PROSITE documentation PDOC51037YEATS domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC51037
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:
- Yeast YNL107w or YAF9 (yeast AF-9) protein, a nonessential NuA4 histone acetyltransferase (HAT) subunit that also associates with the SWR1 complex, which deposits the histone H2A variant Htz1.
- Yeast something about silencing protein 5 (SAS5), a subunit of the SAS HAT complex.
- Yeast transcription initiation factor TFIID subunit 14 (TAF14), a component of the NuA3 (SAS3) HAT complex which is also associated with the SWI/SNF ATPase remodeling complex and the TFIIF and TFIID RNA polymerase II transcription complexes.
- Human Glioma-amplified sequence-41 (Gas41), a member of the TIP60 complex, which might be the human counterpart of the yeast NuA4 complex.
- Human AF-9 protein.
- Human ENL protein.
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). | |
| PubMed ID | 15485911 | |
| DOI | 10.1128/MCB.24.21.9424-9436.2004 |
| 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). | |
| PubMed ID | 28300602 | |
| DOI | 10.1016/j.jmb.2017.03.010 |
| 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. | |
| Source | Structure 24:1606-1612(2016). | |
| PubMed ID | 27545619 | |
| DOI | 10.1016/j.str.2016.05.023 |
| 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). | |
| PubMed ID | 29463709 | |
| DOI | 10.1073/pnas.1717664115 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.