Death effector domain
SMART accession number:SM00031
Description: -
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, 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)
Family alignment:
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There are 4001 DED domains in 2589 proteins in SMART's nrdb database.

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