|PROSITE documentation PDOC51037 [for PROSITE entry PS51037]|
The YEATS (Yaf9, ENL, AF9, Taf14, and Sas5) domain is an evolutionarily conserved module present from yeast to human. The YEATS domain proteins are found in major chromatin-remodeling and histone acetyltransferase (HAT) complexes and implicated in the regulation of chromatin structure, histone acetylation and deposition, gene transcription, and DNA damage response. The YEATS domain is a reader module that selectively recognizes histone lysine acylation, including acetylation, propionylation, butyrylation, crotonylation, 2-hydroxyisobutyrylation, and succinylation [1,2,3,4,5].
The YEATS domain consists of a conserved immunoglobin fold made of a two-layer β sandwich with eight antiparallel β-strands(see <PDB:2NDG>). While two α helices cap the β sandwich at one end, the acyl-lysine is bound into a surface-exposed cavity formed by inter-β strand loops of L1 and L4. The YEATS domain adopts the same pocket for different acyl-lysine readout with acyl-lysine side chain snugly sandwiched by a set of aromatic residues [4,5].
Some proteins known to contain a YEATS domain are listed below:
The profile we developed covers the entire YEATS domain.Last update:
August 2020 / Profile and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Le Masson I. Yu D.Y. Jensen K. Chevalier A. Courbeyrette R. Boulard Y. Smith M.M. Mann C.|
|Source||Mol. Cell. Biol. 23:6086-6102(2003).|
|2||Authors||Zhang H. Richardson D.O. Roberts D.N. Utley R. Erdjument-Bromage H. Tempst P. Cote J. Cairns B.R.|
|Title||The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres.|
|Source||Mol. Cell. Biol. 24:9424-9436(2004).|
|3||Authors||Zhao D. Li Y. Xiong X. Chen Z. Li H.|
|Title||YEATS Domain-A Histone Acylation Reader in Health and Disease.|
|Source||J. Mol. Biol. 429:1994-2002(2017).|
|4||Authors||Zhang Q. Zeng L. Zhao C. Ju Y. Konuma T. Zhou M.-M.|
|Title||Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain.|
|5||Authors||Wang Y. Jin J. Chung M.W.H. Feng L. Sun H. Hao Q.|
|Title||Identification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation.|
|Source||Proc. Natl. Acad. Sci. U. S. A. 115:2365-2370(2018).|