Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC50918WWE domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC50918
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 2.4.2.30) (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 [1].
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 [1].
Some proteins known to contain a WWE domain are listed below:
- Animal members of the Deltex (DTX) family, which act as Notch signaling modifiers and may also regulate transcription through interactions with specific transcription factors.
- Vertebrate thyroid receptor interacting protein 12 (TRIP12), an HECT- domain-containing E3 ubiquitin ligase.
- An eukaryotic family of poly-ADP ribose polymerases (EC 2.4.2.30) (PARPs).
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:
| 1 | Authors | Aravind L. |
| Title | The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation. | |
| Source | Trends Biochem. Sci. 26:273-275(2001). | |
| PubMed ID | 11343911 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.