8; -.
DR   DMDM; 68565938; -.
DR   EPD; Q9H7Z6; -.
DR   jPOST; Q9H7Z6; -.
DR   MassIVE; Q9H7Z6; -.
DR   MaxQB; Q9H7Z6; -.
DR   PaxDb; Q9H7Z6; -.
DR   PeptideAtlas; Q9H7Z6; -.
DR   PRIDE; Q9H7Z6; -.
DR   ProteomicsDB; 81162; -. [Q9H7Z6-1]
DR   ProteomicsDB; 81163; -. [Q9H7Z6-2]
DR   Antibodypedia; 27640; 292 antibodies.
DR   DNASU; 84148; -.
DR   Ensembl; ENST00000219797; ENSP00000219797; ENSG00000103510. [Q9H7Z6-1]
DR   Ensembl; ENST00000448516; ENSP00000406037; ENSG00000103510. [Q9H7Z6-2]
DR   Ensembl; ENST00000543774; ENSP00000456933; ENSG00000103510. [Q9H7Z6-1]
DR   GeneID; 84148; -.
DR   KEGG; hsa:84148; -.
DR   UCSC; uc002eax.4; human. [Q9H7Z6-1]
DR   CTD; 84148; -.
DR   DisGeNET; 84148; -.
DR   GeneCards; KAT8; -.
DR   HGNC; HGNC:17933; KAT8.
DR   HPA; ENSG00000103510; Low tissue specificity.
DR   MIM; 609912; gene.
DR   MIM; 618974; phenotype.
DR   neXtProt; NX_Q9H7Z6; -.
DR   OpenTargets; ENSG00000103510; -.
DR   PharmGKB; PA38476; -.
DR   VEuPathDB; HostDB:ENSG00000103510; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   GeneTree; ENSGT00940000159512; -.
DR   HOGENOM; CLU_011815_2_1_1; -.
DR   InParanoid; Q9H7Z6; -.
DR   OMA; EKTYRYH; -.
DR   OrthoDB; 629545at2759; -.
DR   PhylomeDB; Q9H7Z6; -.
DR   TreeFam; TF317619; -.
DR   BRENDA; 2.3.1.48; 2681.
DR   PathwayCommons; Q9H7Z6; -.
DR   Reactome; R-HSA-3214847; HATs acetylate histones.
DR   SIGNOR; Q9H7Z6; -.
DR   BioGRID-ORCS; 84148; 783 hits in 1025 CRISPR screens.
DR   ChiTaRS; KAT8; human.
DR   EvolutionaryTrace; Q9H7Z6; -.
DR   GeneWiki; MYST1; -.
DR   GenomeRNAi; 84148; -.
DR   Pharos; Q9H7Z6; Tchem.
DR   PRO; PR:Q9H7Z6; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9H7Z6; protein.
DR   Bgee; ENSG00000103510; Expressed in cerebellar vermis and 242 other tissues.
DR   ExpressionAtlas; Q9H7Z6; baseline and differential.
DR   Genevisible; Q9H7Z6; HS.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR   GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR   GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR   GO; GO:0072487; C:MSL complex; IDA:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); IDA:UniProtKB.
DR   GO; GO:0043995; F:histone acetyltransferase activity (H4-K5 specific); IDA:UniProtKB.
DR   GO; GO:0043996; F:histone acetyltransferase activity (H4-K8 specific); IC:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
DR   GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR   GO; GO:0043984; P:histone H4-K16 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:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0010506; P:regulation of autophagy; IDA:MGI.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR002717; HAT_MYST-type.
DR   InterPro; IPR037906; KAT8.
DR   InterPro; IPR025995; Tudor-knot.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR040706; Zf-MYST.
DR   PANTHER; PTHR10615:SF82; PTHR10615:SF82; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF11717; Tudor-knot; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51726; MYST_HAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Acyltransferase;
KW   Alternative splicing; Chromatin regulator; Chromosome; Disease variant;
KW   Mental retardation; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation; Transferase;
KW   Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..458
FT                   /note="Histone acetyltransferase KAT8"
FT                   /id="PRO_0000051566"
FT   DOMAIN          69..123
FT                   /note="Chromo"
FT   DOMAIN          174..447
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         207..232
FT                   /note="C2HC MYST-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063,
FT                   ECO:0000269|PubMed:22020126"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..458
FT                   /note="Sufficient for interaction with KANSL1"
FT   REGION          317..319
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23"
FT   REGION          324..330
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23"
FT   ACT_SITE        350
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000303|PubMed:21217699,
FT                   ECO:0000303|PubMed:22020126, ECO:0000305"
FT   BINDING         354
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23"
FT   BINDING         363
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23"
FT   BINDING         432
FT                   /note="Acetyl-CoA"
FT                   /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XI06"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XI06"
FT   MOD_RES         113
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         274
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:21217699,
FT                   ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126,
FT                   ECO:0000269|PubMed:22547026, ECO:0000269|Ref.23"
FT   MOD_RES         348
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         438..458
FT                   /note="VDSVCLKWAPPKHKQVKLSKK -> GGWGAAVCRGRWGSVSIWTGRSQGLLI
FT                   AVT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_014579"
FT   VARIANT         90
FT                   /note="Y -> C (in LIGOWS; no effect on protein expression;
FT                   no effect on MSL complex assembly; decreased histone
FT                   acetyltransferase activity)"
FT                   /evidence="ECO:0000269|PubMed:31794431"
FT                   /id="VAR_084751"
FT   VARIANT         98
FT                   /note="R -> Q (in LIGOWS; no effect on protein expression;
FT                   no effect on MSL complex assembly; decreased histone
FT                   acetyltransferase activity)"
FT                   /evidence="ECO:0000269|PubMed:31794431"
FT                   /id="VAR_084752"
FT   VARIANT         99
FT                   /note="R -> Q (in LIGOWS; no effect on protein expression;
FT                   no effect on MSL complex assembly; decreased histone
FT                   acetyltransferase activity)"
FT                   /evidence="ECO:0000269|PubMed:31794431"
FT                   /id="VAR_084753"
FT   VARIANT         165
FT                   /note="A -> V (in LIGOWS; unknown pathological
FT                   significance; no effect on protein expression; no effect on
FT                   MSL complex assembly; decreased histone acetyltransferase
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:31794431"
FT                   /id="VAR_084754"
FT   VARIANT         175..458
FT                   /note="Missing (found in a severe neurodevelopmental
FT                   disorder similar to Li-Ghorbani-Weisz-Hubshman syndrome
FT                   with apparently autosomal recessive inheritance; unknown
FT                   pathological significance; loss of protein expression)"
FT                   /evidence="ECO:0000269|PubMed:31794431"
FT                   /id="VAR_084755"
FT   VARIANT         175
FT                   /note="K -> E (in LIGOWS; no effect on protein expression;
FT                   no effect on MSL complex assembly; decreased histone
FT                   acetyltransferase activity)"
FT                   /evidence="ECO:0000269|PubMed:31794431"
FT                   /id="VAR_084756"
FT   VARIANT         181
FT                   /note="K -> N (in LIGOWS; unknown pathological
FT                   significance; no effect on protein expression; no effect on
FT                   MSL complex assembly; decreased histone acetyltransferase
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:31794431"
FT                   /id="VAR_084757"
FT   VARIANT         325
FT                   /note="R -> C (found in a severe neurodevelopmental
FT                   disorder similar to Li-Ghorbani-Weisz-Hubshman syndrome
FT                   with apparently autosomal recessive inheritance; unknown
FT                   pathological significance; no effect on protein expression;
FT                   no effect on localization to the nucleus; no effect on MSL
FT                   complex assembly; decreased histone acetyltransferase
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:31794431"
FT                   /id="VAR_084758"
FT   MUTAGEN         274
FT                   /note="K->A: Abolishes histone acetyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:21217699"
FT   MUTAGEN         274
FT                   /note="K->R: Abolishes histone acetyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:22020126"
FT   MUTAGEN         316
FT                   /note="C->S: Strongly reduces histone acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:21217699"
FT   MUTAGEN         350
FT                   /note="E->Q: Abolishes histone acetyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:21217699"
FT   CONFLICT        222
FT                   /note="S -> T (in Ref. 7; AAL55762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="Y -> H (in Ref. 1; BAB14827)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        372
FT                   /note="I -> N (in Ref. 1; BAB14827)"
FT                   /evidence="ECO:0000305"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:5H43"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:5H43"
FT   STRAND          181..184
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   HELIX           199..203
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   TURN            211..213
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   HELIX           220..229
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          236..243
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          246..252
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   TURN            253..255
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   HELIX           257..268
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   HELIX           274..277
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          283..292
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          295..305
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          312..315
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          317..319
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   HELIX           321..323
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          325..327
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   HELIX           328..342
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          347..349
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   HELIX           355..372
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   TURN            376..378
FT                   /evidence="ECO:0007829|PDB:6CT2"
FT   HELIX           383..389
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   HELIX           393..402
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   STRAND          406..409
FT                   /evidence="ECO:0007829|PDB:6OIN"
FT   STRAND          412..415
FT                   /evidence="ECO:0007829|PDB:6OIN"
FT   HELIX           419..427
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   HELIX           429..431
FT                   /evidence="ECO:0007829|PDB:6OIN"
FT   HELIX           440..442
FT                   /evidence="ECO:0007829|PDB:2PQ8"
FT   CONFLICT        Q9H7Z6-2:454
FT                   /note="I -> M (in Ref. 4; AAH37773)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   458 AA;  52403 MW;  66C474BE5B90E8E3 CRC64;
     MAAQGAAAAV AAGTSGVAGE GEPGPGENAA AEGTAPSPGR VSPPTPARGE PEVTVEIGET
     YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL DEWVDKNRLA LTKTVKDAVQ
     KNSEKYLSEL AEQPERKITR NQKRKHDEIN HVQKTYAEMD PTTAALEKEH EAITKVKYVD
     KIHIGNYEID AWYFSPFPED YGKQPKLWLC EYCLKYMKYE KSYRFHLGQC QWRQPPGKEI
     YRKSNISVYE VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG
     YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE KPLSDLGKLS
     YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL QSLNMVKYWK GQHVICVTPK
     LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH KQVKLSKK
//
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