Death effector domain

Definition

The death effector domain (DED) is a homotypic protein interaction module composed of a bundle of six α-helices. DED is related in sequence and structure to the death domain (DD, see [interpro:IPR000488]) and the caspase recruitment domain (CARD, see [interpro:IPR001315]), which work in similar pathways and show similar interaction properties PMID: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) PMID: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 PMID:15173180.

7 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (7 proteins: gene, accession, name)

• CASP10
• CASP8
• CFLAR
• DEDD
• DEDD2
• FADD
• PEA15