death effector domain-containing protein isoform 2 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
DD super family | cl14633 | Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ... |
22-111 | 4.42e-47 | |||
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer. The actual alignment was detected with superfamily member cd08790: Pssm-ID: 472698 Cd Length: 97 Bit Score: 152.58 E-value: 4.42e-47
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Name | Accession | Description | Interval | E-value | |||
DED_DEDD | cd08790 | Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown ... |
22-111 | 4.42e-47 | |||
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. Pssm-ID: 260058 Cd Length: 97 Bit Score: 152.58 E-value: 4.42e-47
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DED | smart00031 | Death effector domain; |
24-102 | 1.98e-18 | |||
Death effector domain; Pssm-ID: 214477 Cd Length: 79 Bit Score: 77.71 E-value: 1.98e-18
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DED | pfam01335 | Death effector domain; |
26-107 | 2.20e-12 | |||
Death effector domain; Pssm-ID: 460163 Cd Length: 82 Bit Score: 61.34 E-value: 2.20e-12
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Name | Accession | Description | Interval | E-value | |||
DED_DEDD | cd08790 | Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown ... |
22-111 | 4.42e-47 | |||
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. Pssm-ID: 260058 Cd Length: 97 Bit Score: 152.58 E-value: 4.42e-47
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DED_DEDD-like | cd08339 | Death Effector Domain of DEDD and DEDD2; Death Effector Domain (DED) found in DEDD and DEDD2. ... |
22-111 | 3.38e-28 | |||
Death Effector Domain of DEDD and DEDD2; Death Effector Domain (DED) found in DEDD and DEDD2. Both proteins have a single N-terminal DED and a long C-terminal portion with no known domains. DEDD has been shown to block mitotic progression by inhibiting Cdk1 and to be involved in regulating the insulin signaling cascade. DEDD and DEDD2 can bind to themselves, to each other, 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 they can recruit other proteins into signaling complexes. Pssm-ID: 176750 Cd Length: 97 Bit Score: 104.00 E-value: 3.38e-28
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DED_DEDD2 | cd08791 | Death Effector Domain of DEDD2; Death Effector Domain (DED) found in DEDD2. DEDD2 has been ... |
21-111 | 1.58e-27 | |||
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. Pssm-ID: 176769 Cd Length: 106 Bit Score: 102.62 E-value: 1.58e-27
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DED | smart00031 | Death effector domain; |
24-102 | 1.98e-18 | |||
Death effector domain; Pssm-ID: 214477 Cd Length: 79 Bit Score: 77.71 E-value: 1.98e-18
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DED | cd00045 | Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ... |
26-102 | 4.52e-18 | |||
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. Pssm-ID: 260016 Cd Length: 77 Bit Score: 76.47 E-value: 4.52e-18
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DED | pfam01335 | Death effector domain; |
26-107 | 2.20e-12 | |||
Death effector domain; Pssm-ID: 460163 Cd Length: 82 Bit Score: 61.34 E-value: 2.20e-12
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DED_Caspase_8_10_r1 | cd08792 | Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) ... |
26-98 | 2.27e-06 | |||
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. Pssm-ID: 260059 Cd Length: 77 Bit Score: 44.51 E-value: 2.27e-06
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Blast search parameters | ||||
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