KAT2A

Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene.[5][6]

KAT2A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1F68, 1Z4R, 3D7C, 5H86, 5H84
Identifiers
Aliases	KAT2A, GCN5, GCN5L2, PCAF-b, hGCN5, lysine acetyltransferase 2A
External IDs	OMIM: 602301 MGI: 1343101 HomoloGene: 41343 GeneCards: KAT2A
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q21.2 Start 42,113,111 bp[1] End 42,121,367 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 D|11 63.53 cM Start 100,704,746 bp[2] End 100,712,465 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • GO:0001105 transcription coactivator activity • N-acetyltransferase activity • transcription factor binding • histone deacetylase binding • chromatin binding • H3 histone acetyltransferase activity • GO:0001948 protein binding • acetyltransferase activity • histone acetyltransferase activity (H4-K12 specific) • protein phosphatase binding • transferase activity, transferring acyl groups • histone acetyltransferase activity • thiol-dependent ubiquitinyl hydrolase activity • peptide-lysine-N-acetyltransferase activity • histone succinyltransferase activity Cellular component • Ada2/Gcn5/Ada3 transcription activator complex • transcription factor TFTC complex • STAGA complex • nucleoplasm • nuclear chromatin • histone acetyltransferase complex • mitotic spindle • extracellular • cell nucleus • chromosome • cytoplasm • centrosome • microtubule organizing center • cytoskeleton • oxoglutarate dehydrogenase complex Biological process • positive regulation of transcription regulatory region DNA binding • somitogenesis • positive regulation of gene expression, epigenetic • chromatin remodeling • metencephalon development • cellular response to nerve growth factor stimulus • regulation of transcription, DNA-templated • regulation of protein stability • response to organic cyclic compound • multicellular organism growth • positive regulation of protein targeting to mitochondrion • regulation of transcription from RNA polymerase II promoter • cardiac muscle cell differentiation • cellular response to tumor necrosis factor • histone H3-K14 acetylation • positive regulation of cell projection organization • in utero embryonic development • transcription from RNA polymerase II promoter • transcription, DNA-templated • nervous system development • positive regulation of histone acetylation • histone deubiquitination • telencephalon development • neural tube closure • response to nutrient levels • regulation of autophagy of mitochondrion • histone acetylation • histone H3 acetylation • cellular proliferation • GO:0022415 viral process • intracellular distribution of mitochondria • histone H4-K12 acetylation • alpha-tubulin acetylation • midbrain development • protein deubiquitination • cytokine production • heart development • long-term memory • internal peptidyl-lysine acetylation • regulation of regulatory T cell differentiation • positive regulation of transcription from RNA polymerase II promoter • negative regulation of centriole replication • regulation of synaptic plasticity • regulation of T cell activation • limb development • histone succinylation • positive regulation of cardiac muscle cell differentiation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2648	14534
Ensembl	ENSG00000108773	ENSMUSG00000020918
UniProt	Q92830	Q9JHD2
RefSeq (mRNA)	NM_021078 NM_001376227	NM_001038010 NM_020004
RefSeq (protein)	NP_066564 NP_001363156	NP_001033099 NP_064388
Location (UCSC)	Chr 17: 42.11 – 42.12 Mb	Chr 11: 100.7 – 100.71 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

GCN5L2 has been shown to interact with:

• DDB1,[7]
• Ku70,[8]
• Ku80,[8]
• TADA2L,[8][9]
• TAF9,[7] and
• Transcription initiation protein SPT3 homolog.[7][10]

References

1. GRCh38: Ensembl release 89: ENSG00000108773 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020918 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Candau R, Moore PA, Wang L, Barlev N, Ying CY, Rosen CA, Berger SL (February 1996). "Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5". Mol Cell Biol. 16 (2): 593–602. doi:10.1128/mcb.16.2.593. PMC 231038. PMID 8552087.
6. "Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)".
7. Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (October 2001). "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. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856. PMID 11564863.
8. Barlev NA, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman JL, Berger SL (March 1998). "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. doi:10.1128/mcb.18.3.1349. PMC 108848. PMID 9488450.
9. Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL (January 1997). "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. doi:10.1128/mcb.17.1.519. PMC 231776. PMID 8972232.
10. Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (June 2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC 150203. PMID 11406595.

Further reading

• Berry R, Stevens TJ, Walter NA, Wilcox AS, Rubano T, Hopkins JA, Weber J, Goold R, Soares MB, Sikela JM (1995). "Gene-based sequence-tagged-sites (STSs) as the basis for a human gene map". Nat. Genet. 10 (4): 415–23. doi:10.1038/ng0895-415. PMID 7670491.
• Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y (1996). "A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A". Nature. 382 (6589): 319–24. doi:10.1038/382319a0. PMID 8684459.
• Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL (1997). "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. doi:10.1128/mcb.17.1.519. PMC 231776. PMID 8972232.
• Carter KC, Wang L, Shell BK, Zamir I, Berger SL, Moore PA (1997). "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. doi:10.1006/geno.1996.4605. PMID 9073520.
• Barlev NA, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman JL, Berger SL (1998). "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. doi:10.1128/mcb.18.3.1349. PMC 108848. PMID 9488450.
• Smith ER, Belote JM, Schiltz RL, Yang XJ, Moore PA, Berger SL, Nakatani Y, Allis CD (1998). "Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members". Nucleic Acids Res. 26 (12): 2948–54. doi:10.1093/nar/26.12.2948. PMC 147644. PMID 9611240.
• Randhawa GS, Bell DW, Testa JR, Feinberg AP (1998). "Identification and mapping of human histone acetylation modifier gene homologues". Genomics. 51 (2): 262–9. doi:10.1006/geno.1998.5370. PMID 9722949.
• Xu W, Edmondson DG, Roth SY (1998). "Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates". Mol. Cell. Biol. 18 (10): 5659–69. doi:10.1128/MCB.18.10.5659. PMC 109152. PMID 9742083.
• Brand M, Yamamoto K, Staub A, Tora L (1999). "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. doi:10.1074/jbc.274.26.18285. PMID 10373431.
• McMahon SB, Wood MA, Cole MD (2000). "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc". Mol. Cell. Biol. 20 (2): 556–62. doi:10.1128/MCB.20.2.556-562.2000. PMC 85131. PMID 10611234.
• Kurooka H, Honjo T (2000). "Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5". J. Biol. Chem. 275 (22): 17211–20. doi:10.1074/jbc.M000909200. PMID 10747963.
• Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE (2000). "Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain". J. Mol. Biol. 304 (3): 355–70. doi:10.1006/jmbi.2000.4207. PMID 11090279.
• Col E, Caron C, Seigneurin-Berny D, Gracia J, Favier A, Khochbin S (2001). "The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat". J. Biol. Chem. 276 (30): 28179–84. doi:10.1074/jbc.M101385200. PMID 11384967.
• Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC 150203. PMID 11406595.
• Gangloff YG, Pointud JC, Thuault S, Carré L, Romier C, Muratoglu S, Brand M, Tora L, Couderc JL, Davidson I (2001). "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. doi:10.1128/MCB.21.15.5109-5121.2001. PMC 87236. PMID 11438666.
• Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (2001). "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. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856. PMID 11564863.
• Yanagisawa J, Kitagawa H, Yanagida M, Wada O, Ogawa S, Nakagomi M, Oishi H, Yamamoto Y, Nagasawa H, McMahon SB, Cole MD, Tora L, Takahashi N, Kato S (2002). "Nuclear receptor function requires a TFTC-type histone acetyl transferase complex". Mol. Cell. 9 (3): 553–62. doi:10.1016/S1097-2765(02)00478-1. PMID 11931763.
• Brès V, Kiernan R, Emiliani S, Benkirane M (2002). "Tat acetyl-acceptor lysines are important for human immunodeficiency virus type-1 replication". J. Biol. Chem. 277 (25): 22215–21. doi:10.1074/jbc.M201895200. PMID 11956210.
• Col E, Gilquin B, Caron C, Khochbin S (2002). "Tat-controlled protein acetylation". J. Biol. Chem. 277 (40): 37955–60. doi:10.1074/jbc.M206694200. PMID 12154097.

External links

• FactorBook GCN5