GCN5L2

K(lysine) acetyltransferase 2A

PDB rendering based on 1f68.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols KAT2A ; GCN5; GCN5L2; PCAF-b; hGCN5
External IDs OMIM: 602301 MGI: 1343101 HomoloGene: 41343 ChEMBL: 5501 GeneCards: KAT2A Gene
EC number 2.3.1.48
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 2648 14534
Ensembl ENSG00000108773 ENSMUSG00000020918
UniProt Q92830 Q9JHD2
RefSeq (mRNA) NM_021078 NM_001038010
RefSeq (protein) NP_066564 NP_001033099
Location (UCSC) Chr 17:
42.11 – 42.12 Mb
Chr 11:
100.7 – 100.71 Mb
PubMed search

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:

References

  1. 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.
  2. "Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)".
  3. 1 2 3 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.
  4. 1 2 3 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.
  5. 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.
  6. 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

External links


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