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-MAY-2023, entry version 185. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 82. 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 GlyGen; Q9H7Z6; 1 site, 1 O-linked glycan (1 site). 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 ProteomicsDB; 81162; -. [Q9H7Z6-1] DR ProteomicsDB; 81163; -. [Q9H7Z6-2] DR Antibodypedia; 27640; 308 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 AGR; HGNC:17933; -. 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; ILCEVDK; -. DR OrthoDB; 118560at2759; -. 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; 832 hits in 1185 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:0046972; F:histone H4K16 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0043984; P:histone H4-K16 acetylation; IDA:ComplexPortal. DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:ComplexPortal. DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:ComplexPortal. DR GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0022008; P:neurogenesis; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:ComplexPortal. DR GO; GO:0010506; P:regulation of autophagy; IDA:MGI. DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; ISO:ComplexPortal. DR CDD; cd18984; CBD_MOF_like; 1. DR CDD; cd04301; NAT_SF; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR002717; HAT_MYST-type. DR InterPro; IPR025995; Tudor-knot. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR040706; Zf-MYST. DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10615:SF82; HISTONE ACETYLTRANSFERASE KAT8; 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; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF54160; Chromo domain-like; 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 //