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myeloid differentiation primary response protein MyD88 isoform 1 [Homo sapiens]
Death_MyD88 and TIR domain-containing protein( domain architecture ID 10169774)
Death_MyD88 and TIR domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
Death_MyD88 | cd08312 | Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ... |
29-106 | 2.92e-33 | |||
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: 116.93 E-value: 2.92e-33
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TIR | smart00255 | Toll - interleukin 1 - resistance; |
160-304 | 5.51e-33 | |||
Toll - interleukin 1 - resistance; : Pssm-ID: 214587 [Multi-domain] Cd Length: 140 Bit Score: 118.58 E-value: 5.51e-33
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Name | Accession | Description | Interval | E-value | ||||
Death_MyD88 | cd08312 | Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ... |
29-106 | 2.92e-33 | ||||
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: 116.93 E-value: 2.92e-33
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TIR | smart00255 | Toll - interleukin 1 - resistance; |
160-304 | 5.51e-33 | ||||
Toll - interleukin 1 - resistance; Pssm-ID: 214587 [Multi-domain] Cd Length: 140 Bit Score: 118.58 E-value: 5.51e-33
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Death | pfam00531 | Death domain; |
30-105 | 1.02e-13 | ||||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 65.46 E-value: 1.02e-13
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DEATH | smart00005 | DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ... |
27-105 | 3.14e-11 | ||||
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers. Pssm-ID: 214467 [Multi-domain] Cd Length: 88 Bit Score: 58.58 E-value: 3.14e-11
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TIR | pfam01582 | TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ... |
161-302 | 4.91e-10 | ||||
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades. Pssm-ID: 396246 [Multi-domain] Cd Length: 165 Bit Score: 57.37 E-value: 4.91e-10
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Name | Accession | Description | Interval | E-value | ||||
Death_MyD88 | cd08312 | Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ... |
29-106 | 2.92e-33 | ||||
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: 116.93 E-value: 2.92e-33
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TIR | smart00255 | Toll - interleukin 1 - resistance; |
160-304 | 5.51e-33 | ||||
Toll - interleukin 1 - resistance; Pssm-ID: 214587 [Multi-domain] Cd Length: 140 Bit Score: 118.58 E-value: 5.51e-33
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Death | pfam00531 | Death domain; |
30-105 | 1.02e-13 | ||||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 65.46 E-value: 1.02e-13
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DEATH | smart00005 | DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ... |
27-105 | 3.14e-11 | ||||
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers. Pssm-ID: 214467 [Multi-domain] Cd Length: 88 Bit Score: 58.58 E-value: 3.14e-11
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TIR | pfam01582 | TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ... |
161-302 | 4.91e-10 | ||||
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades. Pssm-ID: 396246 [Multi-domain] Cd Length: 165 Bit Score: 57.37 E-value: 4.91e-10
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TIR_2 | pfam13676 | TIR domain; This is a family of Toll-like receptors. |
164-265 | 6.45e-10 | ||||
TIR domain; This is a family of Toll-like receptors. Pssm-ID: 463954 [Multi-domain] Cd Length: 118 Bit Score: 55.78 E-value: 6.45e-10
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Death_p75NR | cd08311 | Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ... |
30-101 | 7.69e-10 | ||||
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin receptor (p75NTR, NGFR, TNFRSF16). p75NTR binds members of the neurotrophin (NT) family including nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and NT3, among others. It contains an NT-binding extracellular region that bears four cysteine-rich repeats, a transmembrane domain, and an intracellular DD. p75NTR plays roles in the immune, vascular, and nervous systems, and has been shown to promote cell death or survival, and to induce neurite outgrowth or collapse depending on its ligands and co-receptors. 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: 260025 Cd Length: 80 Bit Score: 54.60 E-value: 7.69e-10
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Death | cd01670 | Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ... |
36-105 | 2.24e-07 | ||||
Death Domain: a protein-protein interaction domain; Death Domains (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. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they 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. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells. Pssm-ID: 260017 [Multi-domain] Cd Length: 79 Bit Score: 47.66 E-value: 2.24e-07
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Death_UNC5C | cd08799 | Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ... |
27-105 | 4.90e-05 | ||||
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). UNC5C is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5C plays a critical role in the development of spinal accessory motor neurons. Methylation of the UNC5C gene is associated with early stages of colorectal carcinogenesis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. 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: 260064 Cd Length: 83 Bit Score: 41.15 E-value: 4.90e-05
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Death_NFkB-like | cd08310 | Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ... |
29-100 | 6.42e-05 | ||||
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear Factor-KappaB (NF-kB) precursor proteins. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). Two of these, NF-kB1 and NF-kB2 are produced from the processing of the precursor proteins p105 and p100, respectively. In addition to RHD, p105 and p100 contain ANK repeats and a C-terminal DD. NF-kBs are regulated by the Inhibitor of NF-kB (IkB) Kinase (IKK) complex through classical and non-canonical pathways, which differ in the IKK subunits involved and downstream targets. IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. The precursor proteins p105 and p100 function as IkBs and as NF-kB proteins after being processed by the proteasome. 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: 260024 Cd Length: 72 Bit Score: 40.30 E-value: 6.42e-05
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Death_IRAK | cd08309 | Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ... |
25-97 | 8.28e-05 | ||||
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: 40.79 E-value: 8.28e-05
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Death_NMPP84 | cd08318 | Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ... |
41-101 | 1.17e-04 | ||||
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix Protein P84 (also known as HPR1 or THOC1). HPR1/p84 resides in the nuclear matrix and is part of the THO complex, also called TREX (transcription/export) complex, which functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Mice lacking THOC1 have abnormal testis development and are sterile. 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: 260030 Cd Length: 86 Bit Score: 40.20 E-value: 1.17e-04
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Death_UNC5-like | cd08781 | Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ... |
25-103 | 3.92e-04 | ||||
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in Uncoordinated-5 (UNC-5) homolog family, which includes Unc5A, B, C and D in vertebrates. UNC5 proteins are receptors for secreted netrins (netrin-1, -3 and -4) that are involved in diverse processes like axonal guidance, neuronal migration, blood vessel patterning, and apoptosis. They are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. 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: 260051 Cd Length: 83 Bit Score: 38.41 E-value: 3.92e-04
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Death_DAPK1 | cd08782 | Death domain found in death-associated protein kinase 1; Death domain (DD) found in ... |
29-101 | 1.32e-03 | ||||
Death domain found in death-associated protein kinase 1; Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. 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: 260052 Cd Length: 82 Bit Score: 36.94 E-value: 1.32e-03
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Death_UNC5B | cd08802 | Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ... |
25-103 | 2.06e-03 | ||||
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). UNC5B is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5B signaling is involved in the netrin-1-induced proliferation and migration of renal proximal tubular cells. It is also required for vascular patterning during embryonic development, and its activation inhibits sprouting angiogenesis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. 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: 176780 Cd Length: 84 Bit Score: 36.54 E-value: 2.06e-03
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Death_ank2 | cd08804 | Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ... |
28-102 | 3.03e-03 | ||||
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-2, also called ankyrin-B (for broadly expressed), is required for proper function of the Na/Ca ion exchanger-1 in cardiomyocytes, and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. Human ANK-2 is associated with "Ankyrin-B syndrome", an atypical arrythmia disorder with risk of sudden cardiac death. It also plays key roles in the brain and striated muscle. Loss of ANK-2 is associated with significant nervous system defects and sarcomere disorganization. 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: 260066 Cd Length: 84 Bit Score: 36.21 E-value: 3.03e-03
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