ID KAT6A_HUMAN Reviewed; 2004 AA. AC Q92794; Q76L81; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 225. DE RecName: Full=Histone acetyltransferase KAT6A; DE EC=2.3.1.48 {ECO:0000269|PubMed:11313971, ECO:0000269|PubMed:11742995}; DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3; DE Short=MYST-3; DE AltName: Full=Monocytic leukemia zinc finger protein; DE AltName: Full=Runt-related transcription factor-binding protein 2; DE AltName: Full=Zinc finger protein 220; GN Name=KAT6A; Synonyms=MOZ, MYST3, RUNXBP2, ZNF220; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION WITH CREBBP. RX PubMed=8782817; DOI=10.1038/ng0996-33; RA Borrow J., Stanton V.P. Jr., Andresen J.M., Becher R., Behm F.G., RA Chaganti R.S.K., Civin C.I., Disteche C., Dube I., Frischauf A.M., RA Horsman D., Mitelman F., Volinia S., Watmore A.E., Housman D.E.; RT "The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a RT putative acetyltransferase to the CREB-binding protein."; RL Nat. Genet. 14:33-41(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-813, AND CHROMOSOMAL TRANSLOCATION WITH RP ASXL2. RC TISSUE=Bone marrow; RA Hosoda F., Kitabayashi I., Kakazu N., Fukushima M., Aikawa Y., Abe T., RA Hibi S., Yagi T., Ohki M.; RT "MOZ is fused to a novel Polycomb group gene in a therapy-related RT myelodysplastic syndrome with t(2;8)(p23;p11.2)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1089-1117, AND CHROMOSOMAL TRANSLOCATION WITH RP NCOA2. RX PubMed=9558366; RA Carapeti M., Aguiar R.C.T., Goldman J.M., Cross N.C.P.; RT "A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in RT acute myeloid leukemia."; RL Blood 91:3127-3133(1998). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1111-1128, AND CHROMOSOMAL TRANSLOCATION WITH RP EP300. RX PubMed=10824998; RX DOI=10.1002/(sici)1098-2264(200006)28:2<138::aid-gcc2>3.0.co;2-2; RA Chaffanet M., Gressin L., Preudhomme C., Soenen-Cornu V., Birnbaum D., RA Pebusque M.-J.; RT "MOZ is fused to p300 in an acute monocytic leukemia with t(8;22)."; RL Genes Chromosomes Cancer 28:138-144(2000). RN [6] RP INTERACTION WITH RUNX1, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, RP ACETYLATION, CHROMOSOMAL TRANSLOCATION WITH CREBBP, AND FUNCTION. RX PubMed=11742995; DOI=10.1093/emboj/20.24.7184; RA Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.; RT "Activation of AML1-mediated transcription by MOZ and inhibition by the RT MOZ-CBP fusion protein."; RL EMBO J. 20:7184-7196(2001). RN [7] RP CATALYTIC ACTIVITY, AND DOMAIN. RX PubMed=11313971; DOI=10.1038/sj.onc.1204114; RA Champagne N., Pelletier N., Yang X.-J.; RT "The monocytic leukemia zinc finger protein MOZ is a histone RT acetyltransferase."; RL Oncogene 20:404-409(2001). RN [8] RP INTERACTION WITH RUNX2, AND FUNCTION. RX PubMed=11965546; DOI=10.1038/sj.onc.1205367; RA Pelletier N., Champagne N., Stifani S., Yang X.-J.; RT "MOZ and MORF histone acetyltransferases interact with the Runt-domain RT transcription factor Runx2."; RL Oncogene 21:2729-2740(2002). RN [9] RP CHROMOSOMAL TRANSLOCATION WITH NCOA2, AND MUTAGENESIS OF CYS-543 AND RP GLY-657. RX PubMed=12676584; DOI=10.1016/s1535-6108(03)00051-5; RA Deguchi K., Ayton P.M., Carapeti M., Kutok J.L., Snyder C.S., RA Williams I.R., Cross N.C.P., Glass C.K., Cleary M.L., Gilliland D.G.; RT "MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome RT binding motif and TIF2-mediated recruitment of CBP."; RL Cancer Cell 3:259-271(2003). RN [10] RP FUNCTION. RX PubMed=12771199; DOI=10.1093/nar/gkg401; RA Bristow C.A.P., Shore P.; RT "Transcriptional regulation of the human MIP-1alpha promoter by RUNX1 and RT MOZ."; RL Nucleic Acids Res. 31:2735-2744(2003). RN [11] RP SUBCELLULAR LOCATION, AND CHROMOSOMAL TRANSLOCATION WITH NCOA2. RX PubMed=15657427; DOI=10.1128/mcb.25.3.988-1002.2005; RA Kindle K.B., Troke P.J.F., Collins H.M., Matsuda S., Bossi D., Bellodi C., RA Kalkhoven E., Salomoni P., Pelicci P.G., Minucci S., Heery D.M.; RT "MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment RT of CBP function."; RL Mol. Cell. Biol. 25:988-1002(2005). RN [12] RP FUNCTION, AND IDENTIFICATION IN THE MOZ/MORF COMPLEX. RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007; RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., RA Lane W.S., Tan S., Yang X.-J., Cote J.; RT "ING tumor suppressor proteins are critical regulators of chromatin RT acetylation required for genome expression and perpetuation."; RL Mol. Cell 21:51-64(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [14] RP IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, AND RP SUBCELLULAR LOCATION. RX PubMed=18794358; DOI=10.1128/mcb.01297-08; RA Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C., RA Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J., RA Yang X.-J.; RT "Molecular architecture of quartet MOZ/MORF histone acetyltransferase RT complexes."; RL Mol. Cell. Biol. 28:6828-6843(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350; LYS-355 AND LYS-1007, AND RP IDENTIFICATION BY MASS 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-1113, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420; SER-473; SER-812; RP SER-941; SER-954; SER-974; SER-1089; SER-1090 AND SER-1113, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP FUNCTION, INTERACTION WITH PML AND TP53, AND PHOSPHORYLATION AT THR-369. RX PubMed=23431171; DOI=10.1073/pnas.1300490110; RA Rokudai S., Laptenko O., Arnal S.M., Taya Y., Kitabayashi I., Prives C.; RT "MOZ increases p53 acetylation and premature senescence through its complex RT formation with PML."; RL Proc. Natl. Acad. Sci. U.S.A. 110:3895-3900(2013). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP INVOLVEMENT IN ARTHS. RX PubMed=25728775; DOI=10.1016/j.ajhg.2015.01.017; RG UCLA Clinical Genomics Center; RA Arboleda V.A., Lee H., Dorrani N., Zadeh N., Willis M., Macmurdo C.F., RA Manning M.A., Kwan A., Hudgins L., Barthelemy F., Miceli M.C., RA Quintero-Rivera F., Kantarci S., Strom S.P., Deignan J.L., Grody W.W., RA Vilain E., Nelson S.F.; RT "De novo nonsense mutations in KAT6A, a lysine acetyl-transferase gene, RT cause a syndrome including microcephaly and global developmental delay."; RL Am. J. Hum. Genet. 96:498-506(2015). RN [23] RP INVOLVEMENT IN ARTHS. RX PubMed=25728777; DOI=10.1016/j.ajhg.2015.01.016; RA Tham E., Lindstrand A., Santani A., Malmgren H., Nesbitt A., Dubbs H.A., RA Zackai E.H., Parker M.J., Millan F., Rosenbaum K., Wilson G.N., RA Nordgren A.; RT "Dominant mutations in KAT6A cause intellectual disability with RT recognizable syndromic features."; RL Am. J. Hum. Genet. 96:507-513(2015). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-834 AND LYS-1342, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [25] RP STRUCTURE BY NMR OF 531-563. RA Kwan A.H.Y., Gell D.A., Liew C.K., Mackay J.P.; RT "Solution structure of a CCCCCHC zinc finger from MOZ."; RL Submitted (JUN-2002) to the PDB data bank. RN [26] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 501-784 IN COMPLEXES WITH RP ACETYL-COA; HISTONE H3 AND HISTONE H4 AND ZINC IONS, FUNCTION, CATALYTIC RP ACTIVITY, DNA-BINDING, AND MUTAGENESIS OF LYS-545; ILE-727 AND HIS-732. RX PubMed=17925393; DOI=10.1074/jbc.m705812200; RA Holbert M.A., Sikorski T., Carten J., Snowflack D., Hodawadekar S., RA Marmorstein R.; RT "The human monocytic leukemia zinc finger histone acetyltransferase domain RT contains DNA-binding activity implicated in chromatin targeting."; RL J. Biol. Chem. 282:36603-36613(2007). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 497-780 IN COMPLEX WITH RP ACETYL-COA, AND ACETYLATION AT LYS-604. RG Structural genomics consortium (SGC); RT "The crystal structure of human MYST histone acetyltransferase 3 in complex RT with acetylcoenzyme A."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Histone acetyltransferase that acetylates lysine residues in CC histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex CC which has a histone H3 acetyltransferase activity. May act as a CC transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at CC 'Lys-120' and 'Lys-382' and controls its transcriptional activity via CC association with PML. {ECO:0000269|PubMed:11742995, CC ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:12771199, CC ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:17925393, CC ECO:0000269|PubMed:23431171}. 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:11313971, ECO:0000269|PubMed:11742995, CC ECO:0000269|PubMed:17925393}; CC -!- SUBUNIT: Component of the MOZ/MORF complex composed at least of ING5, CC KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts CC with RUNX1; phosphorylation of RUNX1 enhances the interaction. CC Interacts with RUNX2. Interacts with p53/TP53. Interacts with PML CC (isoform PML-4) and this interaction positively regulates its CC acetylation activity towards p53/TP53. {ECO:0000269|PubMed:11742995, CC ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:16387653, CC ECO:0000269|PubMed:18794358, ECO:0000269|PubMed:23431171, CC ECO:0000269|Ref.27}. CC -!- INTERACTION: CC Q92794; PRO_0000390950 [Q03164]: KMT2A; NbExp=10; IntAct=EBI-948013, EBI-2638616; CC Q92794; P61964: WDR5; NbExp=4; IntAct=EBI-948013, EBI-540834; CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus, CC nucleoplasm. Nucleus, PML body. Note=Recruited into PML body after DNA CC damage. CC -!- DOMAIN: The N-terminus is involved in transcriptional activation while CC the C-terminus is involved in transcriptional repression. CC {ECO:0000269|PubMed:11313971}. CC -!- PTM: Autoacetylation at Lys-604 is required for proper function (By CC similarity). Autoacetylated. {ECO:0000250|UniProtKB:Q9H7Z6, CC ECO:0000269|Ref.27}. CC -!- PTM: Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction CC with PML and negatively regulates its acetylation activity towards CC p53/TP53. {ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:23431171}. CC -!- DISEASE: Note=Chromosomal aberrations involving KAT6A may be a cause of CC acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP CC (PubMed:8782817). Translocation t(8;22)(p11;q13) with EP300 CC (PubMed:10824998). KAT6A-CREBBP may induce leukemia by inhibiting CC RUNX1-mediated transcription (PubMed:11742995). Inversion CC inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of CC the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. CC KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription CC activation (PubMed:12676584). {ECO:0000269|PubMed:10824998, CC ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:12676584, CC ECO:0000269|PubMed:8782817}. CC -!- DISEASE: Note=A chromosomal aberration involving KAT6A is a cause of CC therapy-related myelodysplastic syndrome. Translocation CC t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein. CC {ECO:0000269|Ref.3}. CC -!- DISEASE: Arboleda-Tham syndrome (ARTHS) [MIM:616268]: An autosomal CC dominant disorder characterized by intellectual disability, dysmorphic CC facial features, delayed psychomotor development, and lack of speech. CC {ECO:0000269|PubMed:25728775, ECO:0000269|PubMed:25728777}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/25/MYST3"; 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; U47742; AAC50662.1; -; mRNA. DR EMBL; AC090571; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB084281; BAD00088.1; ALT_TERM; mRNA. DR CCDS; CCDS6124.1; -. DR RefSeq; NP_006757.2; NM_006766.4. DR RefSeq; XP_016869352.1; XM_017013863.1. DR RefSeq; XP_016869353.1; XM_017013864.1. DR PDB; 1M36; NMR; -; A=533-563. DR PDB; 2LN0; NMR; -; A=204-313. DR PDB; 2OZU; X-ray; 2.30 A; A=497-780. DR PDB; 2RC4; X-ray; 3.00 A; A=501-784. DR PDB; 3V43; X-ray; 1.47 A; A=204-313. DR PDB; 4LJN; X-ray; 3.00 A; A=194-323. DR PDB; 4LK9; X-ray; 1.60 A; A=194-323. DR PDB; 4LKA; X-ray; 1.61 A; A=194-323. DR PDB; 4LLB; X-ray; 2.50 A; A/B=194-323. DR PDB; 5B75; X-ray; 1.70 A; A=194-323. DR PDB; 5B76; X-ray; 1.65 A; A=194-323. DR PDB; 5B77; X-ray; 1.55 A; A=194-323. DR PDB; 5B78; X-ray; 1.40 A; A=194-323. DR PDB; 6LSB; X-ray; 2.00 A; A=194-323. DR PDB; 7Y43; X-ray; 1.50 A; A=1-85. DR PDB; 8DD5; X-ray; 2.58 A; A=501-784. DR PDB; 8H7A; X-ray; 1.92 A; A/B/E/F=1-85. DR PDBsum; 1M36; -. DR PDBsum; 2LN0; -. DR PDBsum; 2OZU; -. DR PDBsum; 2RC4; -. DR PDBsum; 3V43; -. DR PDBsum; 4LJN; -. DR PDBsum; 4LK9; -. DR PDBsum; 4LKA; -. DR PDBsum; 4LLB; -. DR PDBsum; 5B75; -. DR PDBsum; 5B76; -. DR PDBsum; 5B77; -. DR PDBsum; 5B78; -. DR PDBsum; 6LSB; -. DR PDBsum; 7Y43; -. DR PDBsum; 8DD5; -. DR PDBsum; 8H7A; -. DR AlphaFoldDB; Q92794; -. DR BMRB; Q92794; -. DR SMR; Q92794; -. DR BioGRID; 113703; 104. DR ComplexPortal; CPX-727; MOZ1 histone acetyltransferase complex. DR ComplexPortal; CPX-733; MOZ2 histone acetyltransferase complex. DR ComplexPortal; CPX-736; MOZ3 histone acetyltransferase complex. DR CORUM; Q92794; -. DR IntAct; Q92794; 26. DR MINT; Q92794; -. DR STRING; 9606.ENSP00000265713; -. DR BindingDB; Q92794; -. DR ChEMBL; CHEMBL3774298; -. DR GlyCosmos; Q92794; 4 sites, 1 glycan. DR GlyGen; Q92794; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; Q92794; -. DR PhosphoSitePlus; Q92794; -. DR SwissPalm; Q92794; -. DR BioMuta; KAT6A; -. DR DMDM; 215274095; -. DR EPD; Q92794; -. DR jPOST; Q92794; -. DR MassIVE; Q92794; -. DR MaxQB; Q92794; -. DR PaxDb; 9606-ENSP00000380136; -. DR PeptideAtlas; Q92794; -. DR ProteomicsDB; 75473; -. DR Pumba; Q92794; -. DR Antibodypedia; 23986; 153 antibodies from 29 providers. DR DNASU; 7994; -. DR Ensembl; ENST00000265713.8; ENSP00000265713.2; ENSG00000083168.11. DR Ensembl; ENST00000396930.4; ENSP00000380136.3; ENSG00000083168.11. DR GeneID; 7994; -. DR KEGG; hsa:7994; -. DR MANE-Select; ENST00000265713.8; ENSP00000265713.2; NM_006766.5; NP_006757.2. DR UCSC; uc003xon.4; human. DR AGR; HGNC:13013; -. DR CTD; 7994; -. DR DisGeNET; 7994; -. DR GeneCards; KAT6A; -. DR HGNC; HGNC:13013; KAT6A. DR HPA; ENSG00000083168; Low tissue specificity. DR MalaCards; KAT6A; -. DR MIM; 601408; gene. DR MIM; 616268; phenotype. DR neXtProt; NX_Q92794; -. DR OpenTargets; ENSG00000083168; -. DR Orphanet; 370026; Acute myeloid leukemia with t(8;16)(p11;p13) translocation. DR Orphanet; 457193; Autosomal dominant intellectual disability-craniofacial anomalies-cardiac defects syndrome. DR PharmGKB; PA37592; -. DR VEuPathDB; HostDB:ENSG00000083168; -. DR eggNOG; KOG2747; Eukaryota. DR GeneTree; ENSGT00940000156962; -. DR HOGENOM; CLU_001232_0_1_1; -. DR InParanoid; Q92794; -. DR OrthoDB; 118560at2759; -. DR PhylomeDB; Q92794; -. DR TreeFam; TF106483; -. DR BRENDA; 2.3.1.48; 2681. DR PathwayCommons; Q92794; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation. DR SignaLink; Q92794; -. DR SIGNOR; Q92794; -. DR BioGRID-ORCS; 7994; 84 hits in 1100 CRISPR screens. DR ChiTaRS; KAT6A; human. DR EvolutionaryTrace; Q92794; -. DR GeneWiki; MYST3; -. DR GenomeRNAi; 7994; -. DR Pharos; Q92794; Tchem. DR PRO; PR:Q92794; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q92794; Protein. DR Bgee; ENSG00000083168; Expressed in nipple and 220 other cell types or tissues. DR ExpressionAtlas; Q92794; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0000786; C:nucleosome; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; IDA:UniProtKB. DR GO; GO:0016407; F:acetyltransferase activity; TAS:Reactome. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0036408; F:histone H3K14 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043997; F:histone H4K12 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043995; F:histone H4K5 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0043996; F:histone H4K8 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0090398; P:cellular senescence; IMP:UniProtKB. DR GO; GO:0051276; P:chromosome organization; TAS:ProtInc. 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:0006334; P:nucleosome assembly; IEA:InterPro. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB. DR GO; GO:0050793; P:regulation of developmental process; NAS:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:ComplexPortal. DR GO; GO:1903706; P:regulation of hemopoiesis; NAS:ComplexPortal. DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome. DR CDD; cd04301; NAT_SF; 1. DR CDD; cd15618; PHD1_MOZ_MORF; 1. DR CDD; cd15527; PHD2_KAT6A_6B; 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; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR IDEAL; IID00489; -. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR002717; HAT_MYST-type. DR InterPro; IPR005818; Histone_H1/H5_H15. DR InterPro; IPR048589; SAMD1-like_WH. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR InterPro; IPR040706; Zf-MYST. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10615:SF26; HISTONE ACETYLTRANSFERASE KAT6A; 1. DR Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF00628; PHD; 2. DR Pfam; PF21524; SAMD1_WH; 1. DR Pfam; PF17772; zf-MYST; 1. DR SMART; SM00526; H15; 1. DR SMART; SM00249; PHD; 2. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS51504; H15; 1. DR PROSITE; PS51726; MYST_HAT; 1. DR PROSITE; PS52014; SAMD1_WH; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 2. DR Genevisible; Q92794; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Acyltransferase; Chromatin regulator; KW Chromosomal rearrangement; Intellectual disability; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; KW Repeat; Repressor; Transcription; Transcription regulation; Transferase; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..2004 FT /note="Histone acetyltransferase KAT6A" FT /id="PRO_0000051572" FT DOMAIN 1..77 FT /note="SAMD1-like winged helix (WH)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01358" FT DOMAIN 95..171 FT /note="H15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837" FT DOMAIN 504..778 FT /note="MYST-type HAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063" FT ZN_FING 206..265 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 259..313 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 537..562 FT /note="C2HC MYST-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063" FT REGION 1..144 FT /note="Required for activation of RUNX1-1" FT REGION 52..166 FT /note="Required for nuclear localization" FT REGION 144..664 FT /note="Interaction with PML" FT /evidence="ECO:0000269|PubMed:23431171" FT REGION 312..664 FT /note="Interaction with RUNX1-1" FT REGION 334..375 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 441..464 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 488..778 FT /note="Catalytic" FT REGION 507..810 FT /note="Mediates interaction with BRPF1, required for FT histone H3 acetyltransferase activity" FT /evidence="ECO:0000269|PubMed:18794358" FT REGION 785..1445 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1461..1621 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1517..1741 FT /note="Interaction with PML" FT /evidence="ECO:0000269|PubMed:23431171" FT REGION 1517..1642 FT /note="Interaction with RUNX1-2" FT REGION 1637..1721 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1913..1948 FT /note="Required for activation of RUNX1-2" FT COMPBIAS 339..353 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 786..803 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 804..832 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 842..862 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 873..888 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 889..926 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 930..946 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 952..987 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1011..1029 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1124..1148 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1149..1171 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1201..1226 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1227..1245 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1271..1286 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1287..1320 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1321..1347 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1355..1369 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1390..1420 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1423..1437 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1478..1621 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1646..1701 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 680 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6" FT BINDING 645..649 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|Ref.27" FT BINDING 654..660 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|Ref.27" FT BINDING 684 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|Ref.27" FT SITE 813..814 FT /note="Breakpoint for translocation to form KAT6A-ASXL2" FT SITE 1117..1118 FT /note="Breakpoint for translocation to form KAT6A-EP300 and FT KAT6A-NCOA2" FT SITE 1546..1547 FT /note="Breakpoint for translocation to form KAT6A-CREBBP" FT MOD_RES 172 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BZ21" FT MOD_RES 350 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 355 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 369 FT /note="Phosphothreonine; by PKB/AKT1" FT /evidence="ECO:0000269|PubMed:23431171" FT MOD_RES 420 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 473 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 604 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000269|Ref.27" FT MOD_RES 787 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BZ21" FT MOD_RES 812 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 815 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BZ21" FT MOD_RES 899 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q5TKR9" FT MOD_RES 941 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 954 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 974 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1007 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1089 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1090 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 834 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1342 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 134 FT /note="L -> S (in dbSNP:rs3824276)" FT /id="VAR_047548" FT MUTAGEN 543 FT /note="C->G: Abrogates HAT activity." FT /evidence="ECO:0000269|PubMed:12676584" FT MUTAGEN 545 FT /note="K->A: Reduced affinity for DNA." FT /evidence="ECO:0000269|PubMed:17925393" FT MUTAGEN 657 FT /note="G->E: Abrogates HAT activity." FT /evidence="ECO:0000269|PubMed:12676584" FT MUTAGEN 727 FT /note="I->E: Slightly reduced affinity for DNA." FT /evidence="ECO:0000269|PubMed:17925393" FT MUTAGEN 732 FT /note="H->D: Reduced affinity for DNA." FT /evidence="ECO:0000269|PubMed:17925393" FT CONFLICT 401 FT /note="K -> R (in Ref. 1; AAC50662 and 3; BAD00088)" FT /evidence="ECO:0000305" FT HELIX 7..22 FT /evidence="ECO:0007829|PDB:7Y43" FT HELIX 29..40 FT /evidence="ECO:0007829|PDB:7Y43" FT HELIX 44..56 FT /evidence="ECO:0007829|PDB:7Y43" FT STRAND 59..65 FT /evidence="ECO:0007829|PDB:7Y43" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:7Y43" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:5B78" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:5B76" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:5B78" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:5B78" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:5B78" FT HELIX 239..242 FT /evidence="ECO:0007829|PDB:5B78" FT HELIX 246..252 FT /evidence="ECO:0007829|PDB:5B78" FT TURN 253..256 FT /evidence="ECO:0007829|PDB:5B78" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:5B78" FT TURN 266..268 FT /evidence="ECO:0007829|PDB:5B78" FT HELIX 275..277 FT /evidence="ECO:0007829|PDB:5B78" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:4LK9" FT TURN 282..284 FT /evidence="ECO:0007829|PDB:5B78" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:4LK9" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:5B78" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:5B78" FT TURN 308..310 FT /evidence="ECO:0007829|PDB:5B78" FT STRAND 511..514 FT /evidence="ECO:0007829|PDB:2OZU" FT STRAND 517..520 FT /evidence="ECO:0007829|PDB:2OZU" FT HELIX 529..532 FT /evidence="ECO:0007829|PDB:2RC4" FT STRAND 535..539 FT /evidence="ECO:0007829|PDB:2OZU" FT TURN 541..543 FT /evidence="ECO:0007829|PDB:2OZU" FT STRAND 546..549 FT /evidence="ECO:0007829|PDB:2OZU" FT HELIX 550..559 FT /evidence="ECO:0007829|PDB:2OZU" FT STRAND 566..573 FT /evidence="ECO:0007829|PDB:2OZU" FT STRAND 576..582 FT /evidence="ECO:0007829|PDB:2OZU" FT TURN 583..585 FT /evidence="ECO:0007829|PDB:2OZU" FT HELIX 587..598 FT /evidence="ECO:0007829|PDB:2OZU" FT STRAND 613..622 FT /evidence="ECO:0007829|PDB:2OZU" FT STRAND 625..637 FT /evidence="ECO:0007829|PDB:2OZU" FT STRAND 642..649 FT /evidence="ECO:0007829|PDB:2OZU" FT HELIX 651..653 FT /evidence="ECO:0007829|PDB:2OZU" FT STRAND 655..657 FT /evidence="ECO:0007829|PDB:2RC4" FT HELIX 658..672 FT /evidence="ECO:0007829|PDB:2OZU" FT STRAND 677..679 FT /evidence="ECO:0007829|PDB:2OZU" FT HELIX 685..705 FT /evidence="ECO:0007829|PDB:2OZU" FT HELIX 713..720 FT /evidence="ECO:0007829|PDB:2OZU" FT HELIX 724..733 FT /evidence="ECO:0007829|PDB:2OZU" FT HELIX 750..759 FT /evidence="ECO:0007829|PDB:2OZU" FT HELIX 771..773 FT /evidence="ECO:0007829|PDB:2OZU" SQ SEQUENCE 2004 AA; 225028 MW; 78357EFAC4698A5F CRC64; MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQNVDWN KLIKRAVEGL AESGGSTLKS IERFLKGQKD VSALFGGSAA SGFHQQLRLA IKRAIGHGRL LKDGPLYRLN TKATNVDGKE SCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKKPEELISC ADCGNSGHPS CLKFSPELTV RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YTNPIGRPKN RLKKQNTVSK GPFSKVRTGP GRGRKRKITL SSQSASSSSE EGYLERIDGL DFCRDSNVSL KFNKKTKGLI DGLTKFFTPS PDGRKARGEV VDYSEQYRIR KRGNRKSSTS DWPTDNQDGW DGKQENEERL FGSQEIMTEK DMELFRDIQE QALQKVGVTG PPDPQVRCPS VIEFGKYEIH TWYSSPYPQE YSRLPKLYLC EFCLKYMKSR TILQQHMKKC GWFHPPANEI YRKNNISVFE VDGNVSTIYC QNLCLLAKLF LDHKTLYYDV EPFLFYVLTQ NDVKGCHLVG YFSKEKHCQQ KYNVSCIMIL PQYQRKGYGR FLIDFSYLLS KREGQAGSPE KPLSDLGRLS YMAYWKSVIL ECLYHQNDKQ ISIKKLSKLT GICPQDITST LHHLRMLDFR SDQFVIIRRE KLIQDHMAKL QLNLRPVDVD PECLRWTPVI VSNSVVSEEE EEEAEEGENE EPQCQERELE ISVGKSVSHE NKEQDSYSVE SEKKPEVMAP VSSTRLSKQV LPHDSLPANS QPSRRGRWGR KNRKTQERFG DKDSKLLLEE TSSAPQEQYG ECGEKSEATQ EQYTESEEQL VASEEQPSQD GKPDLPKRRL SEGVEPWRGQ LKKSPEALKC RLTEGSERLP RRYSEGDRAV LRGFSESSEE EEEPESPRSS SPPILTKPTL KRKKPFLHRR RRVRKRKHHN SSVVTETISE TTEVLDEPFE DSDSERPMPR LEPTFEIDEE EEEEDENELF PREYFRRLSS QDVLRCQSSS KRKSKDEEED EESDDADDTP ILKPVSLLRK RDVKNSPLEP DTSTPLKKKK GWPKGKSRKP IHWKKRPGRK PGFKLSREIM PVSTQACVIE PIVSIPKAGR KPKIQESEET VEPKEDMPLP EERKEEEEMQ AEAEEAEEGE EEDAASSEVP AASPADSSNS PETETKEPEV EEEEEKPRVS EEQRQSEEEQ QELEEPEPEE EEDAAAETAQ NDDHDADDED DGHLESTKKK ELEEQPTRED VKEEPGVQES FLDANMQKSR EKIKDKEETE LDSEEEQPSH DTSVVSEQMA GSEDDHEEDS HTKEELIELK EEEEIPHSEL DLETVQAVQS LTQEESSEHE GAYQDCEETL AACQTLQSYT QADEDPQMSM VEDCHASEHN SPISSVQSHP SQSVRSVSSP NVPALESGYT QISPEQGSLS APSMQNMETS PMMDVPSVSD HSQQVVDSGF SDLGSIESTT ENYENPSSYD STMGGSICGN SSSQSSCSYG GLSSSSSLTQ SSCVVTQQMA SMGSSCSMMQ QSSVQPAANC SIKSPQSCVV ERPPSNQQQQ PPPPPPQQPQ PPPPQPQPAP QPPPPQQQPQ QQPQPQPQQP PPPPPPQQQP PLSQCSMNNS FTPAPMIMEI PESGSTGNIS IYERIPGDFG AGSYSQPSAT FSLAKLQQLT NTIMDPHAMP YSHSPAVTSY ATSVSLSNTG LAQLAPSHPL AGTPQAQATM TPPPNLASTT MNLTSPLLQC NMSATNIGIP HTQRLQGQMP VKGHISIRSK SAPLPSAAAH QQQLYGRSPS AVAMQAGPRA LAVQRGMNMG VNLMPTPAYN VNSMNMNTLN AMNSYRMTQP MMNSSYHSNP AYMNQTAQYP MQMQMGMMGS QAYTQQPMQP NPHGNMMYTG PSHHSYMNAA GVPKQSLNGP YMRR //