DEDDeath effector domain
|SMART accession number:||SM00031|
|Interpro abstract (IPR001875):|
The death effector domain (DED) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DED is related in sequence and structure to the death domain (DD, see IPR000488) and the caspase recruitment domain (CARD, see IPR001315), which work in similar pathways and show similar interaction properties [(PUBMED:11504623)]. The dimerisation of DED domains is mediated primarily by electrostatic interactions. DED domains can be found in isolation, or in combination with other domains. Domains associated with DED include: caspase catalytic domains (in caspase-8, -10), death domains (in FADD), nuclear localisation sequences (in DEDD), transmembrane domains (in Bap31 and Bar), nucleotide-binding domains (in Dap3), coiled-coil domains (in Hip and Hippi), SAM domains (in Bar), and E2-binding RING domains (in Bar) [(PUBMED:15226512)].
Several DED-containing proteins are involved in the regulation of apoptosis through their interactions with DED-containing caspases (IPR002398), such as caspases 8 and 10 in humans, both of which contain tandem pairs of DEDs. There are many DED-containing modulators of apoptosis, which can either enhance or inhibit caspase activation [(PUBMED:15173180)].
|GO process:||regulation of apoptotic process (GO:0042981)|
|GO function:||protein binding (GO:0005515)|
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