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 01-OCT-2014, entry version 157. DE RecName: Full=Histone acetyltransferase KAT6A; DE EC=2.3.1.48; 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA 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., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA 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 RP WITH 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 RP WITH 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 RT in acute myeloid leukemia."; RL Blood 91:3127-3133(1998). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1111-1128, AND CHROMOSOMAL TRANSLOCATION RP WITH 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, ENZYME 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 RT the MOZ-CBP fusion protein."; RL EMBO J. 20:7184-7196(2001). RN [7] RP ENZYME 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 RT and 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., RA Bellodi C., Kalkhoven E., Salomoni P., Pelicci P.G., Minucci S., RA Heery D.M.; RT "MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by RT impairment 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, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., 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 RP BY 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 RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350; LYS-355 AND LYS-1007, RP AND 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., RA Walther T.C., 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP FUNCTION, INTERACTION WITH PML AND TP53, AND PHOSPHORYLATION AT RP THR-369. RX PubMed=23431171; DOI=10.1073/pnas.1300490110; RA Rokudai S., Laptenko O., Arnal S.M., Taya Y., Kitabayashi I., RA Prives C.; RT "MOZ increases p53 acetylation and premature senescence through its RT complex formation with PML."; RL Proc. Natl. Acad. Sci. U.S.A. 110:3895-3900(2013). RN [20] 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 [21] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 501-784 IN COMPLEXES WITH RP ACETYL COENZYME A; HISTONE H3 AND HISTONE H4 AND ZINC IONS, FUNCTION, RP CATALYTIC ACTIVITY, DNA-BINDING, AND MUTAGENESIS OF LYS-545; ILE-727 RP 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 RT domain contains DNA-binding activity implicated in chromatin RT targeting."; RL J. Biol. Chem. 282:36603-36613(2007). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 497-780 IN COMPLEX WITH RP ACETYLCOENZYME A. RG Structural genomics consortium (SGC); RT "The crystal structure of human MYST histone acetyltransferase 3 in RT complex with acetylcoenzyme A."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Histone acetyltransferase that acetylates lysine CC residues in histone H3 and histone H4 (in vitro). Component of the CC MOZ/MORF complex which has a histone H3 acetyltransferase CC activity. May act as a transcriptional coactivator for RUNX1 and CC RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls CC its transcriptional activity via association with PML. CC {ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:11965546, CC ECO:0000269|PubMed:12771199, ECO:0000269|PubMed:16387653, CC ECO:0000269|PubMed:17925393, ECO:0000269|PubMed:23431171}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl- CC [histone]. {ECO:0000269|PubMed:11313971, CC ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:17925393}. CC -!- SUBUNIT: Component of the MOZ/MORF complex composed at least of CC ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. CC Interacts with RUNX1; phosphorylation of RUNX1 enhances the CC interaction. Interacts with RUNX2. Interacts with p53/TP53. CC Interacts with PML (isoform PML-4) and this interaction positively CC regulates its acetylation activity towards p53/TP53. CC {ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:11965546, CC ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358, CC ECO:0000269|PubMed:23431171, ECO:0000269|Ref.22}. CC -!- INTERACTION: CC Q03164:KMT2A; NbExp=10; IntAct=EBI-948013, EBI-2638616; CC 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 CC DNA damage. CC -!- DOMAIN: The N-terminus is involved in transcriptional activation CC while the C-terminus is involved in transcriptional repression. CC {ECO:0000269|PubMed:11313971}. CC -!- PTM: Autoacetylation at Lys-604 is required for proper function CC (By similarity). Autoacetylated. {ECO:0000250}. CC -!- PTM: Phosphorylation at Thr-369 by PKB/AKT1 inhibits its CC interaction with PML and negatively regulates its acetylation CC activity towards p53/TP53. {ECO:0000269|PubMed:11742995, CC ECO:0000269|PubMed:18669648, ECO:0000269|PubMed:19608861, CC ECO:0000269|PubMed:19690332, ECO:0000269|PubMed:20068231, CC ECO:0000269|PubMed:23431171}. CC -!- DISEASE: Note=Chromosomal aberrations involving KAT6A may be a CC cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) CC with CREBBP; translocation t(8;22)(p11;q13) with EP300. KAT6A- CC CREBBP may induce leukemia by inhibiting RUNX1-mediated CC transcription. Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 CC oncogene, which consists of the N-terminal part of KAT6A and the CC C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and CC disrupts its function in transcription activation. CC -!- DISEASE: Note=A chromosomal aberration involving KAT6A is a cause CC of therapy-related myelodysplastic syndrome. Translocation CC t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion CC protein. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 C2HC-type zinc finger. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00837}. CC -!- SIMILARITY: Contains 1 MYST-type HAT (histone acetyltransferase) CC domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 PHD-type zinc fingers. CC {ECO:0000255|PROSITE-ProRule:PRU00146}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/MYST3ID25ch8p11.html"; 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_001092882.1; NM_001099412.1. DR RefSeq; NP_001092883.1; NM_001099413.1. DR RefSeq; NP_006757.2; NM_006766.3. DR UniGene; Hs.491577; -. 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 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 ProteinModelPortal; Q92794; -. DR SMR; Q92794; 204-313, 507-779. DR BioGrid; 113703; 30. DR IntAct; Q92794; 6. DR STRING; 9606.ENSP00000265713; -. DR PhosphoSite; Q92794; -. DR DMDM; 215274095; -. DR MaxQB; Q92794; -. DR PaxDb; Q92794; -. DR PRIDE; Q92794; -. DR DNASU; 7994; -. DR Ensembl; ENST00000265713; ENSP00000265713; ENSG00000083168. DR Ensembl; ENST00000396930; ENSP00000380136; ENSG00000083168. DR Ensembl; ENST00000406337; ENSP00000385888; ENSG00000083168. DR GeneID; 7994; -. DR KEGG; hsa:7994; -. DR UCSC; uc003xon.4; human. DR CTD; 7994; -. DR GeneCards; GC08M041786; -. DR HGNC; HGNC:13013; KAT6A. DR HPA; CAB017023; -. DR HPA; HPA049811; -. DR HPA; HPA053523; -. DR MIM; 601408; gene. DR neXtProt; NX_Q92794; -. DR Orphanet; 370026; Acute myeloid leukemia with t(8;16)(p11;p13) translocation. DR PharmGKB; PA37592; -. DR eggNOG; COG5027; -. DR HOGENOM; HOG000234365; -. DR HOVERGEN; HBG052563; -. DR InParanoid; Q92794; -. DR KO; K11305; -. DR OMA; GAYQDCE; -. DR OrthoDB; EOG7WHH8N; -. DR PhylomeDB; Q92794; -. DR TreeFam; TF106483; -. DR Reactome; REACT_172610; HATs acetylate histones. DR ChiTaRS; KAT6A; human. DR EvolutionaryTrace; Q92794; -. DR GeneWiki; MYST3; -. DR GenomeRNAi; 7994; -. DR NextBio; 30540; -. DR PRO; PR:Q92794; -. DR ArrayExpress; Q92794; -. DR Bgee; Q92794; -. DR CleanEx; HS_MYST3; -. DR Genevestigator; Q92794; -. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; TAS:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl. DR GO; GO:0090398; P:cellular senescence; IMP:UniProtKB. DR GO; GO:0006325; P:chromatin organization; TAS:Reactome. DR GO; GO:0006323; P:DNA packaging; TAS:ProtInc. DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl. DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl. DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl. DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB. DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB. DR GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB. DR GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB. DR GO; GO:0035019; P:somatic stem cell maintenance; IEA:Ensembl. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 2. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR005818; Histone_H1/H5_H15. DR InterPro; IPR002717; MOZ_SAS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF00628; PHD; 1. DR SMART; SM00526; H15; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00184; RING; 2. DR SUPFAM; SSF55729; SSF55729; 1. DR SUPFAM; SSF57903; SSF57903; 2. DR PROSITE; PS51504; H15; 1. DR PROSITE; PS51726; MYST_HAT; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Acyltransferase; KW Chromatin regulator; Chromosomal rearrangement; Complete proteome; KW Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Transferase; Zinc; Zinc-finger. FT CHAIN 1 2004 Histone acetyltransferase KAT6A. FT /FTId=PRO_0000051572. FT DOMAIN 95 171 H15. {ECO:0000255|PROSITE- FT ProRule:PRU00837}. FT DOMAIN 504 778 MYST-type HAT. FT ZN_FING 206 265 PHD-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU00146}. FT ZN_FING 259 313 PHD-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00146}. FT ZN_FING 538 560 C2HC-type. FT REGION 1 144 Required for activation of RUNX1-1. FT REGION 52 166 Required for nuclear localization. FT REGION 144 664 Interaction with PML. FT REGION 312 664 Interaction with RUNX1-1. FT REGION 488 778 Catalytic. FT REGION 507 810 Mediates interaction with BRPF1, required FT for histone H3 acetyltransferase FT activity. FT REGION 645 649 Acetyl-CoA binding. FT REGION 654 660 Acetyl-CoA binding. FT REGION 1517 1741 Interaction with PML. FT REGION 1517 1642 Interaction with RUNX1-2. FT REGION 1913 1948 Required for activation of RUNX1-2. FT COMPBIAS 371 379 Poly-Ser. FT COMPBIAS 788 801 Poly-Glu. FT COMPBIAS 989 995 Poly-Glu. FT COMPBIAS 1019 1026 Poly-Arg. FT COMPBIAS 1069 1078 Poly-Glu. FT COMPBIAS 1147 1150 Poly-Lys. FT COMPBIAS 1221 1242 Glu-rich. FT COMPBIAS 1267 1302 Glu-rich. FT COMPBIAS 1411 1414 Poly-Glu. FT COMPBIAS 1593 1597 Poly-Ser. FT COMPBIAS 1643 1704 Gln/Pro-rich. FT COMPBIAS 1897 1977 Met-rich. FT ACT_SITE 604 604 {ECO:0000250}. FT ACT_SITE 646 646 Nucleophile. {ECO:0000250}. FT BINDING 684 684 Acetyl-CoA. FT SITE 813 814 Breakpoint for translocation to form FT KAT6A-ASXL2. FT SITE 1117 1118 Breakpoint for translocation to form FT KAT6A-EP300 and KAT6A-NCOA2. FT SITE 1546 1547 Breakpoint for translocation to form FT KAT6A-CREBBP. FT MOD_RES 172 172 N6-acetyllysine. {ECO:0000250}. FT MOD_RES 350 350 N6-acetyllysine. FT {ECO:0000269|PubMed:11742995, FT ECO:0000269|PubMed:19608861}. FT MOD_RES 355 355 N6-acetyllysine. FT {ECO:0000269|PubMed:11742995, FT ECO:0000269|PubMed:19608861}. FT MOD_RES 369 369 Phosphothreonine; by PKB/AKT1. FT {ECO:0000269|PubMed:23431171}. FT MOD_RES 473 473 Phosphoserine. FT {ECO:0000269|PubMed:20068231}. FT MOD_RES 604 604 N6-acetyllysine; by autocatalysis. FT {ECO:0000250}. FT MOD_RES 815 815 N6-acetyllysine. {ECO:0000250}. FT MOD_RES 899 899 Phosphotyrosine. {ECO:0000250}. FT MOD_RES 1007 1007 N6-acetyllysine. FT {ECO:0000269|PubMed:11742995, FT ECO:0000269|PubMed:19608861}. FT MOD_RES 1113 1113 Phosphoserine. FT {ECO:0000269|PubMed:18669648, FT ECO:0000269|PubMed:19690332, FT ECO:0000269|PubMed:20068231}. FT VARIANT 134 134 L -> S (in dbSNP:rs3824276). FT /FTId=VAR_047548. FT MUTAGEN 543 543 C->G: Abrogates HAT activity. FT {ECO:0000269|PubMed:12676584}. FT MUTAGEN 545 545 K->A: Reduced affinity for DNA. FT {ECO:0000269|PubMed:17925393}. FT MUTAGEN 657 657 G->E: Abrogates HAT activity. FT {ECO:0000269|PubMed:12676584}. FT MUTAGEN 727 727 I->E: Slightly reduced affinity for DNA. FT {ECO:0000269|PubMed:17925393}. FT MUTAGEN 732 732 H->D: Reduced affinity for DNA. FT {ECO:0000269|PubMed:17925393}. FT CONFLICT 401 401 K -> R (in Ref. 1; AAC50662 and 3; FT BAD00088). {ECO:0000305}. FT HELIX 195 198 FT STRAND 207 209 FT TURN 210 212 FT TURN 231 233 FT HELIX 239 242 FT HELIX 246 253 FT TURN 260 262 FT TURN 266 268 FT HELIX 275 277 FT STRAND 278 280 FT TURN 282 284 FT STRAND 287 289 FT HELIX 290 292 FT STRAND 293 295 FT TURN 308 310 FT STRAND 511 514 FT STRAND 517 520 FT HELIX 529 532 FT STRAND 535 539 FT TURN 541 543 FT STRAND 546 549 FT HELIX 550 559 FT STRAND 566 573 FT STRAND 576 582 FT TURN 583 585 FT HELIX 587 598 FT STRAND 613 622 FT STRAND 625 637 FT STRAND 642 649 FT HELIX 651 653 FT STRAND 655 657 FT HELIX 658 672 FT STRAND 677 679 FT HELIX 685 705 FT HELIX 713 720 FT HELIX 724 733 FT HELIX 750 759 FT HELIX 771 773 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 //