1 Proteins
DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
---|---|---|---|---|
GlymaLee.12G118100.8.p | PAC:41298754 | Glycine max Lee | 918 |
Type: | Domain | Name: | Death effector domain |
Description: | 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 ) and the caspase recruitment domain (CARD, see ), which work in similar pathways and show similar interaction properties []. 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) [].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 []. | Short Name: | DED_dom |
DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
---|---|---|---|---|
GlymaLee.12G118100.8.p | PAC:41298754 | Glycine max Lee | 918 |