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Protein GCN5L2 PDB 1f68.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases KAT2A, GCN5, GCN5L2, PCAF-b, hGCN5, lysine acetyltransferase 2A
External IDs MGI: 1343101 HomoloGene: 41343 GeneCards: KAT2A
RNA expression pattern
PBB GE GCN5L2 202182 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 17: 42.11 – 42.12 Mb Chr 11: 100.7 – 100.71 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene.[3][4]


GCN5L2 has been shown to interact with:


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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 231038Freely accessible. PMID 8552087. 
  4. ^ "Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)". 
  5. ^ a b c 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 99856Freely accessible. PMID 11564863. 
  6. ^ a b c 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 108848Freely accessible. PMID 9488450. 
  7. ^ 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 231776Freely accessible. PMID 8972232. 
  8. ^ 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 150203Freely accessible. PMID 11406595. 

Further reading[edit]

External links[edit]