KAT8_HUMAN
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 03-AUG-2022, entry version 181.
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 (via its Tudor-knot
CC domain) (PubMed:15923642). Interacts with KANSL1; the interaction is
CC 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 AlphaFoldDB; Q9H7Z6; -.
DR BMRB; Q9H7Z6; -.
DR SMR; Q9H7Z6; -.
DR BioGRID; 123914; 77.
DR ComplexPortal; CPX-809; NSL histone acetyltransferase complex.
DR ComplexPortal; CPX-815; MSL histone acetyltransferase complex.
DR CORUM; Q9H7Z6; -.
DR IntAct; Q9H7Z6; 27.
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; 305 antibodies from 38 providers.
DR DNASU; 84148; -.
DR Ensembl; ENST00000219797.9; ENSP00000219797.3; ENSG00000103510.20. [Q9H7Z6-1]
DR Ensembl; ENST00000448516.6; ENSP00000406037.2; ENSG00000103510.20. [Q9H7Z6-2]
DR Ensembl; ENST00000543774.6; ENSP00000456933.2; ENSG00000103510.20. [Q9H7Z6-1]
DR GeneID; 84148; -.
DR KEGG; hsa:84148; -.
DR MANE-Select; ENST00000219797.9; ENSP00000219797.3; NM_032188.3; NP_115564.2.
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 MalaCards; KAT8; -.
DR MIM; 609912; gene.
DR MIM; 618974; phenotype.
DR neXtProt; NX_Q9H7Z6; -.
DR OpenTargets; ENSG00000103510; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
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; MNMVKYW; -.
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 SignaLink; Q9H7Z6; -.
DR SIGNOR; Q9H7Z6; -.
DR BioGRID-ORCS; 84148; 801 hits in 1097 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 hemisphere and 202 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:0044545; C:NSL complex; IDA:ComplexPortal.
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:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0010485; F:H4 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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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:0051571; P:positive regulation of histone H3-K4 methylation; IDA:ComplexPortal.
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 GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IEA:Ensembl.
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 Intellectual disability; 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 55..110
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
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 ACT_SITE 350
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000303|PubMed:21217699,
FT ECO:0000303|PubMed:22020126, ECO:0000305"
FT BINDING 317..319
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23"
FT BINDING 324..330
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23"
FT BINDING 354
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23"
FT BINDING 363
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23"
FT BINDING 432
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
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
