ID KAT2B_HUMAN Reviewed; 832 AA. AC Q92831; Q6NSK1; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 3. DT 09-DEC-2015, entry version 172. DE RecName: Full=Histone acetyltransferase KAT2B; DE EC=2.3.1.48; DE AltName: Full=Histone acetyltransferase PCAF; DE Short=Histone acetylase PCAF; DE AltName: Full=Lysine acetyltransferase 2B; DE AltName: Full=P300/CBP-associated factor; DE Short=P/CAF; GN Name=KAT2B; Synonyms=PCAF; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAC50890.2}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND RP INTERACTION WITH EP300 AND CREBBP. RC TISSUE=Liver; RX PubMed=8684459; DOI=10.1038/382319a0; RA Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.; RT "A p300/CBP-associated factor that competes with the adenoviral RT oncoprotein E1A."; RL Nature 382:319-324(1996). RN [2] {ECO:0000305} RP SEQUENCE REVISION. RC TISSUE=Liver; RA Nakatani Y.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP ENZYME ACTIVITY. RX PubMed=8945521; DOI=10.1016/S0092-8674(00)82001-2; RA Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.; RT "The transcriptional coactivators p300 and CBP are histone RT acetyltransferases."; RL Cell 87:953-959(1996). RN [5] RP INTERACTION WITH NCOA3. RX PubMed=9346901; DOI=10.1074/jbc.272.44.27629; RA Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.; RT "TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, RT exhibits distinct properties from steroid receptor coactivator-1."; RL J. Biol. Chem. 272:27629-27634(1997). RN [6] RP INTERACTION WITH NCOA1. RX PubMed=9296499; DOI=10.1038/38304; RA Spencer T.E., Jenster G., Burcin M.M., Allis C.D., Zhou J., RA Mizzen C.A., McKenna N.J., Onate S.A., Tsai S.Y., Tsai M.-J., RA O'Malley B.W.; RT "Steroid receptor coactivator-1 is a histone acetyltransferase."; RL Nature 389:194-198(1997). RN [7] RP INTERACTION WITH KLF1, AND FUNCTION. RX PubMed=9707565; DOI=10.1073/pnas.95.17.9855; RA Zhang W., Bieker J.J.; RT "Acetylation and modulation of erythroid Krueppel-like factor (EKLF) RT activity by interaction with histone acetyltransferases."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998). RN [8] RP INTERACTION WITH E2F1, AND FUNCTION. RX PubMed=10675335; DOI=10.1093/emboj/19.4.662; RA Martinez-Balbas M.A., Bauer U.M., Nielsen S.J., Brehm A., RA Kouzarides T.; RT "Regulation of E2F1 activity by acetylation."; RL EMBO J. 19:662-671(2000). RN [9] RP INTERACTION WITH HTLV-1 TAX. RX PubMed=10766811; DOI=10.1074/jbc.275.16.11852; RA Harrod R., Kuo Y.-L., Tang Y., Yao Y., Vassilev A., Nakatani Y., RA Giam C.-Z.; RT "p300 and p300/cAMP-responsive element-binding protein associated RT factor interact with human T-cell lymphotropic virus type-1 Tax in a RT multi-histone acetyltransferase/activator-enhancer complex."; RL J. Biol. Chem. 275:11852-11857(2000). RN [10] RP INTERACTION WITH MECOM. RX PubMed=11568182; DOI=10.1074/jbc.M106733200; RA Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.; RT "Interaction of EVI1 with cAMP-responsive element-binding protein- RT binding protein (CBP) and p300/CBP-associated factor (P/CAF) results RT in reversible acetylation of EVI1 and in co-localization in nuclear RT speckles."; RL J. Biol. Chem. 276:44936-44943(2001). RN [11] RP INTERACTION WITH HIV-1 TAT. RX PubMed=12486002; DOI=10.1093/emboj/cdf669; RA Bres V., Tagami H., Peloponese J.-M., Loret E., Jeang K.-T., RA Nakatani Y., Emiliani S., Benkirane M., Kiernan R.E.; RT "Differential acetylation of Tat coordinates its interaction with the RT co-activators cyclin T1 and PCAF."; RL EMBO J. 21:6811-6819(2002). RN [12] RP FUNCTION, AND INTERACTION WITH NPAS2; ARNTL/BMAL1 AND CLOCK. RX PubMed=14645221; DOI=10.1074/jbc.M311973200; RA Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., RA Chakravarti D., FitzGerald G.A., McNamara P.; RT "Histone acetyltransferase-dependent chromatin remodeling and the RT vascular clock."; RL J. Biol. Chem. 279:7091-7097(2004). RN [13] RP INTERACTION WITH NFE4. RX PubMed=15273251; DOI=10.1074/jbc.M405129200; RA Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.; RT "Site-specific acetylation of the fetal globin activator NF-E4 RT prevents its ubiquitination and regulates its interaction with the RT histone deacetylase, HDAC1."; RL J. Biol. Chem. 279:41477-41486(2004). RN [14] RP INTERACTION WITH TACC1; TACC2 AND TACC3. RX PubMed=14767476; DOI=10.1038/sj.onc.1207424; RA Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.; RT "The transforming acidic coiled coil proteins interact with nuclear RT histone acetyltransferases."; RL Oncogene 23:2559-2563(2004). RN [15] RP INTERACTION WITH NR2C2. RX PubMed=16887930; DOI=10.1074/mcp.M600180-MCP200; RA Huq M.D., Gupta P., Tsai N.P., Wei L.N.; RT "Modulation of testicular receptor 4 activity by mitogen-activated RT protein kinase-mediated phosphorylation."; RL Mol. Cell. Proteomics 5:2072-2082(2006). RN [16] RP INTERACTION WITH DDX17. RX PubMed=17226766; DOI=10.1002/jcb.21250; RA Shin S., Janknecht R.; RT "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the RT coactivators p300 and P/CAF."; RL J. Cell. Biochem. 101:1252-1265(2007). RN [17] RP INTERACTION WITH CEBPB. RX PubMed=17301242; DOI=10.1073/pnas.0607378104; RA Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.; RT "Glucocorticoid-stimulated preadipocyte differentiation is mediated RT through acetylation of C/EBPbeta by GCN5."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007). RN [18] RP IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX. RX PubMed=17707232; DOI=10.1016/j.molcel.2007.07.024; RA Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., RA Tempst P., Glass C.K., Rosenfeld M.G.; RT "A histone H2A deubiquitinase complex coordinating histone acetylation RT and H1 dissociation in transcriptional regulation."; RL Mol. Cell 27:609-621(2007). RN [19] RP INTERACTION WITH BCAS3. RX PubMed=17505058; DOI=10.1210/me.2006-0514; RA Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.; RT "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha RT coactivator, through proline-, glutamic acid-, and leucine-rich RT protein-1 (PELP1)."; RL Mol. Endocrinol. 21:1847-1860(2007). RN [20] RP FUNCTION. RX PubMed=23932781; DOI=10.1016/j.molcel.2013.07.002; RA Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.; RT "Acetylation stabilizes ATP-citrate lyase to promote lipid RT biosynthesis and tumor growth."; RL Mol. Cell 51:506-518(2013). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 493-658 IN COMPLEX WITH RP COENZYME A, AND ACTIVE SITE. RX PubMed=10393169; DOI=10.1093/emboj/18.13.3521; RA Clements A., Rojas J.R., Trievel R.C., Wang L., Berger S.L., RA Marmorstein R.; RT "Crystal structure of the histone acetyltransferase domain of the RT human PCAF transcriptional regulator bound to coenzyme A."; RL EMBO J. 18:3521-3532(1999). RN [22] RP STRUCTURE BY NMR OF 715-832, AND MUTAGENESIS OF VAL-752; TYR-760; RP TYR-802 AND TYR-809. RC TISSUE=Liver; RX PubMed=10365964; DOI=10.1038/20974; RA Dhalluin C., Carlson J.E., Zeng L., He C., Aggarwal A.K., Zhou M.-M.; RT "Structure and ligand of a histone acetyltransferase bromodomain."; RL Nature 399:491-496(1999). RN [23] RP STRUCTURE BY NMR OF 719-832 IN COMPLEX WITH HIV-1 TAT. RX PubMed=11931765; DOI=10.1016/S1097-2765(02)00483-5; RA Mujtaba S., He Y., Zeng L., Farooq A., Carlson J.E., Ott M., RA Verdin E., Zhou M.-M.; RT "Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF RT bromodomain."; RL Mol. Cell 9:575-586(2002). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 715-831. RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013; RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., RA Gingras A.C., Arrowsmith C.H., Knapp S.; RT "Histone recognition and large-scale structural analysis of the human RT bromodomain family."; RL Cell 149:214-231(2012). CC -!- FUNCTION: Functions as a histone acetyltransferase (HAT) to CC promote transcriptional activation. Has significant histone CC acetyltransferase activity with core histones (H3 and H4), and CC also with nucleosome core particles. Also acetylates non-histone CC proteins, such as ACLY. Inhibits cell-cycle progression and CC counteracts the mitogenic activity of the adenoviral oncoprotein CC E1A. In case of HIV-1 infection, it is recruited by the viral CC protein Tat. Regulates Tat's transactivating activity and may help CC inducing chromatin remodeling of proviral genes. Acts as a CC circadian transcriptional coactivator which enhances the activity CC of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CC CLOCK-ARNTL/BMAL1 heterodimers. {ECO:0000269|PubMed:10675335, CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:23932781, CC ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:9707565}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl- CC [histone]. {ECO:0000269|PubMed:8945521}. CC -!- SUBUNIT: Interacts with SIRT1. Interacts (unsumoylated form) with CC NR2C1; the interaction promotes transactivation activity (By CC similarity). Interacts with EP300, CREBBP and DDX17. Interacts CC with NCOA1 and NCOA3. Component of a large chromatin remodeling CC complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and CC KIF11/TRIP5. Interacts with NR2C2 (hypophosphorylated and CC unsumoylated form); the interaction promotes the transactivation CC activity of NR2C2. Binds to HTLV-1 Tax. Interacts with and CC acetylates HIV-1 Tat. Interacts with KLF1; the interaction does CC not acetylate KLF1 and there is no enhancement of its CC transactivational activity. Interacts with NFE4. Interacts with CC MECOM. Interacts with E2F1; the interaction acetylates E2F1 CC augmenting its DNA-binding and transcriptional activity. Interacts CC with NPAS2, ARNTL/BMAL1 and CLOCK. Interacts with BCAS3. Interacts CC with CEBPB (PubMed:17301242). Interacts with NR4A3 (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9JHD1, CC ECO:0000269|PubMed:10675335, ECO:0000269|PubMed:10766811, CC ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:11931765, CC ECO:0000269|PubMed:12486002, ECO:0000269|PubMed:14645221, CC ECO:0000269|PubMed:14767476, ECO:0000269|PubMed:15273251, CC ECO:0000269|PubMed:16887930, ECO:0000269|PubMed:17226766, CC ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:17505058, CC ECO:0000269|PubMed:17707232, ECO:0000269|PubMed:8684459, CC ECO:0000269|PubMed:9296499, ECO:0000269|PubMed:9346901, CC ECO:0000269|PubMed:9707565}. CC -!- INTERACTION: CC P03255:- (xeno); NbExp=3; IntAct=EBI-477430, EBI-2603114; CC P03255-2:- (xeno); NbExp=3; IntAct=EBI-477430, EBI-6859460; CC O60566:BUB1B; NbExp=14; IntAct=EBI-477430, EBI-1001438; CC Q92793:CREBBP; NbExp=4; IntAct=EBI-477430, EBI-81215; CC P03129:E7 (xeno); NbExp=3; IntAct=EBI-477430, EBI-866453; CC Q96KQ7:EHMT2; NbExp=3; IntAct=EBI-477430, EBI-744366; CC Q09472:EP300; NbExp=2; IntAct=EBI-477430, EBI-447295; CC Q16665:HIF1A; NbExp=2; IntAct=EBI-477430, EBI-447269; CC P02299:His3:CG31613 (xeno); NbExp=2; IntAct=EBI-477430, EBI-522090; CC P84040:His4 (xeno); NbExp=2; IntAct=EBI-477430, EBI-185028; CC Q96EB6:SIRT1; NbExp=3; IntAct=EBI-477430, EBI-1802965; CC Q8IXJ6:SIRT2; NbExp=4; IntAct=EBI-477430, EBI-477232; CC Q16594:TAF9; NbExp=3; IntAct=EBI-477430, EBI-712521; CC O88898-2:Tp63 (xeno); NbExp=3; IntAct=EBI-477430, EBI-2338228; CC Q15672:TWIST1; NbExp=2; IntAct=EBI-477430, EBI-1797287; CC P22415:USF1; NbExp=5; IntAct=EBI-477430, EBI-1054489; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed but most abundant in CC heart and skeletal muscle. {ECO:0000269|PubMed:8684459}. CC -!- DOMAIN: The bromodomain mediates binding to HIV-1 Tat. CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 bromo domain. {ECO:0000255|PROSITE- CC ProRule:PRU00035}. CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00532}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U57317; AAC50890.2; -; mRNA. DR EMBL; BC060823; AAH60823.1; -; mRNA. DR EMBL; BC070075; AAH70075.1; -; mRNA. DR CCDS; CCDS2634.1; -. DR PIR; S71788; S71788. DR RefSeq; NP_003875.3; NM_003884.4. DR UniGene; Hs.533055; -. DR PDB; 1CM0; X-ray; 2.30 A; A/B=493-658. DR PDB; 1JM4; NMR; -; B=719-832. DR PDB; 1N72; NMR; -; A=719-832. DR PDB; 1WUG; NMR; -; A=719-832. DR PDB; 1WUM; NMR; -; A=719-832. DR PDB; 1ZS5; NMR; -; A=719-832. DR PDB; 2RNW; NMR; -; A=719-832. DR PDB; 2RNX; NMR; -; A=719-832. DR PDB; 3GG3; X-ray; 2.25 A; A/B=715-831. DR PDB; 4NSQ; X-ray; 2.31 A; A/B/C/D=493-658. DR PDBsum; 1CM0; -. DR PDBsum; 1JM4; -. DR PDBsum; 1N72; -. DR PDBsum; 1WUG; -. DR PDBsum; 1WUM; -. DR PDBsum; 1ZS5; -. DR PDBsum; 2RNW; -. DR PDBsum; 2RNX; -. DR PDBsum; 3GG3; -. DR PDBsum; 4NSQ; -. DR ProteinModelPortal; Q92831; -. DR SMR; Q92831; 493-653, 719-832. DR BioGrid; 114375; 175. DR DIP; DIP-29778N; -. DR IntAct; Q92831; 36. DR MINT; MINT-150079; -. DR STRING; 9606.ENSP00000263754; -. DR BindingDB; Q92831; -. DR ChEMBL; CHEMBL5500; -. DR GuidetoPHARMACOLOGY; 2737; -. DR PhosphoSite; Q92831; -. DR BioMuta; KAT2B; -. DR DMDM; 83287776; -. DR REPRODUCTION-2DPAGE; Q92831; -. DR MaxQB; Q92831; -. DR PaxDb; Q92831; -. DR PRIDE; Q92831; -. DR Ensembl; ENST00000263754; ENSP00000263754; ENSG00000114166. DR GeneID; 8850; -. DR KEGG; hsa:8850; -. DR UCSC; uc003cbq.3; human. DR CTD; 8850; -. DR GeneCards; KAT2B; -. DR HGNC; HGNC:8638; KAT2B. DR HPA; CAB004526; -. DR HPA; HPA055839; -. DR MIM; 602303; gene. DR neXtProt; NX_Q92831; -. DR PharmGKB; PA162392705; -. DR eggNOG; KOG1472; Eukaryota. DR eggNOG; COG5076; LUCA. DR GeneTree; ENSGT00760000119099; -. DR HOGENOM; HOG000007151; -. DR InParanoid; Q92831; -. DR KO; K06062; -. DR OMA; HEDASNY; -. DR OrthoDB; EOG7ZKS9B; -. DR PhylomeDB; Q92831; -. DR TreeFam; TF105399; -. DR BRENDA; 2.3.1.48; 2681. DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation. DR Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression. DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants. DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-350054; Notch-HLH transcription pathway. DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation. DR ChiTaRS; KAT2B; human. DR EvolutionaryTrace; Q92831; -. DR GeneWiki; PCAF; -. DR GenomeRNAi; 8850; -. DR NextBio; 33221; -. DR PRO; PR:Q92831; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; Q92831; -. DR CleanEx; HS_KAT2B; -. DR Genevisible; Q92831; HS. DR GO; GO:0031672; C:A band; IEA:Ensembl. DR GO; GO:0042641; C:actomyosin; IEA:Ensembl. DR GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0031674; C:I band; IEA:Ensembl. DR GO; GO:0000776; C:kinetochore; IEA:Ensembl. DR GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0000125; C:PCAF complex; NAS:UniProtKB. DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; ISS:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB. DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB. DR GO; GO:0032403; F:protein complex binding; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription cofactor activity; IPI:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc. DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl. DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl. DR GO; GO:0006325; P:chromatin organization; TAS:Reactome. DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL. DR GO; GO:0043970; P:histone H3-K9 acetylation; IEA:Ensembl. DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB. DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl. DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome. DR GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:BHF-UCL. DR GO; GO:0035563; P:positive regulation of chromatin binding; IEA:Ensembl. DR GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0071442; P:positive regulation of histone H3-K14 acetylation; IEA:Ensembl. DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IEA:Ensembl. DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL. DR GO; GO:0045909; P:positive regulation of vasodilation; IEA:Ensembl. DR GO; GO:0006473; P:protein acetylation; TAS:ProtInc. DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; IDA:BHF-UCL. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0006360; P:transcription from RNA polymerase I promoter; TAS:Reactome. DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 1.20.920.10; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR016376; Hist_acetylase_PCAF. DR InterPro; IPR009464; PCAF_N. DR Pfam; PF13508; Acetyltransf_7; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF06466; PCAF_N; 1. DR PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 1. DR SUPFAM; SSF47370; SSF47370; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS51186; GNAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Acyltransferase; Biological rhythms; KW Bromodomain; Cell cycle; Complete proteome; Host-virus interaction; KW Nucleus; Polymorphism; Reference proteome; Transcription; KW Transcription regulation; Transferase. FT CHAIN 1 832 Histone acetyltransferase KAT2B. FT /FTId=PRO_0000211208. FT DOMAIN 503 651 N-acetyltransferase. FT {ECO:0000250|UniProtKB:Q92830, FT ECO:0000255|PROSITE-ProRule:PRU00532}. FT DOMAIN 740 810 Bromo. {ECO:0000255|PROSITE- FT ProRule:PRU00035, ECO:0000305}. FT REGION 574 576 Acetyl-CoA binding. FT {ECO:0000269|PubMed:10393169}. FT REGION 581 587 Acetyl-CoA binding. FT {ECO:0000269|PubMed:10393169}. FT REGION 612 615 Acetyl-CoA binding. FT {ECO:0000269|PubMed:10393169}. FT ACT_SITE 570 570 Proton donor/acceptor. FT {ECO:0000303|PubMed:10393169}. FT VARIANT 386 386 N -> S (in dbSNP:rs17006625). FT /FTId=VAR_034372. FT MUTAGEN 752 752 V->A: Reduced acetyl-lysine binding. FT {ECO:0000269|PubMed:10365964}. FT MUTAGEN 760 760 Y->A: Reduced acetyl-lysine binding. FT {ECO:0000269|PubMed:10365964}. FT MUTAGEN 802 802 Y->A: Reduced acetyl-lysine binding. FT {ECO:0000269|PubMed:10365964}. FT MUTAGEN 809 809 Y->A: Complete loss of acetyl-lysine FT binding. {ECO:0000269|PubMed:10365964}. FT CONFLICT 804 805 PP -> AA (in Ref. 1; AAC50890). FT {ECO:0000305}. FT STRAND 494 499 {ECO:0000244|PDB:1CM0}. FT STRAND 503 505 {ECO:0000244|PDB:1CM0}. FT HELIX 509 525 {ECO:0000244|PDB:1CM0}. FT HELIX 531 538 {ECO:0000244|PDB:1CM0}. FT STRAND 543 550 {ECO:0000244|PDB:1CM0}. FT STRAND 553 563 {ECO:0000244|PDB:1CM0}. FT TURN 564 567 {ECO:0000244|PDB:1CM0}. FT STRAND 568 576 {ECO:0000244|PDB:1CM0}. FT HELIX 578 580 {ECO:0000244|PDB:1CM0}. FT STRAND 582 584 {ECO:0000244|PDB:1CM0}. FT HELIX 585 599 {ECO:0000244|PDB:1CM0}. FT STRAND 604 609 {ECO:0000244|PDB:1CM0}. FT TURN 611 613 {ECO:0000244|PDB:1CM0}. FT HELIX 614 618 {ECO:0000244|PDB:1CM0}. FT TURN 619 621 {ECO:0000244|PDB:1CM0}. FT STRAND 623 625 {ECO:0000244|PDB:1CM0}. FT HELIX 630 633 {ECO:0000244|PDB:1CM0}. FT STRAND 644 649 {ECO:0000244|PDB:1CM0}. FT HELIX 727 741 {ECO:0000244|PDB:3GG3}. FT STRAND 742 744 {ECO:0000244|PDB:1WUM}. FT HELIX 746 748 {ECO:0000244|PDB:3GG3}. FT HELIX 754 756 {ECO:0000244|PDB:3GG3}. FT STRAND 757 759 {ECO:0000244|PDB:1ZS5}. FT HELIX 760 763 {ECO:0000244|PDB:3GG3}. FT STRAND 764 766 {ECO:0000244|PDB:1JM4}. FT HELIX 770 778 {ECO:0000244|PDB:3GG3}. FT HELIX 785 802 {ECO:0000244|PDB:3GG3}. FT STRAND 805 807 {ECO:0000244|PDB:1WUG}. FT HELIX 808 826 {ECO:0000244|PDB:3GG3}. FT STRAND 828 830 {ECO:0000244|PDB:1N72}. SQ SEQUENCE 832 AA; 93013 MW; 72F516E8BC00CC0C CRC64; MSEAGGAGPG GCGAGAGAGA GPGALPPQPA ALPPAPPQGS PCAAAAGGSG ACGPATAVAA AGTAEGPGGG GSARIAVKKA QLRSAPRAKK LEKLGVYSAC KAEESCKCNG WKNPNPSPTP PRADLQQIIV SLTESCRSCS HALAAHVSHL ENVSEEEMNR LLGIVLDVEY LFTCVHKEED ADTKQVYFYL FKLLRKSILQ RGKPVVEGSL EKKPPFEKPS IEQGVNNFVQ YKFSHLPAKE RQTIVELAKM FLNRINYWHL EAPSQRRLRS PNDDISGYKE NYTRWLCYCN VPQFCDSLPR YETTQVFGRT LLRSVFTVMR RQLLEQARQE KDKLPLEKRT LILTHFPKFL SMLEEEVYSQ NSPIWDQDFL SASSRTSQLG IQTVINPPPV AGTISYNSTS SSLEQPNAGS SSPACKASSG LEANPGEKRK MTDSHVLEEA KKPRVMGDIP MELINEVMST ITDPAAMLGP ETNFLSAHSA RDEAARLEER RGVIEFHVVG NSLNQKPNKK ILMWLVGLQN VFSHQLPRMP KEYITRLVFD PKHKTLALIK DGRVIGGICF RMFPSQGFTE IVFCAVTSNE QVKGYGTHLM NHLKEYHIKH DILNFLTYAD EYAIGYFKKQ GFSKEIKIPK TKYVGYIKDY EGATLMGCEL NPRIPYTEFS VIIKKQKEII KKLIERKQAQ IRKVYPGLSC FKDGVRQIPI ESIPGIRETG WKPSGKEKSK EPRDPDQLYS TLKSILQQVK SHQSAWPFME PVKRTEAPGY YEVIRFPMDL KTMSERLKNR YYVSKKLFMA DLQRVFTNCK EYNPPESEYY KCANILEKFF FSKIKEAGLI DK //