EMSY was originally reported as a transcriptional repressor and breast cancer-associated protein that interacts with the BRCA2 protein []. It contains an N-terminal ENT domain which can bind BRCA2. It is involved in DNA damage repair, genomic instability, and chromatin remodeling []. EMSY can function as an integral component of an NIF-1 complex and play an important role in the regulation of nuclear receptor-mediated transcription []. It is also part of the EMSY/KDM5A/SIN3B complex that may function as a transcriptional repressor [].
This entry represents the EMSY-like proteins from plants. They contain an EMSY N-terminal (ENT) domain, a central Agenet domain, and a putative C-terminal coiled-coil structure. Arabidopsis EMSY-like proteins contribute to RPP7-mediated and basal immunity, especially against Hyaloperonospora arabidopsidis isolate Hiks1 [].
This entry represents an agenet domain found in EMSY-like (AtEML) proteins, which have possible roles in chromatin regulation and are related to the BRCA2-interacting human oncoprotein EMSY []. Proteins containing this domain also include MRG2 (AT1G02740) from Arabidopsis and PHD finger protein 20-like protein 1 (PHF20L1) from animals. MRG2 binds to the FLOWERING LOCUS T locus and elevates the expression in an H3K36me3-dependent manner []. The function of PHF20L1 is not clear.
The EMSY N-terminal (ENT) domain is a ~90-residue module, which is unique in the human proteome, although multiple copies are found in Arabidopsis proteins. In the plant proteins, the ENT domains are accompanied by Agenet domains, plant specific homologues of Tudor domains [, ].The ENT domain consists of a unique arrangement of five α-helices that fold into a helical bundle arrangement. Overall, the three-dimensional structure adopts a club-like shape that consists of an extended N-terminal α-helix that connects to a helical bundle substructure. The ENT domain forms a homodimer via the anti-parallel packing of the long N-terminal α-helix from each subunit [, ].
The EMSY N-terminal (ENT) domain is a ~90-residue module, which is unique in the human proteome, although multiple copies are found in Arabidopsis proteins. In the plant proteins, the ENT domains are accompanied by Agenet domains, plant specific homologues of Tudor domains [, ].The ENT domain consists of a unique arrangement of five α-helices that fold into a helical bundle arrangement. Overall, the three-dimensional structure adopts a club-like shape that consists of an extended N-terminal α-helix that connects to a helical bundle substructure. The ENT domain forms a homodimer via the anti-parallel packing of the long N-terminal α-helix from each subunit [, ].
