Identifiers and Description

Gene Model Identifier

TTHERM_00248390

Standard Name

HAT2 (Histone AcetylTransferase 2)

Aliases

PreTt02535 | 21.m00382 | GCN5

Description

Member of the SAGA complex. Histone acetyltransferase; homolog of Saccharomyces cerevisiae GCN5; contains bromodomain

Genome Browser (Macronucleus)

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Genome Browser (Micronucleus)

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Gene Ontology Annotations

Cellular Component

Molecular Function

Biological Process

Domains

  • ( PF00439 ) Bromodomain
  • ( PF00583 ) acetyltransferase, GNAT family
  • ( TIGR01575 ) ribosomal-protein-alanine acetyltransferase

Gene Expression Profile

  • Tetrahymena Functional Genomics Database:

Change in Gene Expression

TMHMM

TMHMM

Signal Peptide

Signal Peptide Present?: No
Presense Probability: 10.6%

TetraMine Data

TTHERM_00248390

WebApollo

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Tetrahymena Stock Center

No Data fetched for StockID

Homologs (v.2006 protein sequences)

SourceIdentifierScoreDescription
Tetrahymena borealisEI9_00461.19.997093137033517e-262histone acetyltransferase gcn5
(419 aa)
OxytrichaContig18994.0.g686.999054974866289e-109Bromodomain
SGDYGR252W6.997194614751282e-100GCN5 Acetyltransferase, modifi
es N-terminal lysines on histo
nes H2B and H3; acetylates Rsc
4p, a subunit of the RSC chrom
atin-remodeling complex, alter
ing replication stress toleran
ce; catalytic subunit of the A
DA and SAGA histone acetyltran
sferase complexes; founding me
mber of the Gcn5p-related N-ac
etyltransferase superfamily; m
utant displays reduced transcr
iption elongation in the G-les
s-based run-on (GLRO) assay
DictyBaseDDB_G02834592.999180586171967e-98gcn5 on chromosome: 4 position
727119 to 728357
WormBaseWBGene000216366.996899116468003e-76locus:pcaf-1 status:Partiall
y_confirmed UniProt:Q9N3S7
protein_id:CCD72550.1
Stentor CoeruleusSteCoe_375717.47197233734299e-43

General Information

No Data fetched for General Information

Associated Literature

  1. Ref:29523178: Saettone A, Garg J, Lambert JP, Nabeel-Shah S, Ponce M, Burtch A, Thuppu Mudalige C, Gingras AC, Pearlman RE, Fillingham J (2018) The bromodomain-containing protein Ibd1 links multiple chromatin-related protein complexes to highly expressed genes in Tetrahymena thermophila. Epigenetics & chromatin 11(1):10
  2. Ref:17189264: Morris SA, Rao B, Garcia BA, Hake SB, Diaz RL, Shabanowitz J, Hunt DF, Allis CD, Lieb JD, Strahl BD (2007) Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification. The Journal of biological chemistry 282(10):7632-40
  3. Ref:17070031: Couture JF, Trievel RC (2006) Histone-modifying enzymes: encrypting an enigmatic epigenetic code. Current opinion in structural biology 16(6):753-60
  4. Ref:16060659: Zheng Y, Mamdani F, Toptygin D, Brand L, Stivers JT, Cole PA (2005) Fluorescence analysis of a dynamic loop in the PCAF/GCN5 histone acetyltransferase. Biochemistry 44(31):10501-9
  5. Ref:14536085: Clements A, Poux AN, Lo WS, Pillus L, Berger SL, Marmorstein R (2003) Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase. Molecular cell 12(2):461-73
  6. Ref:14661947: Poux AN, Marmorstein R (2003) Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates. Biochemistry 42(49):14366-74
  7. Ref:11994311: Langer MR, Fry CJ, Peterson CL, Denu JM (2002) Modulating acetyl-CoA binding in the GCN5 family of histone acetyltransferases. The Journal of biological chemistry 277(30):27337-44
  8. Ref:11135657: Tan S (2001) One HAT size fits all? Nature structural biology 8(1):8-10
  9. Ref:11112280: Trievel RC, Li FY, Marmorstein R (2000) Application of a fluorescent histone acetyltransferase assay to probe the substrate specificity of the human p300/CBP-associated factor. Analytical biochemistry 287(2):319-28
  10. Ref:10536141: Hettmann C, Soldati D (1999) Cloning and analysis of a Toxoplasma gondii histone acetyltransferase: a novel chromatin remodelling factor in Apicomplexan parasites. Nucleic acids research 27(22):4344-52
  11. Ref:10485713: Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, Berger SL, Allis CD, Marmorstein R (1999) Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Nature 401(6748):93-8
  12. Ref:10022893: Ohba R, Steger DJ, Brownell JE, Mizzen CA, Cook RG, Côté J, Workman JL, Allis CD (1999) A novel H2A/H4 nucleosomal histone acetyltransferase in Tetrahymena thermophila. Molecular and cellular biology 19(3):2061-8
  13. Ref:10403255: Lin Y, Fletcher CM, Zhou J, Allis CD, Wagner G (1999) Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A. Nature 400(6739):86-9
  14. Ref:9697775: Utley RT, Ikeda K, Grant PA, Côté J, Steger DJ, Eberharter A, John S, Workman JL (1998) Transcriptional activators direct histone acetyltransferase complexes to nucleosomes. Nature 394(6692):498-502
  15. Ref:9115421: Tsukiyama T, Wu C (1997) Chromatin remodeling and transcription. Current opinion in genetics & development 7(2):182-91
  16. Ref:8601308: Brownell JE, Zhou J, Ranalli T, Kobayashi R, Edmondson DG, Roth SY, Allis CD (1996) Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84(6):843-51
  17. Ref:15157517: Roth SY, Allis CD (1996) The subunit-exchange model of histone acetylation. Trends in cell biology 6(10):371-5
  18. Ref:8805705: Kuo MH, Brownell JE, Sobel RE, Ranalli TA, Cook RG, Edmondson DG, Roth SY, Allis CD (1996) Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Nature 383(6597):269-72
  19. Ref:7603997: Brownell JE, Allis CD (1995) An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei. Proceedings of the National Academy of Sciences of the United States of America 92(14):6364-8
  20. Ref:8034606: Sobel RE, Cook RG, Allis CD (1994) Non-random acetylation of histone H4 by a cytoplasmic histone acetyltransferase as determined by novel methodology. The Journal of biological chemistry 269(28):18576-82
  21. Ref:SUPR000150
  22. Ref:SUPR000151

Sequences 

>TTHERM_00248390(protein)
MADQEKSAQDAQNAAPQETAFVGMNGEETGLGFATRDQGAKVEEDQGLLDFDILTNDGTH
RNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMVILKNKQKVIGGICFRQYKPQRF
AEVAFLAVTANEQVRGYGTRLMNKFKDHMQKQNIEYLLTYADNFAIGYFKKQGFTKEHRM
PQEKWKGYIKDYDGGTLMECYIHPYVDYGNISQIIKRQKELLIERIKKLSLNEKVFSGKE
YAALIQNSMDNEDPENPKVNPSDIPGVAFSGWEWKDYHELKKSKERSFNLQCANVIENMK
RHKQSWPFLDPVNKDDVPDYYDVITDPIDIKAIEKKLQNNQYVDKDQFIKDVKRIFTNAK
IYNQPDTIYYKAAKELEDFVEPYLTKLKDTKESNTPSNNNSAHGSKKPLPVRKSIKKK


>TTHERM_00248390(coding)
ATGGCTGATTAAGAAAAATCTGCTTAAGATGCATAGAATGCAGCACCATAAGAGACTGCA
TTTGTAGGAATGAATGGTGAAGAAACTGGACTTGGATTTGCAACTCGTGATTAAGGAGCG
AAGGTTGAAGAAGATTAGGGTCTTTTAGATTTTGACATTTTGACTAATGATGGTACTCAT
AGAAACATGAAACTGCTTATAGATTTAAAGAATATTTTCTCTCGTTAGTTGCCAAAAATG
CCTAAAGAATATATTGTTAAATTAGTATTTGATAGACATCATGAATCGATGGTGATATTA
AAGAATAAATAAAAAGTTATTGGTGGTATCTGCTTTCGTTAATATAAGCCTTAAAGATTT
GCAGAAGTAGCTTTCCTTGCTGTCACTGCAAATGAATAGGTTAGAGGGTATGGCACAAGA
TTGATGAATAAATTTAAAGATCATATGTAAAAATAGAATATTGAATATCTTCTCACTTAT
GCTGATAACTTTGCTATTGGATACTTTAAGAAATAAGGTTTTACAAAAGAACATAGAATG
CCATAAGAAAAATGGAAGGGATATATTAAAGATTATGATGGCGGTACTCTTATGGAGTGC
TACATTCACCCATATGTTGATTACGGAAATATATCTCAGATCATCAAAAGATAAAAAGAG
CTTTTGATAGAAAGAATCAAGAAATTATCATTAAATGAAAAAGTATTCTCTGGTAAAGAG
TATGCTGCATTAATATAAAATTCTATGGATAATGAGGATCCTGAAAACCCTAAAGTGAAT
CCTTCAGATATTCCTGGAGTTGCATTTAGTGGTTGGGAGTGGAAAGACTACCATGAACTC
AAGAAATCAAAAGAGAGATCATTCAATCTTTAGTGTGCTAATGTTATTGAAAATATGAAG
AGACACAAACAATCTTGGCCCTTCTTAGATCCTGTTAATAAAGATGATGTTCCAGATTAT
TATGATGTGATTACTGATCCTATAGATATTAAAGCAATAGAAAAGAAGTTATAAAATAAT
CAATATGTTGACAAAGACTAATTTATCAAAGACGTCAAAAGAATTTTTACTAATGCTAAA
ATTTATAACTAGCCCGATACTATATATTATAAAGCTGCTAAAGAATTAGAAGATTTTGTT
GAACCTTATCTTACTAAACTTAAAGATACTAAAGAAAGTAATACTCCATCTAATAATAAT
TCTGCACATGGAAGTAAGAAACCACTTCCTGTTAGAAAAAGTATAAAAAAGAAATGA


>TTHERM_00248390(gene)
ATGGGTAATTAAGATTATTTATTTTGCAGAATTCATTTTACGTCTTTTTTGTTAATTAAA
ATAGCTGATTAAGAAAAATCTGCTTAAGATGCATAGAATGCAGCACCATAAGAGACTGCA
TTTGTAGGAATGAATGGTGAAGTAAAAATTCAAATTTAAGTTTTTATTAAGTTTATTCAG
AAATAAAACCTACTGAATTTAATAATAGGAAACTGGACTTGGATTTGCAACTCGTGATTA
AGGAGCGAAGGTTGAAGAAGATTAGGGTCTTTTAGATTTTGACATTTTGACTAATGATGG
GTAAATAAAATTAATTATAAATTATTCAACTAACAAGAATGAATTTTAAAAGCTCAAAAT
ACAAATTTTAATAATCATATTAATTTCAAAAGTACTCATAGAAACATGAAACTGCTTATA
GATTTAAAGAATATTTTCTCTCGTTAGTTGCCAAAAATGCCTAAAGAATATATTGTTAAA
TTAGTATTTGATAGACATCATGAATCGATGGTGATATTAAAGAATAAATAAAAAGTTATT
GGTGGTATCTGCTTTCGTTAATATAAGCCTTAAAGATTTGCAGAAGTAGCTTTCCTTGCT
GTCACTGCAAATGAATAGGTTAGAGGGTATGGCACAAGATTGATGAATAAATTTAAAGAT
CATATGTAAAAATAGAATATTGAATATCTTCTCACTTATGCTGATAACTTTGCTATTGGA
TACTTTAAGAAATAAGGTTTTACAAAAGAACATAGAATGCCATAAGAAAAATGGAAGGGA
TATATTAAAGATTATGATGGCGGTACTCTTATGGAGTGCTACATTCACCCATATGTTGAT
TACGGAAATATATCTCAGATCATCAAAAGATAAAAAGAGGTATTCTTAATATTATCTTTT
AAAATCTTATTAATTGTTCAAAATAATGACACAAGCATGATAAATTAATTTACTAAATCA
ACAACAAAACAAATGAATAATTTGAATAGTTTAATAAATTAAATTGGCTATTTATTTTTT
GCAAATAAGGAAATTCTGAAAGCATATAATATTTTATTTCAGTCAAAAAAAGATGTTATG
CAATCAATATTTCAATTAAAATTGTAAAAGATAAACTAAATATTATAATAAAGCGGTTTA
ACAAATTTCTTTGGAAAGAAAATAATTCAAATAATATTAAAAAGCCAAAAAAATAATTCA
AACTAAAGATAATTTATGCAAAAATAATGAATGATTTAGCAATATTTTAGTTAATTTTTA
TTGAAATTTATTTTAGAGAAAATTAATTTATAATAAATTTATTAATTATTTTTTATTTGA
AATGTTAGCTTTTGATAGAAAGAATCAAGAAATTATCATTAAATGAAAAAGTATTCTCTG
GTAAAGAGTATGCTGCATTAATATAAAATTCTATGGATAATGAGGATCCTGAAAACCCTA
AAGTGAATCCTTCAGATATTCCTGGAGTTGGTATAGATATTAGAAGAATAATATTCATTT
AATTTATTAATTTTTAAATAAATTTGATAGCATTTAGTGGTTGGGAGTGGAAAGACTACC
ATGAACTCAAGAAATCAAAAGAGAGATCATTCAATCTTTAGTGTGCTAATGTTATTGAAA
ATATGAAGAGACACAAACAATCTTGGCCCTTCTTAGATCCTGTTAATAAAGATGATGTTC
CAGATTATTATGATGTGATTACTGATCCTATAGGTATTTTAAATAAAATAAATTGATAAA
GCAAGTTTTTTTAACATTATATTTATAAAAAAGATATTAAAGCAATAGAAAAGAAGTTAT
AAAATAATCAATATGTTGACAAAGACTAATTTATCAAAGACGTCAAAAGAATTTTTACTA
ATGCTAAAATTTATAACTAGCCCGATACTATATATTATAAAGCTGCTAAAGAATTAGAAG
ATTTTGTTGAACCTTATCTTACTAAACTTAAAGATACTAAAGAAAGTAATACTCCATCTA
ATAATAATTCTGCACATGGAAGTAAGAAACCACTTCCTGTTAGAAAAAGTATAAAAAAGA
AATGA