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PROSITE documentation PDOC51037 [for PROSITE entry PS51037]

YEATS domain profile





Description

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.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

YEATS, PS51037; YEATS domain profile  (MATRIX)


References

1AuthorsLe Masson I. Yu D.Y. Jensen K. Chevalier A. Courbeyrette R. Boulard Y. Smith M.M. Mann C.
SourceMol. Cell. Biol. 23:6086-6102(2003).

2AuthorsZhang H. Richardson D.O. Roberts D.N. Utley R. Erdjument-Bromage H. Tempst P. Cote J. Cairns B.R.
TitleThe Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres.
SourceMol. Cell. Biol. 24:9424-9436(2004).
PubMed ID15485911
DOI10.1128/MCB.24.21.9424-9436.2004

3AuthorsZhao D. Li Y. Xiong X. Chen Z. Li H.
TitleYEATS Domain-A Histone Acylation Reader in Health and Disease.
SourceJ. Mol. Biol. 429:1994-2002(2017).
PubMed ID28300602
DOI10.1016/j.jmb.2017.03.010

4AuthorsZhang Q. Zeng L. Zhao C. Ju Y. Konuma T. Zhou M.-M.
TitleStructural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain.
SourceStructure 24:1606-1612(2016).
PubMed ID27545619
DOI10.1016/j.str.2016.05.023

5AuthorsWang Y. Jin J. Chung M.W.H. Feng L. Sun H. Hao Q.
TitleIdentification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation.
SourceProc. Natl. Acad. Sci. U. S. A. 115:2365-2370(2018).
PubMed ID29463709
DOI10.1073/pnas.1717664115



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