Histone acetyltransferase KAT2B

Details

Name
Histone acetyltransferase KAT2B
Synonyms
  • 2.3.1.48
  • Histone acetylase PCAF
  • Histone acetyltransferase PCAF
  • Lysine acetyltransferase 2B
  • P/CAF
  • P300/CBP-associated factor
  • PCAF
Gene Name
KAT2B
Organism
Humans
Amino acid sequence
>lcl|BSEQ0021330|Histone acetyltransferase KAT2B
MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAA
AGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTP
PRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEED
ADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKE
RQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPR
YETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQ
NSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSG
LEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSA
RDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFD
PKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKH
DILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFS
VIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSK
EPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNR
YYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK
Number of residues
832
Molecular Weight
93012.295
Theoretical pI
9.37
GO Classification
Functions
acetyltransferase activity / chromatin binding / cyclin-dependent protein serine/threonine kinase inhibitor activity / histone acetyltransferase activity / histone deacetylase binding / lysine N-acetyltransferase activity, acting on acetyl phosphate as donor / protein complex binding / protein kinase binding / RNA polymerase II regulatory region sequence-specific DNA binding / transcription coactivator activity / transcription cofactor activity / transcription factor binding
Processes
cell cycle arrest / cellular response to insulin stimulus / cellular response to oxidative stress / cellular response to parathyroid hormone stimulus / chromatin organization / chromatin remodeling / gene expression / histone H3 acetylation / histone H3-K9 acetylation / internal peptidyl-lysine acetylation / memory / N-terminal peptidyl-lysine acetylation / negative regulation of cell proliferation / negative regulation of cyclin-dependent protein serine/threonine kinase activity / Notch signaling pathway / peptidyl-lysine acetylation / positive regulation of chromatin binding / positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter / positive regulation of histone H3-K14 acetylation / positive regulation of histone H3-K9 acetylation / positive regulation of neuron projection development / positive regulation of transcription from RNA polymerase II promoter / positive regulation of vasodilation / protein acetylation / regulation of protein ADP-ribosylation / rhythmic process / transcription from RNA polymerase I promoter / transcription initiation from RNA polymerase I promoter / transcription initiation from RNA polymerase II promoter / viral process
Components
A band / actomyosin / Ada2/Gcn5/Ada3 transcription activator complex / cytosol / I band / kinetochore / nuclear chromatin / nucleoplasm / nucleus / PCAF complex
General Function
Transcription factor binding
Specific Function
Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0021331|Histone acetyltransferase KAT2B (KAT2B)
ATGTCCGAGGCTGGCGGGGCCGGGCCGGGCGGCTGCGGGGCAGGAGCCGGGGCAGGGGCC
GGGCCCGGGGCGCTGCCCCCGCAGCCTGCGGCGCTTCCGCCCGCGCCCCCGCAGGGCTCC
CCCTGCGCCGCTGCCGCCGGGGGCTCGGGCGCCTGCGGTCCGGCGACGGCAGTGGCTGCA
GCGGGCACGGCCGAAGGACCGGGAGGCGGTGGCTCGGCCCGAATCGCCGTGAAGAAAGCG
CAACTACGCTCCGCTCCGCGGGCCAAGAAACTGGAGAAACTCGGAGTGTACTCCGCCTGC
AAGGCCGAGGAGTCTTGTAAATGTAATGGCTGGAAAAACCCTAACCCCTCACCCACTCCC
CCCAGAGCCGACCTGCAGCAAATAATTGTCAGTCTAACAGAATCCTGTCGGAGTTGTAGC
CATGCCCTAGCTGCTCATGTTTCCCACCTGGAGAATGTGTCAGAGGAAGAAATGAACAGA
CTCCTGGGAATAGTATTGGATGTGGAATATCTCTTTACCTGTGTCCACAAGGAAGAAGAT
GCAGATACCAAACAAGTTTATTTCTATCTATTTAAGCTCTTGAGAAAGTCTATTTTACAA
AGAGGAAAACCTGTGGTTGAAGGCTCTTTGGAAAAGAAACCCCCATTTGAAAAACCTAGC
ATTGAACAGGGTGTGAATAACTTTGTGCAGTACAAATTTAGTCACCTGCCAGCAAAAGAA
AGGCAAACAATAGTTGAGTTGGCAAAAATGTTCCTAAACCGCATCAACTATTGGCATCTG
GAGGCACCATCTCAACGAAGACTGCGATCTCCCAATGATGATATTTCTGGATACAAAGAG
AACTACACAAGGTGGCTGTGTTACTGCAACGTGCCACAGTTCTGCGACAGTCTACCTCGG
TACGAAACCACACAGGTGTTTGGGAGAACATTGCTTCGCTCGGTCTTCACTGTTATGAGG
CGACAACTCCTGGAACAAGCAAGACAGGAAAAAGATAAACTGCCTCTTGAAAAACGAACT
CTAATCCTCACTCATTTCCCAAAATTTCTGTCCATGCTAGAAGAAGAAGTATATAGTCAA
AACTCTCCCATCTGGGATCAGGATTTTCTCTCAGCCTCTTCCAGAACCAGCCAGCTAGGC
ATCCAAACAGTTATCAATCCACCTCCTGTGGCTGGGACAATTTCATACAATTCAACCTCA
TCTTCCCTTGAGCAGCCAAACGCAGGGAGCAGCAGTCCTGCCTGCAAAGCCTCTTCTGGA
CTTGAGGCAAACCCAGGAGAAAAGAGGAAAATGACTGATTCTCATGTTCTGGAGGAGGCC
AAGAAACCCCGAGTTATGGGGGATATTCCGATGGAATTAATCAACGAGGTTATGTCTACC
ATCACGGACCCTGCAGCAATGCTTGGACCAGAGACCAATTTTCTGTCAGCACACTCGGCC
AGGGATGAGGCGGCAAGGTTGGAAGAGCGCAGGGGTGTAATTGAATTTCACGTGGTTGGC
AATTCCCTCAACCAGAAACCAAACAAGAAGATCCTGATGTGGCTGGTTGGCCTACAGAAC
GTTTTCTCCCACCAGCTGCCCCGAATGCCAAAAGAATACATCACACGGCTCGTCTTTGAC
CCGAAACACAAAACCCTTGCTTTAATTAAAGATGGCCGTGTTATTGGTGGTATCTGTTTC
CGTATGTTCCCATCTCAAGGATTCACAGAGATTGTCTTCTGTGCTGTAACCTCAAATGAG
CAAGTCAAGGGCTATGGAACACACCTGATGAATCATTTGAAAGAATATCACATAAAGCAT
GACATCCTGAACTTCCTCACATATGCAGATGAATATGCAATTGGATACTTTAAGAAACAG
GGTTTCTCCAAAGAAATTAAAATACCTAAAACCAAATATGTTGGCTATATCAAGGATTAT
GAAGGAGCCACTTTAATGGGATGTGAGCTAAATCCACGGATCCCGTACACAGAATTTTCT
GTCATCATTAAAAAGCAGAAGGAGATAATTAAAAAACTGATTGAAAGAAAACAGGCACAA
ATTCGAAAAGTTTACCCTGGACTTTCATGTTTTAAAGATGGAGTTCGACAGATTCCTATA
GAAAGCATTCCTGGAATTAGAGAGACAGGCTGGAAACCGAGTGGAAAAGAGAAAAGTAAA
GAGCCCAGAGACCCTGACCAGCTTTACAGCACGCTCAAGAGCATCCTCCAGCAGGTGAAG
AGCCATCAAAGCGCTTGGCCCTTCATGGAACCTGTGAAGAGAACAGAAGCTCCAGGATAT
TATGAAGTTATAAGGTTCCCCATGGATCTGAAAACCATGAGTGAACGCCTCAAGAATAGG
TACTACGTGTCTAAGAAATTATTCATGGCAGACTTACAGCGAGTCTTTACCAATTGCAAA
GAGTACAACCCCCCTGAGAGTGAATACTACAAATGTGCCAATATCCTGGAGAAATTCTTC
TTCAGTAAAATTAAGGAAGCTGGATTAATTGACAAGTGA
Chromosome Location
3
Locus
3p24
External Identifiers
ResourceLink
UniProtKB IDQ92831
UniProtKB Entry NameKAT2B_HUMAN
GenBank Gene IDU57317
GenAtlas IDPCAF
HGNC IDHGNC:8638
General References
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  3. Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y: The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 1996 Nov 29;87(5):953-9. [Article]
  4. Takeshita A, Cardona GR, Koibuchi N, Suen CS, Chin WW: TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J Biol Chem. 1997 Oct 31;272(44):27629-34. [Article]
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  6. Zhang W, Bieker JJ: Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases. Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9855-60. [Article]
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  9. Chakraborty S, Senyuk V, Sitailo S, Chi Y, Nucifora G: 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. J Biol Chem. 2001 Nov 30;276(48):44936-43. Epub 2001 Sep 21. [Article]
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  15. Shin S, Janknecht R: Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF. J Cell Biochem. 2007 Aug 1;101(5):1252-65. [Article]
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  19. Lin R, Tao R, Gao X, Li T, Zhou X, Guan KL, Xiong Y, Lei QY: Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth. Mol Cell. 2013 Aug 22;51(4):506-18. doi: 10.1016/j.molcel.2013.07.002. Epub 2013 Aug 8. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01992Coenzyme Ainvestigational, nutraceuticalunknownDetails
DB08186(3E)-4-(1-METHYL-1H-INDOL-3-YL)BUT-3-EN-2-ONEexperimentalunknownDetails
DB08291N-(3-AMINOPROPYL)-2-NITROBENZENAMINEexperimentalunknownDetails