Details for: KAT2B

Gene ID: 8850

Symbol: KAT2B

Ensembl ID: ENSG00000114166

Description: lysine acetyltransferase 2B

Associated with

Other Information

Genular Protein ID: 3193514494

Symbol: KAT2B_HUMAN

Name: Histone acetyltransferase KAT2B

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 8684459

Title: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A.

PubMed ID: 8684459

DOI: 10.1038/382319a0

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8945521

Title: The transcriptional coactivators p300 and CBP are histone acetyltransferases.

PubMed ID: 8945521

DOI: 10.1016/s0092-8674(00)82001-2

PubMed ID: 9346901

Title: TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1.

PubMed ID: 9346901

DOI: 10.1074/jbc.272.44.27629

PubMed ID: 9296499

Title: Steroid receptor coactivator-1 is a histone acetyltransferase.

PubMed ID: 9296499

DOI: 10.1038/38304

PubMed ID: 9707565

Title: Acetylation and modulation of erythroid Krueppel-like factor (EKLF) activity by interaction with histone acetyltransferases.

PubMed ID: 9707565

DOI: 10.1073/pnas.95.17.9855

PubMed ID: 10675335

Title: Regulation of E2F1 activity by acetylation.

PubMed ID: 10675335

DOI: 10.1093/emboj/19.4.662

PubMed ID: 10766811

Title: p300 and p300/cAMP-responsive element-binding protein associated factor interact with human T-cell lymphotropic virus type-1 Tax in a multi-histone acetyltransferase/activator-enhancer complex.

PubMed ID: 10766811

DOI: 10.1074/jbc.275.16.11852

PubMed ID: 11568182

Title: Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles.

PubMed ID: 11568182

DOI: 10.1074/jbc.m106733200

PubMed ID: 12486002

Title: Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF.

PubMed ID: 12486002

DOI: 10.1093/emboj/cdf669

PubMed ID: 14645221

Title: Histone acetyltransferase-dependent chromatin remodeling and the vascular clock.

PubMed ID: 14645221

DOI: 10.1074/jbc.m311973200

PubMed ID: 15273251

Title: Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1.

PubMed ID: 15273251

DOI: 10.1074/jbc.m405129200

PubMed ID: 14767476

Title: The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases.

PubMed ID: 14767476

DOI: 10.1038/sj.onc.1207424

PubMed ID: 16887930

Title: Modulation of testicular receptor 4 activity by mitogen-activated protein kinase-mediated phosphorylation.

PubMed ID: 16887930

DOI: 10.1074/mcp.m600180-mcp200

PubMed ID: 17226766

Title: Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF.

PubMed ID: 17226766

DOI: 10.1002/jcb.21250

PubMed ID: 17301242

Title: Glucocorticoid-stimulated preadipocyte differentiation is mediated through acetylation of C/EBPbeta by GCN5.

PubMed ID: 17301242

DOI: 10.1073/pnas.0607378104

PubMed ID: 17707232

Title: A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation.

PubMed ID: 17707232

DOI: 10.1016/j.molcel.2007.07.024

PubMed ID: 17505058

Title: Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1).

PubMed ID: 17505058

DOI: 10.1210/me.2006-0514

PubMed ID: 20940255

Title: Acetylation of Rb by PCAF is required for nuclear localization and keratinocyte differentiation.

PubMed ID: 20940255

DOI: 10.1242/jcs.068924

PubMed ID: 27389534

Title: P/CAF-mediated spermidine acetylation regulates histone acetyltransferase activity.

PubMed ID: 27389534

DOI: 10.1080/14756366.2016.1205045

PubMed ID: 23001180

Title: EB1 acetylation by P300/CBP-associated factor (PCAF) ensures accurate kinetochore-microtubule interactions in mitosis.

PubMed ID: 23001180

DOI: 10.1073/pnas.1202639109

PubMed ID: 23932781

Title: Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth.

PubMed ID: 23932781

DOI: 10.1016/j.molcel.2013.07.002

PubMed ID: 25593309

Title: Screen identifies bromodomain protein ZMYND8 in chromatin recognition of transcription-associated DNA damage that promotes homologous recombination.

PubMed ID: 25593309

DOI: 10.1101/gad.252189.114

PubMed ID: 27796307

Title: KAT2A/KAT2B-targeted acetylome reveals a role for PLK4 acetylation in preventing centrosome amplification.

PubMed ID: 27796307

DOI: 10.1038/ncomms13227

PubMed ID: 26867678

Title: SIRT7-dependent deacetylation of the U3-55k protein controls pre-rRNA processing.

PubMed ID: 26867678

DOI: 10.1038/ncomms10734

PubMed ID: 29174768

Title: Acetylation of TBX5 by KAT2B and KAT2A regulates heart and limb development.

PubMed ID: 29174768

DOI: 10.1016/j.yjmcc.2017.11.013

PubMed ID: 10393169

Title: Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A.

PubMed ID: 10393169

DOI: 10.1093/emboj/18.13.3521

PubMed ID: 10365964

Title: Structure and ligand of a histone acetyltransferase bromodomain.

PubMed ID: 10365964

DOI: 10.1038/20974

PubMed ID: 11931765

Title: Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain.

PubMed ID: 11931765

DOI: 10.1016/s1097-2765(02)00483-5

PubMed ID: 22464331

Title: Histone recognition and large-scale structural analysis of the human bromodomain family.

PubMed ID: 22464331

DOI: 10.1016/j.cell.2012.02.013

PubMed ID: 28493397

Title: A recurrent de novo mutation in ACTG1 causes isolated ocular coloboma.

PubMed ID: 28493397

DOI: 10.1002/humu.23246

Sequence Information:

  • Length: 832
  • Mass: 93013
  • Checksum: 72F516E8BC00CC0C
  • Sequence:
  • 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

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.