[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND CHARACTERIZATION.
TISSUE=Testis;
PubMed=8552087 [NCBI, ExPASy, EBI, Israel, Japan]
Candau R.,
Moore P.A.,
Wang L.,
Barlev N.,
Ying C.Y.,
Rosen C.A.,
Berger S.L.;
"Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5.";
Mol. Cell. Biol. 16:593-602(1996).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Liver;
DOI=10.1093/nar/26.12.2948; PubMed=9611240 [NCBI, ExPASy, EBI, Israel, Japan]
Smith E.R.,
Belote J.M.,
Schlitz R.L.,
Yang X.-J.,
Moore P.A.,
Berger S.L.,
Nakatani Y.,
Allis C.D.;
"Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members.";
Nucleic Acids Res. 26:2948-2954(1998).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J.,
Istrail S.,
Sutton G.G.,
Florea L.,
Halpern A.L.,
Mobarry C.M.,
Lippert R.,
Walenz B.,
Shatkay H.,
Dew I.,
Miller J.R.,
Flanigan M.J.,
Edwards N.J.,
Bolanos R.,
Fasulo D.,
Halldorsson B.V.,
Hannenhalli S.,
Turner R.,
Yooseph S., ![]()
Lu F.,
Nusskern D.R.,
Shue B.C.,
Zheng X.H.,
Zhong F.,
Delcher A.L.,
Huson D.H.,
Kravitz S.A.,
Mouchard L.,
Reinert K.,
Remington K.A.,
Clark A.G.,
Waterman M.S.,
Eichler E.E.,
Adams M.D.,
Hunkapiller M.W.,
Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, Skin, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[5]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-837 (ISOFORM 1).
TISSUE=Brain;
DOI=10.1038/382319a0; PubMed=8684459 [NCBI, ExPASy, EBI, Israel, Japan]
Yang X.-J.,
Ogryzko V.V.,
Nishikawa J.,
Howard B.H.,
Nakatani Y.;
"A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A.";
Nature 382:319-324(1996).
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[6]
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MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10; TAF12 AND TAF9.
DOI=10.1128/MCB.21.20.6782-6795.2001; PubMed=11564863 [NCBI, ExPASy, EBI, Israel, Japan]
Martinez E.,
Palhan V.B.,
Tjernberg A.,
Lymar E.S.,
Gamper A.M.,
Kundu T.K.,
Chait B.T.,
Roeder R.G.;
"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. 21:6782-6795(2001).
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[7]
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IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; TAF2; TAF4; TAF5; TRRAP AND TAF10.
DOI=10.1074/jbc.274.26.18285; PubMed=10373431 [NCBI, ExPASy, EBI, Israel, Japan]
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. 274:18285-18289(1999).
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[8]
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INTERACTION WITH TRRAP.
DOI=10.1128/MCB.20.2.556-562.2000; PubMed=10611234 [NCBI, ExPASy, EBI, Israel, Japan]
McMahon S.B.,
Wood M.A.,
Cole M.D.;
"The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc.";
Mol. Cell. Biol. 20:556-562(2000).
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[9]
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INTERACTION WITH HIV-1 TAT.
DOI=10.1074/jbc.M101385200; PubMed=11384967 [NCBI, ExPASy, EBI, Israel, Japan]
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. 276:28179-28184(2001).
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[10]
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INTERACTION WITH TAF3.
DOI=10.1128/MCB.21.15.5109-5121.2001; PubMed=11438666 [NCBI, ExPASy, EBI, Israel, Japan]
Gangloff Y.G.,
Pointud J.-C.,
Thuault S.,
Carre L.,
Romier C.,
Muratoglu S.,
Brand M.,
Tora L.,
Couderc J.-L.,
Davidson I.;
"The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger.";
Mol. Cell. Biol. 21:5109-5121(2001).
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[11]
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INTERACTION WITH TACC1; TACC2 AND TACC3.
DOI=10.1038/sj.onc.1207424; PubMed=14767476 [NCBI, ExPASy, EBI, Israel, Japan]
Gangisetty O.,
Lauffart B.,
Sondarva G.V.,
Chelsea D.M.,
Still I.H.;
"The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases.";
Oncogene 23:2559-2563(2004).
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[12]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-734, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J.,
Moritz A.,
Lee K.A.,
Guo A.,
Goss V.L.,
Spek E.J.,
Zhang H.,
Zha X.-M.,
Polakiewicz R.D.,
Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
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[13]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-734, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K.,
Guo A.,
Zeng Q.,
Possemato A.,
Yu J.,
Haack H.,
Nardone J.,
Lee K.,
Reeves C.,
Li Y.,
Hu Y.,
Tan Z.,
Stokes M.,
Sullivan L.,
Mitchell J.,
Wetzel R.,
Macneill J.,
Ren J.M.,
Yuan J., ![]()
Bakalarski C.E.,
Villen J.,
Kornhauser J.M.,
Smith B.,
Li D.,
Zhou X.,
Gygi S.P.,
Gu T.-L.,
Polakiewicz R.D.,
Rush J.,
Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
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[14]
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IDENTIFICATION IN STAGA COMPLEX.
DOI=10.1016/j.molcel.2007.12.011; PubMed=18206972 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao Y.,
Lang G.,
Ito S.,
Bonnet J.,
Metzger E.,
Sawatsubashi S.,
Suzuki E.,
Le Guezennec X.,
Stunnenberg H.G.,
Krasnov A.,
Georgieva S.G.,
Schuele 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 29:92-101(2008).
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[15]
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STRUCTURE BY NMR OF 730-832.
DOI=10.1006/jmbi.2000.4207; PubMed=11090279 [NCBI, ExPASy, EBI, Israel, Japan]
Hudson B.P.,
Martinez-Yamout M.A.,
Dyson H.J.,
Wright P.E.;
"Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain.";
J. Mol. Biol. 304:355-370(2000).
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- 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. 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.
- CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
- SUBUNIT: Interacts with EP300, CREBBP and ADA2. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TAF3, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5, TAF10 and TRRAP. Interacts with TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated with a subcomplex required for histone deubiquitinylation composed of ATXN7L3, ENY2 and USP22. Interacts with and acetylates HIV-1 Tat.
- INTERACTION:
Q8IXJ6:SIRT2; NbExp=1; IntAct=EBI-477636, EBI-477232;
Q8IXJ6:SIRT2; NbExp=1; IntAct=EBI-477641, EBI-477232;
- SUBCELLULAR LOCATION: Nucleus.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
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| Name | 2 |
| Synonyms | GCN5-S |
| Isoform ID | Q92830-2 |
| Features which should be applied to build the isoform sequence: VSP_000556. |
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- TISSUE SPECIFICITY: Expressed in all tissues tested, with most abundant expression in ovary.
- SIMILARITY: Belongs to the GCN5 family.
- SIMILARITY: Contains 1 bromo domain.
- SIMILARITY: Contains 1 N-acetyltransferase domain.
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