ectodysplasin-A receptor-associated adapter protein isoform 1 [Mus musculus]
Protein Classification
Death domain-containing protein( domain architecture ID 10455265)
Death domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Death | pfam00531 | Death domain; |
122-192 | 5.52e-15 | ||
Death domain; : Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 67.39 E-value: 5.52e-15
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| Name | Accession | Description | Interval | E-value | ||
| Death | pfam00531 | Death domain; |
122-192 | 5.52e-15 | ||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 67.39 E-value: 5.52e-15
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| Death_IRAK | cd08309 | Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ... |
122-188 | 1.37e-04 | ||
Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in Interleukin-1 (IL-1) Receptor-Associated Kinases (IRAK1-4) and similar proteins. IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. All four types are involved in signal transduction involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinase pathways. IRAK1 and IRAK4 are active kinases while IRAK2 and IRAK-M (also called IRAK3) are inactive. In general, IRAKs are expressed ubiquitously, except for IRAK-M which is detected only in macrophages. The insect homologs, Pelle and Tube, are important components of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in the innate immune response. Most members have an N-terminal DD followed by a kinase domain. In general, 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260023 Cd Length: 88 Bit Score: 39.25 E-value: 1.37e-04
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| Name | Accession | Description | Interval | E-value | ||
| Death | pfam00531 | Death domain; |
122-192 | 5.52e-15 | ||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 67.39 E-value: 5.52e-15
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| Death_IRAK | cd08309 | Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ... |
122-188 | 1.37e-04 | ||
Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in Interleukin-1 (IL-1) Receptor-Associated Kinases (IRAK1-4) and similar proteins. IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. All four types are involved in signal transduction involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinase pathways. IRAK1 and IRAK4 are active kinases while IRAK2 and IRAK-M (also called IRAK3) are inactive. In general, IRAKs are expressed ubiquitously, except for IRAK-M which is detected only in macrophages. The insect homologs, Pelle and Tube, are important components of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in the innate immune response. Most members have an N-terminal DD followed by a kinase domain. In general, 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260023 Cd Length: 88 Bit Score: 39.25 E-value: 1.37e-04
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| Death_MyD88 | cd08312 | Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ... |
122-184 | 4.23e-03 | ||
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. In general, 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260026 Cd Length: 79 Bit Score: 34.88 E-value: 4.23e-03
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