KAT6B_HUMAN
ID KAT6B_HUMAN Reviewed; 2073 AA.
AC Q8WYB5; O15087; Q86Y05; Q8WU81; Q9UKW2; Q9UKW3; Q9UKX0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Histone acetyltransferase KAT6B;
DE EC=2.3.1.48 {ECO:0000269|PubMed:10497217};
DE AltName: Full=Histone acetyltransferase MOZ2;
DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4;
DE Short=MYST-4;
DE AltName: Full=Monocytic leukemia zinc finger protein-related factor;
GN Name=KAT6B; Synonyms=KIAA0383, MORF, MOZ2, MYST4;
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] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY,
RP AUTOACETYLATION, CATALYTIC ACTIVITY, DOMAIN, AND FUNCTION.
RC TISSUE=Bone marrow;
RX PubMed=10497217; DOI=10.1074/jbc.274.40.28528;
RA Champagne N., Bertos N.R., Pelletier N., Wang A.H., Vezmar M., Yang Y.,
RA Heng H.H., Yang X.-J.;
RT "Identification of a human histone acetyltransferase related to monocytic
RT leukemia zinc finger protein.";
RL J. Biol. Chem. 274:28528-28536(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Borrow J., Housman D.E.;
RT "Structure and function of the human MYST family: MOZ2, MYST1 and MYST2.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-322 AND 1187-2073.
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1136-1287, AND CHROMOSOMAL TRANSLOCATION WITH
RP CREBBP.
RX PubMed=11157802; DOI=10.1093/hmg/10.4.395;
RA Panagopoulos I., Fioretos T., Isaksson M., Samuelsson U., Billstroem R.,
RA Stroembeck B., Mitelman F., Johansson B.;
RT "Fusion of the MORF and CBP genes in acute myeloid leukemia with the
RT t(10;16)(q22;p13).";
RL Hum. Mol. Genet. 10:395-404(2001).
RN [7]
RP INTERACTION WITH RUNX1 AND RUNX2, AUTOACETYLATION, 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 [8]
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 [9]
RP IDENTIFICATION IN THE MOZ/MORF COMPLEX, AND INTERACTION WITH BRPF1.
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1038; LYS-1042 AND LYS-1044, 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 [11]
RP INVOLVEMENT IN SBBYSS, AND VARIANT LYS-360.
RX PubMed=22077973; DOI=10.1016/j.ajhg.2011.10.008;
RA Clayton-Smith J., O'Sullivan J., Daly S., Bhaskar S., Day R., Anderson B.,
RA Voss A.K., Thomas T., Biesecker L.G., Smith P., Fryer A., Chandler K.E.,
RA Kerr B., Tassabehji M., Lynch S.A., Krajewska-Walasek M., McKee S.,
RA Smith J., Sweeney E., Mansour S., Mohammed S., Donnai D., Black G.;
RT "Whole-exome-sequencing identifies mutations in histone acetyltransferase
RT gene KAT6B in individuals with the Say-Barber-Biesecker variant of Ohdo
RT syndrome.";
RL Am. J. Hum. Genet. 89:675-681(2011).
RN [12]
RP INVOLVEMENT IN GTPTS.
RX PubMed=22265014; DOI=10.1016/j.ajhg.2011.11.023;
RA Campeau P.M., Kim J.C., Lu J.T., Schwartzentruber J.A., Abdul-Rahman O.A.,
RA Schlaubitz S., Murdock D.M., Jiang M.M., Lammer E.J., Enns G.M.,
RA Rhead W.J., Rowland J., Robertson S.P., Cormier-Daire V., Bainbridge M.N.,
RA Yang X.J., Gingras M.C., Gibbs R.A., Rosenblatt D.S., Majewski J.,
RA Lee B.H.;
RT "Mutations in KAT6B, encoding a histone acetyltransferase, cause
RT Genitopatellar syndrome.";
RL Am. J. Hum. Genet. 90:282-289(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-647 AND SER-1048,
RP AND 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-673, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-673, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-673, AND IDENTIFICATION BY MASS
RP 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 [17]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-483.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Histone acetyltransferase which may be involved in both
CC positive and negative regulation of transcription. Required for RUNX2-
CC dependent transcriptional activation. May be involved in cerebral
CC cortex development. Component of the MOZ/MORF complex which has a
CC histone H3 acetyltransferase activity. {ECO:0000269|PubMed:10497217,
CC ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:16387653}.
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:10497217};
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 and RUNX2. {ECO:0000269|PubMed:11965546,
CC ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Beta;
CC IsoId=Q8WYB5-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q8WYB5-2; Sequence=VSP_014587;
CC Name=3;
CC IsoId=Q8WYB5-3; Sequence=VSP_014586;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in heart,
CC pancreas, testis and ovary. {ECO:0000269|PubMed:10497217}.
CC -!- DOMAIN: The N-terminus is involved in transcriptional activation while
CC the C-terminus is involved in transcriptional repression.
CC {ECO:0000269|PubMed:10497217}.
CC -!- PTM: Autoacetylated (PubMed:10497217 and PubMed:11965546).
CC Autoacetylation at Lys-815 is required for proper function.
CC {ECO:0000250|UniProtKB:Q9H7Z6, ECO:0000269|PubMed:10497217,
CC ECO:0000269|PubMed:11965546}.
CC -!- DISEASE: Note=A chromosomal aberration involving KAT6B may be a cause
CC acute myeloid leukemias. Translocation t(10;16)(q22;p13) with CREBBP.
CC {ECO:0000269|PubMed:11157802}.
CC -!- DISEASE: Ohdo syndrome, SBBYS variant (SBBYSS) [MIM:603736]: A syndrome
CC characterized by distinctive facial appearance with severe
CC blepharophimosis, an immobile mask-like face, a bulbous nasal tip, and
CC a small mouth with a thin upper lip. The condition presents in infancy
CC with severe hypotonia and feeding problems. Associated skeletal
CC problems include joint laxity, abnormally long thumbs and great toes,
CC and dislocated or hypoplastic patellae. Structural cardiac defects are
CC present in around 50% of cases, and dental anomalies, including small
CC and pointed teeth, are common. Optic atrophy and conductive or
CC sensorineural deafness are repeatedly reported. Many affected
CC individuals have abnormalities of thyroid structure or function. SBBYSS
CC is usually associated with severe intellectual disability, delayed
CC motor milestones, and significantly impaired speech.
CC {ECO:0000269|PubMed:22077973}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Genitopatellar syndrome (GTPTS) [MIM:606170]: A rare disorder
CC consisting of microcephaly, severe psychomotor retardation, and
CC characteristic coarse facial features, including broad nose and small
CC or retracted chin, associated with congenital flexion contractures of
CC the lower extremities, abnormal or missing patellae, and urogenital
CC anomalies. {ECO:0000269|PubMed:22265014}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF00100.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH14143.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH48199.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MYST4ID41488ch10q22.html";
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DR EMBL; AF113514; AAF00095.1; -; mRNA.
DR EMBL; AF119230; AAF00099.1; -; mRNA.
DR EMBL; AF119231; AAF00100.1; ALT_FRAME; mRNA.
DR EMBL; AF217500; AAL56647.1; -; mRNA.
DR EMBL; AB002381; BAA20837.2; -; mRNA.
DR EMBL; BC014143; AAH14143.1; ALT_SEQ; mRNA.
DR EMBL; BC021128; AAH21128.1; -; mRNA.
DR EMBL; BC048199; AAH48199.1; ALT_SEQ; mRNA.
DR CCDS; CCDS58084.1; -. [Q8WYB5-3]
DR CCDS; CCDS58085.1; -. [Q8WYB5-2]
DR CCDS; CCDS7345.1; -. [Q8WYB5-1]
DR RefSeq; NP_001243397.1; NM_001256468.1. [Q8WYB5-2]
DR RefSeq; NP_001243398.1; NM_001256469.1. [Q8WYB5-3]
DR RefSeq; NP_036462.2; NM_012330.3. [Q8WYB5-1]
DR RefSeq; XP_005269721.1; XM_005269664.2. [Q8WYB5-1]
DR RefSeq; XP_016871489.1; XM_017016000.1.
DR RefSeq; XP_016871490.1; XM_017016001.1.
DR RefSeq; XP_016871491.1; XM_017016002.1.
DR RefSeq; XP_016871492.1; XM_017016003.1. [Q8WYB5-1]
DR RefSeq; XP_016871494.1; XM_017016005.1.
DR RefSeq; XP_016871495.1; XM_017016006.1.
DR RefSeq; XP_016871496.1; XM_017016007.1.
DR RefSeq; XP_016871497.1; XM_017016008.1.
DR PDB; 5U2J; X-ray; 1.60 A; A/B=211-320.
DR PDB; 6OIE; X-ray; 2.08 A; A/B=211-322.
DR PDBsum; 5U2J; -.
DR PDBsum; 6OIE; -.
DR AlphaFoldDB; Q8WYB5; -.
DR SMR; Q8WYB5; -.
DR BioGRID; 117069; 27.
DR ComplexPortal; CPX-738; MORF1 histone acetyltransferase complex.
DR ComplexPortal; CPX-739; MORF2 histone acetyltransferase complex.
DR ComplexPortal; CPX-740; MORF3 histone acetyltransferase complex.
DR CORUM; Q8WYB5; -.
DR IntAct; Q8WYB5; 14.
DR MINT; Q8WYB5; -.
DR STRING; 9606.ENSP00000287239; -.
DR BindingDB; Q8WYB5; -.
DR ChEMBL; CHEMBL3774300; -.
DR MoonDB; Q8WYB5; Predicted.
DR GlyGen; Q8WYB5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WYB5; -.
DR PhosphoSitePlus; Q8WYB5; -.
DR BioMuta; KAT6B; -.
DR DMDM; 143811424; -.
DR EPD; Q8WYB5; -.
DR jPOST; Q8WYB5; -.
DR MassIVE; Q8WYB5; -.
DR MaxQB; Q8WYB5; -.
DR PaxDb; Q8WYB5; -.
DR PeptideAtlas; Q8WYB5; -.
DR PRIDE; Q8WYB5; -.
DR ProteomicsDB; 75154; -. [Q8WYB5-1]
DR ProteomicsDB; 75155; -. [Q8WYB5-2]
DR ProteomicsDB; 75156; -. [Q8WYB5-3]
DR Antibodypedia; 1807; 82 antibodies from 22 providers.
DR DNASU; 23522; -.
DR Ensembl; ENST00000287239.10; ENSP00000287239.4; ENSG00000156650.14. [Q8WYB5-1]
DR Ensembl; ENST00000372711.2; ENSP00000361796.1; ENSG00000156650.14. [Q8WYB5-2]
DR Ensembl; ENST00000372714.6; ENSP00000361799.1; ENSG00000156650.14. [Q8WYB5-3]
DR Ensembl; ENST00000372724.6; ENSP00000361809.2; ENSG00000156650.14. [Q8WYB5-2]
DR Ensembl; ENST00000372725.6; ENSP00000361810.1; ENSG00000156650.14. [Q8WYB5-3]
DR Ensembl; ENST00000628038.3; ENSP00000485896.1; ENSG00000281813.4. [Q8WYB5-3]
DR Ensembl; ENST00000628523.3; ENSP00000487238.2; ENSG00000281813.4. [Q8WYB5-2]
DR Ensembl; ENST00000629233.3; ENSP00000487219.1; ENSG00000281813.4. [Q8WYB5-3]
DR Ensembl; ENST00000629879.2; ENSP00000486731.1; ENSG00000281813.4. [Q8WYB5-2]
DR Ensembl; ENST00000630001.4; ENSP00000486595.1; ENSG00000281813.4. [Q8WYB5-1]
DR Ensembl; ENST00000647630.1; ENSP00000497352.1; ENSG00000281813.4. [Q8WYB5-1]
DR Ensembl; ENST00000648605.1; ENSP00000497718.1; ENSG00000281813.4. [Q8WYB5-1]
DR Ensembl; ENST00000648725.1; ENSP00000497841.1; ENSG00000156650.14. [Q8WYB5-1]
DR Ensembl; ENST00000648892.1; ENSP00000497048.1; ENSG00000156650.14. [Q8WYB5-3]
DR Ensembl; ENST00000649006.1; ENSP00000498139.1; ENSG00000156650.14. [Q8WYB5-3]
DR Ensembl; ENST00000649463.1; ENSP00000497166.1; ENSG00000156650.14. [Q8WYB5-1]
DR Ensembl; ENST00000649574.1; ENSP00000497416.1; ENSG00000281813.4. [Q8WYB5-3]
DR Ensembl; ENST00000650575.1; ENSP00000497453.1; ENSG00000281813.4. [Q8WYB5-3]
DR GeneID; 23522; -.
DR KEGG; hsa:23522; -.
DR MANE-Select; ENST00000287239.10; ENSP00000287239.4; NM_012330.4; NP_036462.2.
DR UCSC; uc001jwm.3; human. [Q8WYB5-1]
DR CTD; 23522; -.
DR DisGeNET; 23522; -.
DR GeneCards; KAT6B; -.
DR GeneReviews; KAT6B; -.
DR HGNC; HGNC:17582; KAT6B.
DR HPA; ENSG00000156650; Low tissue specificity.
DR MalaCards; KAT6B; -.
DR MIM; 603736; phenotype.
DR MIM; 605880; gene.
DR MIM; 606170; phenotype.
DR neXtProt; NX_Q8WYB5; -.
DR OpenTargets; ENSG00000156650; -.
DR Orphanet; 3047; Blepharophimosis-intellectual disability syndrome, SBBYS type.
DR Orphanet; 85201; Genitopatellar syndrome.
DR PharmGKB; PA134880712; -.
DR VEuPathDB; HostDB:ENSG00000156650; -.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000157372; -.
DR HOGENOM; CLU_001232_1_1_1; -.
DR InParanoid; Q8WYB5; -.
DR OMA; KSKQGWP; -.
DR PhylomeDB; Q8WYB5; -.
DR TreeFam; TF106483; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; Q8WYB5; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q8WYB5; -.
DR SIGNOR; Q8WYB5; -.
DR BioGRID-ORCS; 23522; 16 hits in 1095 CRISPR screens.
DR ChiTaRS; KAT6B; human.
DR GeneWiki; MYST4; -.
DR GenomeRNAi; 23522; -.
DR Pharos; Q8WYB5; Tchem.
DR PRO; PR:Q8WYB5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8WYB5; protein.
DR Bgee; ENSG00000156650; Expressed in cortical plate and 111 other tissues.
DR ExpressionAtlas; Q8WYB5; baseline and differential.
DR Genevisible; Q8WYB5; HS.
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; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
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:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
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 InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR005818; Histone_H1/H5_H15.
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 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; 1.
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 Alternative splicing; Chromatin regulator; Chromosomal rearrangement;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2073
FT /note="Histone acetyltransferase KAT6B"
FT /id="PRO_0000051575"
FT DOMAIN 103..176
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 715..989
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 213..272
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 269..320
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 748..773
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 72..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..717
FT /note="Negatively regulates HAT activity"
FT REGION 442..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..1008
FT /note="Catalytic"
FT REGION 752..1008
FT /note="Interaction with BRPF1"
FT /evidence="ECO:0000269|PubMed:18794358"
FT REGION 1022..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..2073
FT /note="Interaction with RUNX1 and RUNX2"
FT /evidence="ECO:0000269|PubMed:11965546"
FT REGION 1580..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1139
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 891
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 856..860
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 865..871
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 895
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT SITE 1222..1223
FT /note="Breakpoint for translocation to form KAT6B-CREBBP"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 815
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 1038
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1042
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1044
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1048
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 673
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 373..664
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10497217,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_014586"
FT VAR_SEQ 482..664
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10497217"
FT /id="VSP_014587"
FT VARIANT 360
FT /note="E -> K"
FT /evidence="ECO:0000269|PubMed:22077973"
FT /id="VAR_067315"
FT VARIANT 483
FT /note="T -> A (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036361"
FT VARIANT 1217
FT /note="A -> S (in dbSNP:rs57372986)"
FT /id="VAR_061367"
FT VARIANT 1499
FT /note="V -> I (in dbSNP:rs3740321)"
FT /id="VAR_050217"
FT CONFLICT 123
FT /note="G -> R (in Ref. 2; AAL56647)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="P -> A (in Ref. 2; AAL56647)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="F -> L (in Ref. 1; AAF00095/AAF00099/AAF00100 and 3;
FT BAA20837)"
FT /evidence="ECO:0000305"
FT CONFLICT 931..933
FT /note="TGM -> RHV (in Ref. 2; AAL56647)"
FT /evidence="ECO:0000305"
FT CONFLICT 934
FT /note="Missing (in Ref. 2; AAL56647)"
FT /evidence="ECO:0000305"
FT CONFLICT 1152
FT /note="T -> S (in Ref. 2; AAL56647)"
FT /evidence="ECO:0000305"
FT CONFLICT 1625
FT /note="S -> T (in Ref. 2; AAL56647)"
FT /evidence="ECO:0000305"
FT CONFLICT 1731
FT /note="S -> T (in Ref. 2; AAL56647)"
FT /evidence="ECO:0000305"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5U2J"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5U2J"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:5U2J"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:5U2J"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:5U2J"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:5U2J"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:5U2J"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5U2J"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:5U2J"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5U2J"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5U2J"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:5U2J"
SQ SEQUENCE 2073 AA; 231378 MW; AEE267B9DA444B08 CRC64;
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV
LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK SAKGSRGSCN DLRNVDWNKL LRRAIEGLEE
PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD
GKGAPQYPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC
GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC
DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRLLSVTSDE
GSMNAFTGRG SPGRGQKTKV CTTPSSGHAA SGKDSSSRLA VTDPTRPGAT TKITTTSTYI
SASTLKVNKK TKGLIDGLTK FFTPSPDGRR SRGEIIDFSK HYRPRKKVSQ KQSCTSHVLA
TGTTQKLKPP PSSLPPPTPI SGQSPSSQKS STATSSPSPQ SSSSQCSVPS LSSLTTNSQL
KALFDGLSHI YTTQGQSRKK GHPSYAPPKR MRRKTELSST AKSKAHFFGK RDIRSRFISH
SSSSSWGMAR GSIFKAIAHF KRTTFLKKHR MLGRLKYKVT PQMGTPSPGK GSLTDGRIKP
DQDDDTEIKI NIKQESADVN VIGNKDVVTE EDLDVFKQAQ ELSWEKIECE SGVEDCGRYP
SVIEFGKYEI QTWYSSPYPQ EYARLPKLYL CEFCLKYMKS KNILLRHSKK CGWFHPPANE
IYRRKDLSVF EVDGNMSKIY CQNLCLLAKL FLDHKTLYYD VEPFLFYVLT KNDEKGCHLV
GYFSKEKLCQ QKYNVSCIMI MPQHQRQGFG RFLIDFSYLL SRREGQAGSP EKPLSDLGRL
SYLAYWKSVI LEYLYHHHER HISIKAISRA TGMCPHDIAT TLQHLHMIDK RDGRFVIIRR
EKLILSHMEK LKTCSRANEL DPDSLRWTPI LISNAAVSEE EREAEKEAER LMEQASCWEK
EEQEILSTRA NSRQSPAKVQ SKNKYLHSPE SRPVTGERGQ LLELSKESSE EEEEEEDEEE
EEEEEEEEED EEEEEEEEEE EEEENIQSSP PRLTKPQSVA IKRKRPFVLK KKRGRKRRRI
NSSVTTETIS ETTEVLNEPF DNSDEERPMP QLEPTCEIEV EEDGRKPVLR KAFQHQPGKK
RQTEEEEGKD NHCFKNADPC RNNMNDDSSN LKEGSKDNPE PLKCKQVWPK GTKRGLSKWR
QNKERKTGFK LNLYTPPETP MEPDEQVTVE EQKETSEGKT SPSPIRIEEE VKETGEALLP
QEENRREETC APVSPNTSPG EKPEDDLIKP EEEEEEEEEE EEEEEEEEGE EEEGGGNVEK
DPDGAKSQEK EEPEISTEKE DSARLDDHEE EEEEDEEPSH NEDHDADDED DSHMESAEVE
KEELPRESFK EVLENQETFL DLNVQPGHSN PEVLMDCGVD LTASCNSEPK ELAGDPEAVP
ESDEEPPPGE QAQKQDQKNS KEVDTEFKEG NPATMEIDSE TVQAVQSLTQ ESSEQDDTFQ
DCAETQEACR SLQNYTRADQ SPQIATTLDD CQQSDHSSPV SSVHSHPGQS VRSVNSPSVP
ALENSYAQIS PDQSAISVPS LQNMETSPMM DVPSVSDHSQ QVVDSGFSDL GSIESTTENY
ENPSSYDSTM GGSICGNGSS QNSCSYSNLT SSSLTQSSCA VTQQMSNISG SCSMLQQTSI
SSPPTCSVKS PQGCVVERPP SSSQQLAQCS MAANFTPPMQ LAEIPETSNA NIGLYERMGQ
SDFGAGHYPQ PSATFSLAKL QQLTNTLIDH SLPYSHSAAV TSYANSASLS TPLSNTGLVQ
LSQSPHSVPG GPQAQATMTP PPNLTPPPMN LPPPLLQRNM AASNIGISHS QRLQTQIASK
GHISMRTKSA SLSPAAATHQ SQIYGRSQTV AMQGPARTLT MQRGMNMSVN LMPAPAYNVN
SVNMNMNTLN AMNGYSMSQP MMNSGYHSNH GYMNQTPQYP MQMQMGMMGT QPYAQQPMQT
PPHGNMMYTA PGHHGYMNTG MSKQSLNGSY MRR
