|PROSITE documentation PDOC50918 [for PROSITE entry PS50918]|
The WWE domain is a ~80-residue globular domain occuring in two functional classes of proteins, namely those associated with ubiquitination and those associated with poly-ADP ribosylation. The former class includes its combinations with the HECT-type E3 ligases (see <PDOC50237>), the classic RING or the RING-H2 domains (see <PDOC00449>), and the ubiquitin-binding UBA domain (see <PDOC50030>). Analogous to the ubiquitin ligases, eukaryotic poly-ADP ribose polymerases (EC 184.108.40.206) (PARPs) covalently modify proteins through the addition of multiple ADP-ribose moieties and participate in functions such as DNA repair and chromatin dynamics. The WWE domain is present in either single or duplicate copies in a novel sub-family of PARPs. The WWE domain was named after its most conserved residues, two tryptophan (W) residues and a glutamate (E) residue. It has been suggested that the WWE domain functions in specific interactions with other proteins and could help in targeting the different kinds of E3-like and ADP-ribosylation activities to proteins participating in various signaling cascades .
Secondary structure prediction suggests the presence of multiple β strands that correspond to the conserved N- and C- terminal motifs of the WWE domain that are enriched in hydrophobic or aromatic residues. There is a single prominent helix that corresponds to the central motif containing the conserved glutamate. The secondary structure pattern with a two-strand hairpin at the N-terminus followed by a helix is reminiscent of the β-grasp fold adopted by ubiquitin and several other eukaryotic specific α/β domains .
Some proteins known to contain a WWE domain are listed below:
The profile we developed covers the entire WWE domain.Last update:
August 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|Title||The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation.|
|Source||Trends Biochem. Sci. 26:273-275(2001).|