PROSITE documentation PDOC52052

PEHE domain profile

The PEHE domain, named after four highly conserved characteristic amino acid residues (P, E, H, E) is found in subunits of two protein complexes, MSL and NSL, involved in histone acetylation in both vertebrates and invertebrates [1,2]:

• Animal Male-specific lethal 1 (MSL1), a non-catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction.
• Vertebrate KAT8 regulatory NSL complex subunit 1 (KANSL1), a non-catalytic component of the NSL histone acetyltransferase complex, a multiprotein complex that mediates histone H4 acetylation at 'Lys-5'- and 'Lys-8' (H4K5ac and H4K8ac) at transcription start sites and promotes transcription initiation.
• Vertebrate KAT8 regulatory NSL complex subunit 1-like protein (KANSL1L).

The N-terminal half the PEHE domain, which contains a β strand, an extended region, and a long α helix (see <PDB:4DNC>), interacts with the HAT domain (see <PDOC51726>) of the KAT8 histone acetyltransferase (also known as MOF and MYST1), a subunit of both MSL and NSL complexes. The C-terminal half of the MSL1 PEHE domain forms a short helical hairpin and wraps around the MSL3 MRG domain (see <PDOC51640>) as an extended chain (see <PDB:2Y0N>) [2,3,4,5].

The profile we developed covers the entire PEHE domain.