YEATS domain

In molecular biology, the YEATS domain is a protein domain found in a variety of proteins from eukaryotic organisms.[1] YEATS domain proteins are found in a variety of chromatin modification molecular complexes. Structurally the domain has an immunoglobulin like fold.[2] The YEATS domain has shown to bind to acetyllysine protein modifications.[3] In addition to lysine acetylation, the YEATS domain has shown to be a reader domain for various lysine acylations, with highest affinity for lysine crotonylation.[4] [5]

YEATS domain
Identifiers
SymbolYEATS
PfamPF03366
InterProIPR005033
PROSITEPS51037
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB4tmp​, 3fk3​, 3rls​, 2l7e​, 3qrl​

See also

Bromodomain

References
  1. Schulze JM, Wang AY, Kobor MS (2009). "YEATS domain proteins: a diverse family with many links to chromatin modification and transcription". Biochem. Cell Biol. 87 (1): 65–75. doi:10.1139/O08-111. PMID 19234524.
  2. Wang AY, Schulze JM, Skordalakes E, Gin JW, Berger JM, Rine J, Kobor MS (2009). "Asf1-like structure of the conserved Yaf9 YEATS domain and role in H2A.Z deposition and acetylation". Proc. Natl. Acad. Sci. U.S.A. 106 (51): 21573–8. doi:10.1073/pnas.0906539106. PMC 2799888. PMID 19966225.
  3. Li Y, Wen H, Xi Y, Tanaka K, Wang H, Peng D, Ren Y, Jin Q, Dent SY, Li W, Li H, Shi X (2014). "AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation". Cell. 159 (3): 558–71. doi:10.1016/j.cell.2014.09.049. PMC 4344132. PMID 25417107.
  4. Li Y, Sabari BR, Panchenko T, Wen H, Zhao D, Guan H, Wan L, Huang H, Tang Z, Zhao Y, Roeder RG, Shi X, Allis CD, Li H (2016). "Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain". Molecular Cell. 62 (2): 181–193. doi:10.1016/j.molcel.2016.03.028. PMC 4841940. PMID 27105114.
  5. Andrews FH, Shinsky SA, Shanle EK, Bridgers JB, Gest A, Tsun IK, Krajewski K, Shi X, Strahl BD, Kutateladze TG (2016). "The Taf14 YEATS domain is a reader of histone crotonylation". Nat. Chem. Biol. 12 (6): 396–8. doi:10.1038/nchembio.2065. PMC 4871749. PMID 27089029.
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