E3 ubiquitin-protein ligase MSL2 (MSL2; [intenz:6.3.2.-]) is an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. It is a component of MSL complex [].The male-specific lethal (MSL) complex is a histone acetyltransferase with specificity for histone H4 'lysine-16' in chromatin. The complex consists of MOF, MSL1, MSL2, and MSL3 []. The complex was first identified in Drosophila.
This entry represents an autonomously folded domain that binds three zinc ions. This domain can be found in E3 ubiquitin-protein ligase Msl2 from eukaryotes. The CXC domain critically contributes to the DNA-binding activity of Msl2 []. It carries 9 invariant cysteines within about a 50 residue region.
This entry represents the short coiled dimerisation domain of higher eukaryotic MSL1, part of the MSL or Male-Specific Lethal complex. This complex regulates the dosage compensation of the male X chromosome in Drosophila and other eukaryotes. The structure of the MSL1/MSL2 core shows that two MSL2 subunits bind to a dimer formed by two molecules of MSL1. MSL1 is a substrate for MSL2 E3 ubiquitin ligase activity [].
