Histone acetyltransferase KAT2A

Details

Name
Histone acetyltransferase KAT2A
Synonyms
  • 2.3.1.48
  • GCN5
  • GCN5L2
  • General control of amino acid synthesis protein 5-like 2
  • HGCN5
  • Histone acetyltransferase GCN5
  • HsGCN5
  • Lysine acetyltransferase 2A
  • STAF97
Gene Name
KAT2A
Organism
Humans
Amino acid sequence
>lcl|BSEQ0009504|Histone acetyltransferase KAT2A
MAEPSQAPTPAPAAQPRPLQSPAPAPTPTPAPSPASAPIPTPTPAPAPAPAAAPAGSTGT
GGPGVGSGGAGSGGDPARPGLSQQQRASQRKAQVRGLPRAKKLEKLGVFSACKANETCKC
NGWKNPKPPTAPRMDLQQPAANLSELCRSCEHPLADHVSHLENVSEDEINRLLGMVVDVE
NLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMTRPVVEGSLGSPPFEKPNIEQGVLNFVQ
YKFSHLAPRERQTMFELSKMFLLCLNYWKLETPAQFRQRSQAEDVATYKVNYTRWLCYCH
VPQSCDSLPRYETTHVFGRSLLRSIFTVTRRQLLEKFRVEKDKLVPEKRTLILTHFPKFL
SMLEEEIYGANSPIWESGFTMPPSEGTQLVPRPASVSAAVVPSTPIFSPSMGGGSNSSLS
LDSAGAEPMPGEKRTLPENLTLEDAKRLRVMGDIPMELVNEVMLTITDPAAMLGPETSLL
SANAARDETARLEERRGIIEFHVIGNSLTPKANRRVLLWLVGLQNVFSHQLPRMPKEYIA
RLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKE
YHIKHNILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIP
YTELSHIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKEGVRQIPVESVPGIRETGWKPLG
KEKGKELKDPDQLYTTLKNLLAQIKSHPSAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTE
RLRSRYYVTRKLFVADLQRVIANCREYNPPDSEYCRCASALEKFFYFKLKEGGLIDK
Number of residues
837
Molecular Weight
93924.72
Theoretical pI
Not Available
GO Classification
Functions
chromatin binding / H3 histone acetyltransferase activity / histone acetyltransferase activity / histone acetyltransferase activity (H4-K12 specific) / histone deacetylase binding / transcription coactivator activity / transcription factor binding
Processes
alpha-tubulin acetylation / cardiac muscle cell differentiation / cell proliferation / cellular response to nerve growth factor stimulus / cellular response to tumor necrosis factor / chromatin organization / chromatin remodeling / histone deubiquitination / histone H3 acetylation / histone H3-K14 acetylation / in utero embryonic development / intracellular distribution of mitochondria / metencephalon development / midbrain development / multicellular organism growth / neural tube closure / positive regulation of cell projection organization / positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter / positive regulation of histone acetylation / positive regulation of protein targeting to mitochondrion / positive regulation of transcription regulatory region DNA binding / regulation of mitophagy / regulation of protein stability / regulation of transcription from RNA polymerase II promoter / response to nutrient levels / response to organic cyclic compound / somitogenesis / telencephalon development / transcription from RNA polymerase II promoter / viral process
Components
Ada2/Gcn5/Ada3 transcription activator complex / extracellular space / mitotic spindle / nuclear chromatin / nucleoplasm / STAGA complex / transcription factor TFTC complex
General Function
Transcription factor binding
Specific Function
Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles. Also acetylates non-histone proteins, such as CEBPB (PubMed:17301242). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0017480|Histone acetyltransferase KAT2A (KAT2A)
ATGGCGGAACCTTCCCAGGCCCCGACCCCGGCCCCGGCTGCGCAGCCCCGGCCCCTTCAG
TCCCCAGCCCCTGCCCCAACTCCGACTCCTGCACCCAGCCCGGCTTCAGCCCCGATTCCG
ACTCCCACCCCGGCACCAGCCCCTGCCCCAGCTGCAGCCCCAGCCGGCAGCACAGGGACT
GGGGGGCCCGGGGTAGGAAGTGGGGGGGCCGGGAGCGGGGGGGATCCGGCTCGACCTGGC
CTGAGCCAGCAGCAGCGCGCCAGTCAGAGGAAGGCGCAAGTCCGGGGGCTGCCGCGCGCC
AAGAAGCTTGAGAAGCTAGGGGTCTTCTCGGCTTGCAAGGCCAATGAAACCTGTAAGTGT
AATGGCTGGAAAAACCCCAAGCCCCCCACTGCACCCCGCATGGATCTGCAGCAGCCAGCT
GCCAACCTGAGTGAGCTGTGCCGCAGTTGTGAGCACCCCTTGGCTGACCACGTATCCCAC
TTGGAGAATGTGTCAGAGGATGAGATAAACCGACTGCTGGGGATGGTGGTGGATGTGGAG
AATCTCTTCATGTCTGTTCACAAGGAAGAGGACACAGACACCAAGCAGGTCTATTTCTAC
CTCTTCAAGCTACTGCGGAAATGCATCCTGCAGATGACCCGGCCTGTGGTGGAGGGGTCC
CTGGGCAGCCCTCCATTTGAGAAACCTAATATTGAGCAGGGTGTGCTGAACTTTGTGCAG
TACAAGTTTAGTCACCTGGCTCCCCGGGAGCGGCAGACGATGTTCGAGCTCTCAAAGATG
TTCTTGCTCTGCCTTAACTACTGGAAGCTTGAGACACCTGCCCAGTTTCGGCAGAGGTCT
CAGGCTGAGGACGTGGCTACCTACAAGGTCAATTACACCAGATGGCTCTGTTACTGCCAC
GTGCCCCAGAGCTGTGATAGCCTCCCCCGCTACGAAACCACTCATGTCTTTGGGCGAAGC
CTTCTCCGGTCCATTTTCACCGTTACCCGCCGGCAGCTGCTGGAAAAGTTCCGAGTGGAG
AAGGACAAATTGGTGCCCGAGAAGAGGACCCTCATCCTCACTCACTTCCCCAAATTCCTG
TCCATGCTGGAGGAGGAGATCTATGGGGCAAACTCTCCAATCTGGGAGTCAGGCTTCACC
ATGCCACCCTCAGAGGGGACACAGCTGGTTCCCCGGCCAGCTTCAGTCAGTGCAGCGGTT
GTTCCCAGCACCCCCATCTTCAGCCCCAGCATGGGTGGGGGCAGCAACAGCTCCCTGAGT
CTGGATTCTGCAGGGGCCGAGCCTATGCCAGGCGAGAAGAGGACGCTCCCAGAGAACCTG
ACCCTGGAGGATGCCAAGCGGCTCCGTGTGATGGGTGACATCCCCATGGAGCTGGTCAAT
GAGGTCATGCTGACCATCACTGACCCTGCTGCCATGCTGGGGCCTGAGACGAGCCTGCTT
TCGGCCAATGCGGCCCGGGATGAGACAGCCCGCCTGGAGGAGCGCCGCGGCATCATCGAG
TTCCATGTCATCGGCAACTCACTGACGCCCAAGGCCAACCGGCGGGTGTTGCTGTGGCTC
GTGGGGCTGCAGAATGTCTTTTCCCACCAGCTGCCGCGCATGCCTAAGGAGTATATCGCC
CGCCTCGTCTTTGACCCGAAGCACAAGACTCTGGCCTTGATCAAGGATGGGCGGGTCATC
GGTGGCATCTGCTTCCGCATGTTTCCCACCCAGGGCTTCACGGAGATTGTCTTCTGTGCT
GTCACCTCGAATGAGCAGGTCAAGGGTTATGGGACCCACCTGATGAACCACCTGAAGGAG
TATCACATCAAGCACAACATTCTCTACTTCCTCACCTACGCCGACGAGTACGCCATCGGC
TACTTCAAAAAGCAGGGTTTCTCCAAGGACATCAAGGTGCCCAAGAGCCGCTACCTGGGC
TACATCAAGGACTACGAGGGAGCGACGCTGATGGAGTGTGAGCTGAATCCCCGCATCCCC
TACACGGAGCTGTCCCACATCATCAAGAAGCAGAAAGAGATCATCAAGAAGCTGATTGAG
CGCAAACAGGCCCAGATCCGCAAGGTCTACCCGGGGCTCAGCTGCTTCAAGGAGGGCGTG
AGGCAGATCCCTGTGGAGAGCGTTCCTGGCATTCGAGAGACAGGCTGGAAGCCATTGGGG
AAGGAGAAGGGGAAGGAGCTGAAGGACCCCGACCAGCTCTACACAACCCTCAAAAACCTG
CTGGCCCAAATCAAGTCTCACCCCAGTGCCTGGCCCTTCATGGAGCCTGTGAAGAAGTCG
GAGGCCCCTGACTACTACGAGGTCATCCGCTTCCCCATTGACCTGAAGACCATGACTGAG
CGGCTGCGAAGCCGCTACTACGTGACCCGGAAGCTCTTTGTGGCCGACCTGCAGCGGGTC
ATCGCCAACTGTCGCGAGTACAACCCCCCGGACAGCGAGTACTGCCGCTGTGCCAGCGCC
CTGGAGAAGTTCTTCTACTTCAAGCTCAAGGAGGGAGGCCTCATTGACAAGTAG
Chromosome Location
17
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ92830
UniProtKB Entry NameKAT2A_HUMAN
HGNC IDHGNC:4201
General References
  1. Candau R, Moore PA, Wang L, Barlev N, Ying CY, Rosen CA, Berger SL: Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5. Mol Cell Biol. 1996 Feb;16(2):593-602. [Article]
  2. Smith ER, Belote JM, Schiltz RL, Yang XJ, Moore PA, Berger SL, Nakatani Y, Allis CD: Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members. Nucleic Acids Res. 1998 Jun 15;26(12):2948-54. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [Article]
  5. Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG: Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. Mol Cell Biol. 2001 Oct;21(20):6782-95. [Article]
  6. Brand M, Yamamoto K, Staub A, Tora L: Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. J Biol Chem. 1999 Jun 25;274(26):18285-9. [Article]
  7. McMahon SB, Wood MA, Cole MD: The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc. Mol Cell Biol. 2000 Jan;20(2):556-62. [Article]
  8. Col E, Caron C, Seigneurin-Berny D, Gracia J, Favier A, Khochbin S: The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat. J Biol Chem. 2001 Jul 27;276(30):28179-84. Epub 2001 May 30. [Article]
  9. Gangloff YG, Pointud JC, Thuault S, Carre L, Romier C, Muratoglu S, Brand M, Tora L, Couderc JL, Davidson I: The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger. Mol Cell Biol. 2001 Aug;21(15):5109-21. [Article]
  10. Gangisetty O, Lauffart B, Sondarva GV, Chelsea DM, Still IH: The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases. Oncogene. 2004 Apr 1;23(14):2559-63. [Article]
  11. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [Article]
  12. Wiper-Bergeron N, Salem HA, Tomlinson JJ, Wu D, Hache RJ: Glucocorticoid-stimulated preadipocyte differentiation is mediated through acetylation of C/EBPbeta by GCN5. Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2703-8. Epub 2007 Feb 14. [Article]
  13. Zhao Y, Lang G, Ito S, Bonnet J, Metzger E, Sawatsubashi S, Suzuki E, Le Guezennec X, Stunnenberg HG, Krasnov A, Georgieva SG, Schule R, Takeyama K, Kato S, Tora L, Devys D: A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing. Mol Cell. 2008 Jan 18;29(1):92-101. doi: 10.1016/j.molcel.2007.12.011. [Article]
  14. Guelman S, Kozuka K, Mao Y, Pham V, Solloway MJ, Wang J, Wu J, Lill JR, Zha J: The double-histone-acetyltransferase complex ATAC is essential for mammalian development. Mol Cell Biol. 2009 Mar;29(5):1176-88. doi: 10.1128/MCB.01599-08. Epub 2008 Dec 22. [Article]
  15. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
  16. Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE: Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. J Mol Biol. 2000 Dec 1;304(3):355-70. [Article]
  17. Schuetz A, Bernstein G, Dong A, Antoshenko T, Wu H, Loppnau P, Bochkarev A, Plotnikov AN: Crystal structure of a binary complex between human GCN5 histone acetyltransferase domain and acetyl coenzyme A. Proteins. 2007 Jul 1;68(1):403-7. [Article]
  18. Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Muller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S: Histone recognition and large-scale structural analysis of the human bromodomain family. Cell. 2012 Mar 30;149(1):214-31. doi: 10.1016/j.cell.2012.02.013. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01992Coenzyme Ainvestigational, nutraceuticalunknownDetails