{PDOC51037}
{PS51037; YEATS}
{BEGIN}
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* YEATS domain profile *
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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
beta sandwich  with eight antiparallel beta-strands(see <PDB:2NDG>). While two
alpha helices  cap the beta sandwich at one end, the acyl-lysine is bound into
a surface-exposed  cavity  formed by inter-beta 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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2020 / Profile and text revised.

[ 1] Le Masson I., Yu D.Y., Jensen K., Chevalier A., Courbeyrette R.,
     Boulard Y., Smith M.M., Mann C.
     Mol. Cell. Biol. 23:6086-6102(2003).
[ 2] Zhang H., Richardson D.O., Roberts D.N., Utley R.,
     Erdjument-Bromage H., Tempst P., Cote J., Cairns B.R.
     "The Yaf9 component of the SWR1 and NuA4 complexes is required for
     proper gene expression, histone H4 acetylation, and Htz1 replacement
     near telomeres."
     Mol. Cell. Biol. 24:9424-9436(2004).
     PubMed=15485911; DOI=10.1128/MCB.24.21.9424-9436.2004
[ 3] Zhao D., Li Y., Xiong X., Chen Z., Li H.
     "YEATS Domain-A Histone Acylation Reader in Health and Disease."
     J. Mol. Biol. 429:1994-2002(2017).
     PubMed=28300602; DOI=10.1016/j.jmb.2017.03.010
[ 4] Zhang Q., Zeng L., Zhao C., Ju Y., Konuma T., Zhou M.-M.
     "Structural Insights into Histone Crotonyl-Lysine Recognition by the
     AF9 YEATS Domain."
     Structure 24:1606-1612(2016).
     PubMed=27545619; DOI=10.1016/j.str.2016.05.023
[ 5] Wang Y., Jin J., Chung M.W.H., Feng L., Sun H., Hao Q.
     "Identification of the YEATS domain of GAS41 as a pH-dependent reader
     of histone succinylation."
     Proc. Natl. Acad. Sci. U. S. A. 115:2365-2370(2018).
     PubMed=29463709; DOI=10.1073/pnas.1717664115

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