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Histone acetyltransferase KAT6A (EC 2.3.1.48) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3) (MYST-3) (Monocytic leukemia zinc finger protein) (Runt-related transcription factor-binding protein 2) (Zinc finger protein 220)

 KAT6A_HUMAN             Reviewed;        2004 AA.
Q92794; Q76L81;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
25-OCT-2017, entry version 190.
RecName: Full=Histone acetyltransferase KAT6A;
EC=2.3.1.48 {ECO:0000269|PubMed:11313971, ECO:0000269|PubMed:11742995};
AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3;
Short=MYST-3;
AltName: Full=Monocytic leukemia zinc finger protein;
AltName: Full=Runt-related transcription factor-binding protein 2;
AltName: Full=Zinc finger protein 220;
Name=KAT6A; Synonyms=MOZ, MYST3, RUNXBP2, ZNF220;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION WITH CREBBP.
PubMed=8782817; DOI=10.1038/ng0996-33;
Borrow J., Stanton V.P. Jr., Andresen J.M., Becher R., Behm F.G.,
Chaganti R.S.K., Civin C.I., Disteche C., Dube I., Frischauf A.M.,
Horsman D., Mitelman F., Volinia S., Watmore A.E., Housman D.E.;
"The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a
putative acetyltransferase to the CREB-binding protein.";
Nat. Genet. 14:33-41(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-813, AND CHROMOSOMAL TRANSLOCATION
WITH ASXL2.
TISSUE=Bone marrow;
Hosoda F., Kitabayashi I., Kakazu N., Fukushima M., Aikawa Y., Abe T.,
Hibi S., Yagi T., Ohki M.;
"MOZ is fused to a novel Polycomb group gene in a therapy-related
myelodysplastic syndrome with t(2;8)(p23;p11.2).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1089-1117, AND CHROMOSOMAL TRANSLOCATION
WITH NCOA2.
PubMed=9558366;
Carapeti M., Aguiar R.C.T., Goldman J.M., Cross N.C.P.;
"A novel fusion between MOZ and the nuclear receptor coactivator TIF2
in acute myeloid leukemia.";
Blood 91:3127-3133(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1111-1128, AND CHROMOSOMAL TRANSLOCATION
WITH EP300.
PubMed=10824998;
DOI=10.1002/(SICI)1098-2264(200006)28:2<138::AID-GCC2>3.0.CO;2-2;
Chaffanet M., Gressin L., Preudhomme C., Soenen-Cornu V., Birnbaum D.,
Pebusque M.-J.;
"MOZ is fused to p300 in an acute monocytic leukemia with t(8;22).";
Genes Chromosomes Cancer 28:138-144(2000).
[6]
INTERACTION WITH RUNX1, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
ACETYLATION, CHROMOSOMAL TRANSLOCATION WITH CREBBP, AND FUNCTION.
PubMed=11742995; DOI=10.1093/emboj/20.24.7184;
Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.;
"Activation of AML1-mediated transcription by MOZ and inhibition by
the MOZ-CBP fusion protein.";
EMBO J. 20:7184-7196(2001).
[7]
CATALYTIC ACTIVITY, AND DOMAIN.
PubMed=11313971; DOI=10.1038/sj.onc.1204114;
Champagne N., Pelletier N., Yang X.-J.;
"The monocytic leukemia zinc finger protein MOZ is a histone
acetyltransferase.";
Oncogene 20:404-409(2001).
[8]
INTERACTION WITH RUNX2, AND FUNCTION.
PubMed=11965546; DOI=10.1038/sj.onc.1205367;
Pelletier N., Champagne N., Stifani S., Yang X.-J.;
"MOZ and MORF histone acetyltransferases interact with the Runt-domain
transcription factor Runx2.";
Oncogene 21:2729-2740(2002).
[9]
CHROMOSOMAL TRANSLOCATION WITH NCOA2, AND MUTAGENESIS OF CYS-543 AND
GLY-657.
PubMed=12676584; DOI=10.1016/S1535-6108(03)00051-5;
Deguchi K., Ayton P.M., Carapeti M., Kutok J.L., Snyder C.S.,
Williams I.R., Cross N.C.P., Glass C.K., Cleary M.L., Gilliland D.G.;
"MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome
binding motif and TIF2-mediated recruitment of CBP.";
Cancer Cell 3:259-271(2003).
[10]
FUNCTION.
PubMed=12771199; DOI=10.1093/nar/gkg401;
Bristow C.A.P., Shore P.;
"Transcriptional regulation of the human MIP-1alpha promoter by RUNX1
and MOZ.";
Nucleic Acids Res. 31:2735-2744(2003).
[11]
SUBCELLULAR LOCATION, AND CHROMOSOMAL TRANSLOCATION WITH NCOA2.
PubMed=15657427; DOI=10.1128/MCB.25.3.988-1002.2005;
Kindle K.B., Troke P.J.F., Collins H.M., Matsuda S., Bossi D.,
Bellodi C., Kalkhoven E., Salomoni P., Pelicci P.G., Minucci S.,
Heery D.M.;
"MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by
impairment of CBP function.";
Mol. Cell. Biol. 25:988-1002(2005).
[12]
FUNCTION, AND IDENTIFICATION IN THE MOZ/MORF COMPLEX.
PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
Lane W.S., Tan S., Yang X.-J., Cote J.;
"ING tumor suppressor proteins are critical regulators of chromatin
acetylation required for genome expression and perpetuation.";
Mol. Cell 21:51-64(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[14]
IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, AND
SUBCELLULAR LOCATION.
PubMed=18794358; DOI=10.1128/MCB.01297-08;
Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C.,
Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J.,
Yang X.-J.;
"Molecular architecture of quartet MOZ/MORF histone acetyltransferase
complexes.";
Mol. Cell. Biol. 28:6828-6843(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350; LYS-355 AND LYS-1007,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-1113, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420; SER-473; SER-812;
SER-941; SER-954; SER-974; SER-1089; SER-1090 AND SER-1113, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
FUNCTION, INTERACTION WITH PML AND TP53, AND PHOSPHORYLATION AT
THR-369.
PubMed=23431171; DOI=10.1073/pnas.1300490110;
Rokudai S., Laptenko O., Arnal S.M., Taya Y., Kitabayashi I.,
Prives C.;
"MOZ increases p53 acetylation and premature senescence through its
complex formation with PML.";
Proc. Natl. Acad. Sci. U.S.A. 110:3895-3900(2013).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
INVOLVEMENT IN MRD32.
PubMed=25728775; DOI=10.1016/j.ajhg.2015.01.017;
UCLA Clinical Genomics Center;
Arboleda V.A., Lee H., Dorrani N., Zadeh N., Willis M., Macmurdo C.F.,
Manning M.A., Kwan A., Hudgins L., Barthelemy F., Miceli M.C.,
Quintero-Rivera F., Kantarci S., Strom S.P., Deignan J.L., Grody W.W.,
Vilain E., Nelson S.F.;
"De novo nonsense mutations in KAT6A, a lysine acetyl-transferase
gene, cause a syndrome including microcephaly and global developmental
delay.";
Am. J. Hum. Genet. 96:498-506(2015).
[23]
INVOLVEMENT IN MRD32.
PubMed=25728777; DOI=10.1016/j.ajhg.2015.01.016;
Tham E., Lindstrand A., Santani A., Malmgren H., Nesbitt A.,
Dubbs H.A., Zackai E.H., Parker M.J., Millan F., Rosenbaum K.,
Wilson G.N., Nordgren A.;
"Dominant mutations in KAT6A cause intellectual disability with
recognizable syndromic features.";
Am. J. Hum. Genet. 96:507-513(2015).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-834 AND LYS-1342, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[25]
STRUCTURE BY NMR OF 531-563.
Kwan A.H.Y., Gell D.A., Liew C.K., Mackay J.P.;
"Solution structure of a CCCCCHC zinc finger from MOZ.";
Submitted (JUN-2002) to the PDB data bank.
[26]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 501-784 IN COMPLEXES WITH
ACETYL-COA; HISTONE H3 AND HISTONE H4 AND ZINC IONS, FUNCTION,
CATALYTIC ACTIVITY, DNA-BINDING, AND MUTAGENESIS OF LYS-545; ILE-727
AND HIS-732.
PubMed=17925393; DOI=10.1074/jbc.M705812200;
Holbert M.A., Sikorski T., Carten J., Snowflack D., Hodawadekar S.,
Marmorstein R.;
"The human monocytic leukemia zinc finger histone acetyltransferase
domain contains DNA-binding activity implicated in chromatin
targeting.";
J. Biol. Chem. 282:36603-36613(2007).
[27]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 497-780 IN COMPLEX WITH
ACETYL-COA, AND ACETYLATION AT LYS-604.
Structural genomics consortium (SGC);
"The crystal structure of human MYST histone acetyltransferase 3 in
complex with acetylcoenzyme A.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Histone acetyltransferase that acetylates lysine
residues in histone H3 and histone H4 (in vitro). Component of the
MOZ/MORF complex which has a histone H3 acetyltransferase
activity. May act as a transcriptional coactivator for RUNX1 and
RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls
its transcriptional activity via association with PML.
{ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:11965546,
ECO:0000269|PubMed:12771199, ECO:0000269|PubMed:16387653,
ECO:0000269|PubMed:17925393, ECO:0000269|PubMed:23431171}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000269|PubMed:11313971,
ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:17925393}.
-!- SUBUNIT: Component of the MOZ/MORF complex composed at least of
ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3.
Interacts with RUNX1; phosphorylation of RUNX1 enhances the
interaction. Interacts with RUNX2. Interacts with p53/TP53.
Interacts with PML (isoform PML-4) and this interaction positively
regulates its acetylation activity towards p53/TP53.
{ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:11965546,
ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358,
ECO:0000269|PubMed:23431171, ECO:0000269|Ref.27}.
-!- INTERACTION:
Q03164:KMT2A; NbExp=10; IntAct=EBI-948013, EBI-2638616;
P61964:WDR5; NbExp=4; IntAct=EBI-948013, EBI-540834;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus,
nucleoplasm. Nucleus, PML body. Note=Recruited into PML body after
DNA damage.
-!- DOMAIN: The N-terminus is involved in transcriptional activation
while the C-terminus is involved in transcriptional repression.
{ECO:0000269|PubMed:11313971}.
-!- PTM: Autoacetylation at Lys-604 is required for proper function
(By similarity). Autoacetylated. {ECO:0000250|UniProtKB:Q9H7Z6,
ECO:0000269|Ref.27}.
-!- PTM: Phosphorylation at Thr-369 by PKB/AKT1 inhibits its
interaction with PML and negatively regulates its acetylation
activity towards p53/TP53. {ECO:0000269|PubMed:11742995,
ECO:0000269|PubMed:23431171}.
-!- DISEASE: Note=Chromosomal aberrations involving KAT6A may be a
cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13)
with CREBBP (PubMed:8782817). Translocation t(8;22)(p11;q13) with
EP300 (PubMed:10824998). KAT6A-CREBBP may induce leukemia by
inhibiting RUNX1-mediated transcription (PubMed:11742995).
Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene,
which consists of the N-terminal part of KAT6A and the C-terminal
part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its
function in transcription activation (PubMed:12676584).
{ECO:0000269|PubMed:10824998, ECO:0000269|PubMed:11742995,
ECO:0000269|PubMed:12676584, ECO:0000269|PubMed:8782817}.
-!- DISEASE: Note=A chromosomal aberration involving KAT6A is a cause
of therapy-related myelodysplastic syndrome. Translocation
t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion
protein. {ECO:0000269|Ref.3}.
-!- DISEASE: Mental retardation, autosomal dominant 32 (MRD32)
[MIM:616268]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period. MRD32 patients
manifest intellectual disability, dysmorphic facial features,
delayed psychomotor development, and lack of speech.
{ECO:0000269|PubMed:25728775, ECO:0000269|PubMed:25728777}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MYST3ID25ch8p11.html";
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EMBL; U47742; AAC50662.1; -; mRNA.
EMBL; AC090571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB084281; BAD00088.1; ALT_TERM; mRNA.
CCDS; CCDS6124.1; -.
RefSeq; NP_006757.2; NM_006766.4.
RefSeq; XP_016869352.1; XM_017013863.1.
RefSeq; XP_016869353.1; XM_017013864.1.
UniGene; Hs.491577; -.
PDB; 1M36; NMR; -; A=533-563.
PDB; 2LN0; NMR; -; A=204-313.
PDB; 2OZU; X-ray; 2.30 A; A=497-780.
PDB; 2RC4; X-ray; 3.00 A; A=501-784.
PDB; 3V43; X-ray; 1.47 A; A=204-313.
PDB; 4LJN; X-ray; 3.00 A; A=194-323.
PDB; 4LK9; X-ray; 1.60 A; A=194-323.
PDB; 4LKA; X-ray; 1.61 A; A=194-323.
PDB; 4LLB; X-ray; 2.50 A; A/B=194-323.
PDB; 5B75; X-ray; 1.70 A; A=194-323.
PDB; 5B76; X-ray; 1.65 A; A=194-323.
PDB; 5B77; X-ray; 1.55 A; A=194-323.
PDB; 5B78; X-ray; 1.40 A; A=194-323.
PDBsum; 1M36; -.
PDBsum; 2LN0; -.
PDBsum; 2OZU; -.
PDBsum; 2RC4; -.
PDBsum; 3V43; -.
PDBsum; 4LJN; -.
PDBsum; 4LK9; -.
PDBsum; 4LKA; -.
PDBsum; 4LLB; -.
PDBsum; 5B75; -.
PDBsum; 5B76; -.
PDBsum; 5B77; -.
PDBsum; 5B78; -.
ProteinModelPortal; Q92794; -.
SMR; Q92794; -.
BioGrid; 113703; 43.
CORUM; Q92794; -.
IntAct; Q92794; 21.
STRING; 9606.ENSP00000265713; -.
ChEMBL; CHEMBL3774298; -.
iPTMnet; Q92794; -.
PhosphoSitePlus; Q92794; -.
BioMuta; KAT6A; -.
DMDM; 215274095; -.
EPD; Q92794; -.
MaxQB; Q92794; -.
PaxDb; Q92794; -.
PeptideAtlas; Q92794; -.
PRIDE; Q92794; -.
DNASU; 7994; -.
Ensembl; ENST00000265713; ENSP00000265713; ENSG00000083168.
Ensembl; ENST00000396930; ENSP00000380136; ENSG00000083168.
Ensembl; ENST00000406337; ENSP00000385888; ENSG00000083168.
GeneID; 7994; -.
KEGG; hsa:7994; -.
UCSC; uc003xon.4; human.
CTD; 7994; -.
DisGeNET; 7994; -.
EuPathDB; HostDB:ENSG00000083168.9; -.
GeneCards; KAT6A; -.
HGNC; HGNC:13013; KAT6A.
HPA; CAB017023; -.
HPA; HPA063266; -.
HPA; HPA065052; -.
MalaCards; KAT6A; -.
MIM; 601408; gene.
MIM; 616268; phenotype.
neXtProt; NX_Q92794; -.
OpenTargets; ENSG00000083168; -.
Orphanet; 370026; Acute myeloid leukemia with t(8;16)(p11;p13) translocation.
PharmGKB; PA37592; -.
eggNOG; KOG2747; Eukaryota.
eggNOG; COG5027; LUCA.
GeneTree; ENSGT00550000074503; -.
HOGENOM; HOG000234365; -.
HOVERGEN; HBG052563; -.
InParanoid; Q92794; -.
KO; K11305; -.
OMA; CDPPLTR; -.
OrthoDB; EOG091G00D2; -.
PhylomeDB; Q92794; -.
TreeFam; TF106483; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
SIGNOR; Q92794; -.
ChiTaRS; KAT6A; human.
EvolutionaryTrace; Q92794; -.
GeneWiki; MYST3; -.
GenomeRNAi; 7994; -.
PRO; PR:Q92794; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000083168; -.
CleanEx; HS_MYST3; -.
ExpressionAtlas; Q92794; baseline and differential.
Genevisible; Q92794; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000786; C:nucleosome; IEA:InterPro.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; TAS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0090398; P:cellular senescence; IMP:UniProtKB.
GO; GO:0006323; P:DNA packaging; TAS:ProtInc.
GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.10.10; -; 2.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR002717; HAT_MYST-type.
InterPro; IPR005818; Histone_H1/H5_H15.
InterPro; IPR031280; KAT6A.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR10615:SF26; PTHR10615:SF26; 5.
Pfam; PF01853; MOZ_SAS; 1.
Pfam; PF00628; PHD; 1.
SMART; SM00526; H15; 1.
SMART; SM00249; PHD; 2.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF55729; SSF55729; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS51504; H15; 1.
PROSITE; PS51726; MYST_HAT; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Acyltransferase;
Chromatin regulator; Chromosomal rearrangement; Complete proteome;
Isopeptide bond; Mental retardation; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome;
Repeat; Repressor; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 2004 Histone acetyltransferase KAT6A.
/FTId=PRO_0000051572.
DOMAIN 95 171 H15. {ECO:0000255|PROSITE-
ProRule:PRU00837}.
DOMAIN 504 778 MYST-type HAT. {ECO:0000255|PROSITE-
ProRule:PRU01063}.
ZN_FING 206 265 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 259 313 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 537 562 C2HC MYST-type. {ECO:0000255|PROSITE-
ProRule:PRU01063}.
REGION 1 144 Required for activation of RUNX1-1.
REGION 52 166 Required for nuclear localization.
REGION 144 664 Interaction with PML.
{ECO:0000269|PubMed:23431171}.
REGION 312 664 Interaction with RUNX1-1.
REGION 488 778 Catalytic.
REGION 507 810 Mediates interaction with BRPF1, required
for histone H3 acetyltransferase
activity. {ECO:0000269|PubMed:18794358}.
REGION 645 649 Acetyl-CoA binding. {ECO:0000269|Ref.27}.
REGION 654 660 Acetyl-CoA binding. {ECO:0000269|Ref.27}.
REGION 1517 1741 Interaction with PML.
{ECO:0000269|PubMed:23431171}.
REGION 1517 1642 Interaction with RUNX1-2.
REGION 1913 1948 Required for activation of RUNX1-2.
COMPBIAS 371 379 Poly-Ser.
COMPBIAS 788 801 Poly-Glu.
COMPBIAS 989 995 Poly-Glu.
COMPBIAS 1019 1026 Poly-Arg.
COMPBIAS 1069 1078 Poly-Glu.
COMPBIAS 1147 1150 Poly-Lys.
COMPBIAS 1221 1242 Glu-rich.
COMPBIAS 1267 1302 Glu-rich.
COMPBIAS 1411 1414 Poly-Glu.
COMPBIAS 1593 1597 Poly-Ser.
COMPBIAS 1643 1704 Gln/Pro-rich.
COMPBIAS 1897 1977 Met-rich.
ACT_SITE 680 680 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q9H7Z6}.
BINDING 684 684 Acetyl-CoA. {ECO:0000269|Ref.27}.
SITE 813 814 Breakpoint for translocation to form
KAT6A-ASXL2.
SITE 1117 1118 Breakpoint for translocation to form
KAT6A-EP300 and KAT6A-NCOA2.
SITE 1546 1547 Breakpoint for translocation to form
KAT6A-CREBBP.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BZ21}.
MOD_RES 350 350 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 355 355 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 369 369 Phosphothreonine; by PKB/AKT1.
{ECO:0000269|PubMed:23431171}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 604 604 N6-acetyllysine; by autocatalysis.
{ECO:0000269|Ref.27}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BZ21}.
MOD_RES 812 812 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 815 815 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BZ21}.
MOD_RES 899 899 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q5TKR9}.
MOD_RES 941 941 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 954 954 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 974 974 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1007 1007 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1089 1089 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1090 1090 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1113 1113 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 834 834 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1342 1342 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 134 134 L -> S (in dbSNP:rs3824276).
/FTId=VAR_047548.
MUTAGEN 543 543 C->G: Abrogates HAT activity.
{ECO:0000269|PubMed:12676584}.
MUTAGEN 545 545 K->A: Reduced affinity for DNA.
{ECO:0000269|PubMed:17925393}.
MUTAGEN 657 657 G->E: Abrogates HAT activity.
{ECO:0000269|PubMed:12676584}.
MUTAGEN 727 727 I->E: Slightly reduced affinity for DNA.
{ECO:0000269|PubMed:17925393}.
MUTAGEN 732 732 H->D: Reduced affinity for DNA.
{ECO:0000269|PubMed:17925393}.
CONFLICT 401 401 K -> R (in Ref. 1; AAC50662 and 3;
BAD00088). {ECO:0000305}.
HELIX 195 197 {ECO:0000244|PDB:5B78}.
STRAND 198 200 {ECO:0000244|PDB:5B76}.
STRAND 207 209 {ECO:0000244|PDB:5B78}.
TURN 210 212 {ECO:0000244|PDB:5B78}.
TURN 231 233 {ECO:0000244|PDB:5B78}.
HELIX 239 242 {ECO:0000244|PDB:5B78}.
HELIX 246 252 {ECO:0000244|PDB:5B78}.
TURN 253 256 {ECO:0000244|PDB:5B78}.
TURN 260 262 {ECO:0000244|PDB:5B78}.
TURN 266 268 {ECO:0000244|PDB:5B78}.
HELIX 275 277 {ECO:0000244|PDB:5B78}.
STRAND 278 280 {ECO:0000244|PDB:4LK9}.
TURN 282 284 {ECO:0000244|PDB:5B78}.
STRAND 287 289 {ECO:0000244|PDB:4LK9}.
HELIX 290 292 {ECO:0000244|PDB:5B78}.
STRAND 293 295 {ECO:0000244|PDB:5B78}.
TURN 308 310 {ECO:0000244|PDB:5B78}.
STRAND 511 514 {ECO:0000244|PDB:2OZU}.
STRAND 517 520 {ECO:0000244|PDB:2OZU}.
HELIX 529 532 {ECO:0000244|PDB:2RC4}.
STRAND 535 539 {ECO:0000244|PDB:2OZU}.
TURN 541 543 {ECO:0000244|PDB:2OZU}.
STRAND 546 549 {ECO:0000244|PDB:2OZU}.
HELIX 550 559 {ECO:0000244|PDB:2OZU}.
STRAND 566 573 {ECO:0000244|PDB:2OZU}.
STRAND 576 582 {ECO:0000244|PDB:2OZU}.
TURN 583 585 {ECO:0000244|PDB:2OZU}.
HELIX 587 598 {ECO:0000244|PDB:2OZU}.
STRAND 613 622 {ECO:0000244|PDB:2OZU}.
STRAND 625 637 {ECO:0000244|PDB:2OZU}.
STRAND 642 649 {ECO:0000244|PDB:2OZU}.
HELIX 651 653 {ECO:0000244|PDB:2OZU}.
STRAND 655 657 {ECO:0000244|PDB:2RC4}.
HELIX 658 672 {ECO:0000244|PDB:2OZU}.
STRAND 677 679 {ECO:0000244|PDB:2OZU}.
HELIX 685 705 {ECO:0000244|PDB:2OZU}.
HELIX 713 720 {ECO:0000244|PDB:2OZU}.
HELIX 724 733 {ECO:0000244|PDB:2OZU}.
HELIX 750 759 {ECO:0000244|PDB:2OZU}.
HELIX 771 773 {ECO:0000244|PDB:2OZU}.
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


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