KAT6A_HUMAN
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 03-AUG-2022, entry version 216.
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="http://atlasgeneticsoncology.org/Genes/MYST3ID25ch8p11.html";
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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 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 AlphaFoldDB; Q92794; -.
DR BMRB; Q92794; -.
DR SMR; Q92794; -.
DR BioGRID; 113703; 82.
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.ENSP00000380136; -.
DR BindingDB; Q92794; -.
DR ChEMBL; CHEMBL3774298; -.
DR GlyGen; Q92794; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q92794; -.
DR PhosphoSitePlus; Q92794; -.
DR BioMuta; KAT6A; -.
DR DMDM; 215274095; -.
DR EPD; Q92794; -.
DR jPOST; Q92794; -.
DR MassIVE; Q92794; -.
DR MaxQB; Q92794; -.
DR PaxDb; Q92794; -.
DR PeptideAtlas; Q92794; -.
DR PRIDE; Q92794; -.
DR ProteomicsDB; 75473; -.
DR Antibodypedia; 23986; 138 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 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; 629545at2759; -.
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; 79 hits in 1042 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 218 other tissues.
DR ExpressionAtlas; Q92794; baseline and differential.
DR Genevisible; Q92794; HS.
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:0010484; F:H3 histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO: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: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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 3.30.40.10; -; 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; IPR031280; KAT6A.
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:SF26; PTHR10615:SF26; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
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; 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 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 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
