Biology:KAT2A
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Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene.[1][2]
Interactions
GCN5L2 has been shown to interact with:
- DDB1,[3]
- Ku70,[4]
- Ku80,[4]
- TADA2L,[4][5]
- TAF9,[3] and
- Transcription initiation protein SPT3 homolog.[3][6]
References
- ↑ "Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5". Mol Cell Biol 16 (2): 593–602. February 1996. doi:10.1128/mcb.16.2.593. PMID 8552087.
- ↑ "Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2648.
- ↑ 3.0 3.1 3.2 "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 (20): 6782–95. October 2001. doi:10.1128/MCB.21.20.6782-6795.2001. PMID 11564863.
- ↑ 4.0 4.1 4.2 "Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex". Mol. Cell. Biol. 18 (3): 1349–58. March 1998. doi:10.1128/mcb.18.3.1349. PMID 9488450.
- ↑ "Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation". Mol. Cell. Biol. 17 (1): 519–27. January 1997. doi:10.1128/mcb.17.1.519. PMID 8972232.
- ↑ "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): 3187–96. June 2001. doi:10.1093/emboj/20.12.3187. PMID 11406595.
Further reading
- "Gene-based sequence-tagged-sites (STSs) as the basis for a human gene map.". Nat. Genet. 10 (4): 415–23. 1995. doi:10.1038/ng0895-415. PMID 7670491.
- "A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A.". Nature 382 (6589): 319–24. 1996. doi:10.1038/382319a0. PMID 8684459. Bibcode: 1996Natur.382..319Y.
- "Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation.". Mol. Cell. Biol. 17 (1): 519–27. 1997. doi:10.1128/mcb.17.1.519. PMID 8972232.
- "The human transcriptional adaptor genes TADA2L and GCN5L2 colocalize to chromosome 17q12-q21 and display a similar tissue expression pattern.". Genomics 40 (3): 497–500. 1997. doi:10.1006/geno.1996.4605. PMID 9073520.
- "Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex.". Mol. Cell. Biol. 18 (3): 1349–58. 1998. doi:10.1128/mcb.18.3.1349. PMID 9488450.
- "Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members.". Nucleic Acids Res. 26 (12): 2948–54. 1998. doi:10.1093/nar/26.12.2948. PMID 9611240.
- "Identification and mapping of human histone acetylation modifier gene homologues.". Genomics 51 (2): 262–9. 1998. doi:10.1006/geno.1998.5370. PMID 9722949.
- "Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates.". Mol. Cell. Biol. 18 (10): 5659–69. 1998. doi:10.1128/MCB.18.10.5659. PMID 9742083.
- "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction.". J. Biol. Chem. 274 (26): 18285–9. 1999. doi:10.1074/jbc.274.26.18285. PMID 10373431.
- "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc.". Mol. Cell. Biol. 20 (2): 556–62. 2000. doi:10.1128/MCB.20.2.556-562.2000. PMID 10611234.
- "Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5.". J. Biol. Chem. 275 (22): 17211–20. 2000. doi:10.1074/jbc.M000909200. PMID 10747963.
- "Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain.". J. Mol. Biol. 304 (3): 355–70. 2000. doi:10.1006/jmbi.2000.4207. PMID 11090279.
- "The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat.". J. Biol. Chem. 276 (30): 28179–84. 2001. doi:10.1074/jbc.M101385200. PMID 11384967.
- "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation.". EMBO J. 20 (12): 3187–96. 2001. doi:10.1093/emboj/20.12.3187. PMID 11406595.
- "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. 21 (15): 5109–21. 2001. doi:10.1128/MCB.21.15.5109-5121.2001. PMID 11438666.
- "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 (20): 6782–95. 2001. doi:10.1128/MCB.21.20.6782-6795.2001. PMID 11564863.
- "Nuclear receptor function requires a TFTC-type histone acetyl transferase complex.". Mol. Cell 9 (3): 553–62. 2002. doi:10.1016/S1097-2765(02)00478-1. PMID 11931763.
- "Tat acetyl-acceptor lysines are important for human immunodeficiency virus type-1 replication.". J. Biol. Chem. 277 (25): 22215–21. 2002. doi:10.1074/jbc.M201895200. PMID 11956210.
- "Tat-controlled protein acetylation.". J. Biol. Chem. 277 (40): 37955–60. 2002. doi:10.1074/jbc.M206694200. PMID 12154097.
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