Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown to block mitotic progression by inhibiting Cdk1 and to be involved in regulating the insulin signaling cascade. DEDD can bind to itself, to DEDD2, and to the two tandem DED-containing caspases, caspase-8 and -10. In general, DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381777  22 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYV 101
Cdd:cd08790    1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                         90
                 ....*....|....*..
gi 564381777 102 TLKKRRAVCPDLVDKYL 118
Cdd:cd08790   81 TLRKRRAVCPDPVDKYL 97

Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown to block mitotic progression by inhibiting Cdk1 and to be involved in regulating the insulin signaling cascade. DEDD can bind to itself, to DEDD2, and to the two tandem DED-containing caspases, caspase-8 and -10. In general, DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381777  22 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYV 101
Cdd:cd08790    1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                         90
                 ....*....|....*..
gi 564381777 102 TLKKRRAVCPDLVDKYL 118
Cdd:cd08790   81 TLRKRRAVCPDPVDKYL 97

Death effector domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381777   26 LHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVTLKK 105
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80

                  ..
gi 564381777  106 RR 107
Cdd:pfam01335  81 RE 82

Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown to block mitotic progression by inhibiting Cdk1 and to be involved in regulating the insulin signaling cascade. DEDD can bind to itself, to DEDD2, and to the two tandem DED-containing caspases, caspase-8 and -10. In general, DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381777  22 GLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYV 101
Cdd:cd08790    1 GLYSLHRMFDIVGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLLPYV 80

                         90
                 ....*....|....*..
gi 564381777 102 TLKKRRAVCPDLVDKYL 118
Cdd:cd08790   81 TLRKRRAVCPDPVDKYL 97

Death Effector Domain of DEDD2; Death Effector Domain (DED) found in DEDD2. DEDD2 has been shown to bind to itself, DEDD, and to the two tandem DED-containing caspases, caspase-8 and -10. It may play a role in apoptosis. In general, DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381777  21 HGLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVID-DHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLP 99
Cdd:cd08791    8 YGMLSLHRMFEVVGSQLTETCGGELAFLLDETYPgKHPLDRPKSGVELLLELERRGYCDESNLRPLLQLLRVLTRHDLLP 87

                         90
                 ....*....|...
gi 564381777 100 YVTLKKRRAVCPD 112
Cdd:cd08791   88 FVSQKRRRTVSPE 100

Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a subfamily of the Death Domain (DD) superfamily. DED-containing proteins include Fas-Associated via Death Domain (FADD), Astrocyte phosphoprotein PEA-15, the initiator caspases (caspase-8 and -10), and FLICE-inhibitory protein (FLIP), among others. These proteins are prominent components of the programmed cell death (apoptosis) pathway. Some members also have non-apoptotic functions such as regulation of insulin signaling (DEDD and PEA15) and cell cycle progression (DEDD). DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564381777  26 LHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVT 102
Cdd:cd00045    1 YRQLLLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLLEKVE 77

Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564381777  26 LHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLL 98
Cdd:cd08792    1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRKDLL 73