hCG16983, isoform CRA_f [Homo sapiens]
Protein Classification
DED_Caspase_8_r1 and CASc domain-containing protein( domain architecture ID 10170020)
protein containing domains DED_Caspase_8_r1, DD, and CASc
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
302-554 | 3.33e-116 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs. : Pssm-ID: 237997 Cd Length: 243 Bit Score: 343.81 E-value: 3.33e-116
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| DED_Caspase_8_r1 | cd08333 | Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ... |
62-143 | 7.85e-43 | |||||
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), 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 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms 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 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains 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: 260041 Cd Length: 82 Bit Score: 147.54 E-value: 7.85e-43
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| DD super family | cl14633 | Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ... |
194-272 | 1.40e-35 | |||||
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 cd08813: Pssm-ID: 472698 Cd Length: 83 Bit Score: 128.00 E-value: 1.40e-35
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| Name | Accession | Description | Interval | E-value | |||||
| CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
302-554 | 3.33e-116 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs. Pssm-ID: 237997 Cd Length: 243 Bit Score: 343.81 E-value: 3.33e-116
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| CASc | smart00115 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ... |
303-554 | 1.81e-111 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues. Pssm-ID: 214521 Cd Length: 241 Bit Score: 331.90 E-value: 1.81e-111
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| Peptidase_C14 | pfam00656 | Caspase domain; |
310-552 | 1.93e-66 | |||||
Caspase domain; Pssm-ID: 425803 Cd Length: 213 Bit Score: 214.49 E-value: 1.93e-66
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| DED_Caspase_8_r1 | cd08333 | Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ... |
62-143 | 7.85e-43 | |||||
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), 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 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms 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 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains 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: 260041 Cd Length: 82 Bit Score: 147.54 E-value: 7.85e-43
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| DED_Caspase_8_r2 | cd08813 | Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ... |
194-272 | 1.40e-35 | |||||
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 2. 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 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms 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 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains 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: 176791 Cd Length: 83 Bit Score: 128.00 E-value: 1.40e-35
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| DED | pfam01335 | Death effector domain; |
62-143 | 9.55e-26 | |||||
Death effector domain; Pssm-ID: 460163 Cd Length: 82 Bit Score: 100.63 E-value: 9.55e-26
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| DED | smart00031 | Death effector domain; |
60-139 | 2.26e-22 | |||||
Death effector domain; Pssm-ID: 214477 Cd Length: 79 Bit Score: 91.19 E-value: 2.26e-22
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| DED | pfam01335 | Death effector domain; |
193-272 | 6.96e-22 | |||||
Death effector domain; Pssm-ID: 460163 Cd Length: 82 Bit Score: 89.85 E-value: 6.96e-22
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| DED | smart00031 | Death effector domain; |
194-270 | 5.21e-17 | |||||
Death effector domain; Pssm-ID: 214477 Cd Length: 79 Bit Score: 75.78 E-value: 5.21e-17
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| Name | Accession | Description | Interval | E-value | |||||
| CASc | cd00032 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent ... |
302-554 | 3.33e-116 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologs. Pssm-ID: 237997 Cd Length: 243 Bit Score: 343.81 E-value: 3.33e-116
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| CASc | smart00115 | Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that ... |
303-554 | 1.81e-111 | |||||
Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues. Pssm-ID: 214521 Cd Length: 241 Bit Score: 331.90 E-value: 1.81e-111
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| Peptidase_C14 | pfam00656 | Caspase domain; |
310-552 | 1.93e-66 | |||||
Caspase domain; Pssm-ID: 425803 Cd Length: 213 Bit Score: 214.49 E-value: 1.93e-66
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| DED_Caspase_8_r1 | cd08333 | Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ... |
62-143 | 7.85e-43 | |||||
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), 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 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms 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 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains 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: 260041 Cd Length: 82 Bit Score: 147.54 E-value: 7.85e-43
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| DED_Caspase_8_r2 | cd08813 | Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ... |
194-272 | 1.40e-35 | |||||
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 2. 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 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms 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 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains 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: 176791 Cd Length: 83 Bit Score: 128.00 E-value: 1.40e-35
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| DED_Caspase-like_r2 | cd08775 | Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED) ... |
194-270 | 3.38e-30 | |||||
Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED), second repeat, found in initator caspase-like proteins like caspase-8, -10 and c-FLIP. 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. 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. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members 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: 176753 Cd Length: 81 Bit Score: 113.03 E-value: 3.38e-30
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| DED_Caspase_8_10_r2 | cd08334 | Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ... |
195-272 | 6.43e-27 | |||||
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 2. 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: 260042 Cd Length: 83 Bit Score: 103.82 E-value: 6.43e-27
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| DED | pfam01335 | Death effector domain; |
62-143 | 9.55e-26 | |||||
Death effector domain; Pssm-ID: 460163 Cd Length: 82 Bit Score: 100.63 E-value: 9.55e-26
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| DED | smart00031 | Death effector domain; |
60-139 | 2.26e-22 | |||||
Death effector domain; Pssm-ID: 214477 Cd Length: 79 Bit Score: 91.19 E-value: 2.26e-22
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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) ... |
62-134 | 5.59e-22 | |||||
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: 89.96 E-value: 5.59e-22
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| DED | pfam01335 | Death effector domain; |
193-272 | 6.96e-22 | |||||
Death effector domain; Pssm-ID: 460163 Cd Length: 82 Bit Score: 89.85 E-value: 6.96e-22
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| DED | smart00031 | Death effector domain; |
194-270 | 5.21e-17 | |||||
Death effector domain; Pssm-ID: 214477 Cd Length: 79 Bit Score: 75.78 E-value: 5.21e-17
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| DED_FADD | cd08336 | Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ... |
56-137 | 2.63e-14 | |||||
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) found in Fas-Associated via Death Domain (FADD). DEDs comprise a subfamily of the Death Domain (DD) superfamily. FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor and its DED recruits the initiator caspases 8 and 10 to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. 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: 260043 Cd Length: 82 Bit Score: 68.37 E-value: 2.63e-14
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| DED | cd00045 | Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ... |
66-136 | 3.25e-14 | |||||
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: 67.61 E-value: 3.25e-14
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| DED_Caspase-like_r1 | cd08776 | Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED) ... |
66-138 | 1.08e-13 | |||||
Death effector domain, repeat 1, of initator caspase-like proteins; Death Effector Domain (DED), first repeat, found in initator caspase-like proteins, like caspase-8 and -10 and c-FLIP. 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. 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. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members 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: 176754 Cd Length: 71 Bit Score: 66.01 E-value: 1.08e-13
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| DED_Caspase_8_10_r2 | cd08334 | Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) ... |
56-125 | 5.39e-11 | |||||
Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 2. 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: 260042 Cd Length: 83 Bit Score: 58.75 E-value: 5.39e-11
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| DED_Caspase_10_r2 | cd08814 | Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ... |
194-272 | 5.88e-11 | |||||
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in Caspase-10, repeat 2. 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-10 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-8 and the pseudo-caspase c-FLIP, it forms 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. It contains 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: 260074 Cd Length: 79 Bit Score: 58.58 E-value: 5.88e-11
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| DED_Caspase_10_r1 | cd08341 | Death effector domain, repeat 1, of Caspase-10; Death effector domain (DED) found in ... |
60-134 | 2.61e-09 | |||||
Death effector domain, repeat 1, of Caspase-10; Death effector domain (DED) found in 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-10 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-8 and the pseudo-caspase c-FLIP, it forms 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. It contains 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: 260047 Cd Length: 82 Bit Score: 53.98 E-value: 2.61e-09
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| DED | cd00045 | Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ... |
193-261 | 4.53e-07 | |||||
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: 47.58 E-value: 4.53e-07
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| DED_PEA15 | cd08338 | Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar ... |
61-143 | 3.11e-06 | |||||
Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar to that found in PEA-15 (Astrocyte phosphoprotein PEA-15). PEA-15 is a multifunctional phosphoprotein that modulates signaling pathways, like the ERK MAP kinase cascade by binding to ERK and changing its subcellular localization. It has been implicated in apoptosis, cell proliferation, and glucose metabolism. It does not possess enzymatic activity and mainly acts as an adaptor protein. PEA-15 contains an N-terminal DED domain and a C-terminal disordered region. 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: 260045 Cd Length: 84 Bit Score: 45.53 E-value: 3.11e-06
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| DED_Caspase_8_r1 | cd08333 | Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 ... |
196-261 | 6.19e-06 | |||||
Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), 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 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms 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 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains 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: 260041 Cd Length: 82 Bit Score: 44.31 E-value: 6.19e-06
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| DED_c-FLIP_r1 | cd08337 | Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain ... |
66-146 | 3.84e-05 | |||||
Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 1, similar to that found in FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-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: 260044 Cd Length: 80 Bit Score: 42.02 E-value: 3.84e-05
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| DED_c-FLIP_r2 | cd08340 | Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ... |
68-133 | 1.31e-04 | |||||
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 2, similar to that found in cellular FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-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: 260046 Cd Length: 81 Bit Score: 40.80 E-value: 1.31e-04
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| DED_DEDD | cd08790 | Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown ... |
69-134 | 1.55e-04 | |||||
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: 40.87 E-value: 1.55e-04
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| DED_Caspase_10_r2 | cd08814 | Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in ... |
56-124 | 3.87e-04 | |||||
Death Effector Domain, repeat 2, of Caspase-10; Death effector domain (DED) found in Caspase-10, repeat 2. 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-10 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-8 and the pseudo-caspase c-FLIP, it forms 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. It contains 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: 260074 Cd Length: 79 Bit Score: 39.32 E-value: 3.87e-04
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| DED_FADD | cd08336 | Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) ... |
194-271 | 5.76e-04 | |||||
Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) found in Fas-Associated via Death Domain (FADD). DEDs comprise a subfamily of the Death Domain (DD) superfamily. FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor and its DED recruits the initiator caspases 8 and 10 to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. 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: 260043 Cd Length: 82 Bit Score: 38.70 E-value: 5.76e-04
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| DED_Caspase_8_r2 | cd08813 | Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 ... |
66-130 | 1.36e-03 | |||||
Death Effector Domain, repeat 2, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 2. 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 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms 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 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains 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: 176791 Cd Length: 83 Bit Score: 37.86 E-value: 1.36e-03
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| DED_c-FLIP_r2 | cd08340 | Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain ... |
194-252 | 1.37e-03 | |||||
Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 2, similar to that found in cellular FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-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: 260046 Cd Length: 81 Bit Score: 37.72 E-value: 1.37e-03
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