CRADD [Mus musculus]
protein kinase family protein( domain architecture ID 10169992)
protein kinase family protein containing a Death domain (DD), may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates
List of domain hits
Name | Accession | Description | Interval | E-value | |||
CARD_RAIDD | cd08327 | Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a ... |
1-94 | 1.23e-50 | |||
Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a death domain; Caspase activation and recruitment domain (CARD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal CARD, which interacts with the caspase-2 CARD, and a C-terminal Death domain (DD), which interacts with the DD of PIDD. In general, CARDs are DDs associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. : Pssm-ID: 260037 Cd Length: 94 Bit Score: 158.78 E-value: 1.23e-50
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Death_RAIDD | cd08319 | Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ... |
116-198 | 3.33e-44 | |||
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. 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, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. : Pssm-ID: 260031 Cd Length: 83 Bit Score: 142.08 E-value: 3.33e-44
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Name | Accession | Description | Interval | E-value | |||
CARD_RAIDD | cd08327 | Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a ... |
1-94 | 1.23e-50 | |||
Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a death domain; Caspase activation and recruitment domain (CARD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal CARD, which interacts with the caspase-2 CARD, and a C-terminal Death domain (DD), which interacts with the DD of PIDD. In general, CARDs are DDs associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260037 Cd Length: 94 Bit Score: 158.78 E-value: 1.23e-50
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Death_RAIDD | cd08319 | Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ... |
116-198 | 3.33e-44 | |||
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. 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, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260031 Cd Length: 83 Bit Score: 142.08 E-value: 3.33e-44
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CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
1-92 | 7.40e-24 | |||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain. Pssm-ID: 128424 Cd Length: 88 Bit Score: 90.09 E-value: 7.40e-24
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CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-87 | 2.16e-16 | |||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold. Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 70.67 E-value: 2.16e-16
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DEATH | smart00005 | DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ... |
113-190 | 2.33e-13 | |||
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: 62.81 E-value: 2.33e-13
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Death | pfam00531 | Death domain; |
117-198 | 1.31e-12 | |||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 60.84 E-value: 1.31e-12
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Name | Accession | Description | Interval | E-value | |||
CARD_RAIDD | cd08327 | Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a ... |
1-94 | 1.23e-50 | |||
Caspase activation and recruitment domain of RIP-associated ICH-1 homologous protein with a death domain; Caspase activation and recruitment domain (CARD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal CARD, which interacts with the caspase-2 CARD, and a C-terminal Death domain (DD), which interacts with the DD of PIDD. In general, CARDs are DDs associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260037 Cd Length: 94 Bit Score: 158.78 E-value: 1.23e-50
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Death_RAIDD | cd08319 | Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ... |
116-198 | 3.33e-44 | |||
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. 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, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260031 Cd Length: 83 Bit Score: 142.08 E-value: 3.33e-44
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CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
1-92 | 7.40e-24 | |||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain. Pssm-ID: 128424 Cd Length: 88 Bit Score: 90.09 E-value: 7.40e-24
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CARD | cd01671 | Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
9-86 | 2.02e-18 | |||
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260018 [Multi-domain] Cd Length: 79 Bit Score: 75.63 E-value: 2.02e-18
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CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-87 | 2.16e-16 | |||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold. Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 70.67 E-value: 2.16e-16
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DEATH | smart00005 | DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ... |
113-190 | 2.33e-13 | |||
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: 62.81 E-value: 2.33e-13
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Death | cd01670 | Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ... |
119-188 | 2.53e-13 | |||
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: 62.30 E-value: 2.53e-13
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Death | pfam00531 | Death domain; |
117-198 | 1.31e-12 | |||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 60.84 E-value: 1.31e-12
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CARD_CASP2 | cd08332 | Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ... |
1-78 | 2.18e-12 | |||
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. 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 DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260040 Cd Length: 87 Bit Score: 60.13 E-value: 2.18e-12
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CARD_BCL10 | cd08810 | Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ... |
6-78 | 1.61e-08 | |||
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and recruitment domain (CARD) similar to that found in BCL10 (B-cell lymphoma 10). BCL10 and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1) are the integral components of CBM signalosomes. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. Both CARMA1 and CARD9 associate with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. 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 DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260072 [Multi-domain] Cd Length: 85 Bit Score: 50.04 E-value: 1.61e-08
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Death_FADD | cd08306 | Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ... |
127-184 | 6.35e-07 | |||
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). 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, FAS, and its DED recruits the initiator caspases, caspase-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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. Pssm-ID: 260020 Cd Length: 85 Bit Score: 45.75 E-value: 6.35e-07
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CARD_CASP9 | cd08326 | Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ... |
5-78 | 2.83e-06 | |||
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment domain (CARD) similar to that found in caspase-9 (CASP9, MCH6, APAF3), which interacts with the CARD of apoptotic protease-activating factor 1 (APAF-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-9 is the initiator caspase associated with the intrinsic or mitochondrial pathway of apoptosis, induced by many pro-apoptotic signals. Together with APAF-1, it forms the heptameric 'apoptosome' in response to the release of cytochrome c from mitochondria. Activated caspase-9 cleaves and activates downstream effector caspases, like caspase-3, caspase-6, and caspase-7, resulting in apoptosis. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 176740 Cd Length: 84 Bit Score: 43.95 E-value: 2.83e-06
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CARD_CARD9-like | cd08785 | Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ... |
29-86 | 2.18e-05 | |||
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation and recruitment domain (CARD) found in CARD9, CARD14 (CARMA2), CARD10 (CARMA3), CARD11 (CARMA1) and BCL10. BCL10 (B-cell lymphoma 10), together with Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), are integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells), and with CARD11 to form L-CBM (CBM complex in lymphoid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. BCL10/Malt1 also associates with CARD10, which is more widely expressed and is not restricted to hematopoietic cells, to play a role in GPCR-induced NF-kB activation. CARD14 has also been shown to associate with BCL10. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. 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 DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260055 Cd Length: 84 Bit Score: 41.20 E-value: 2.18e-05
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Death_ank | cd08317 | Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ... |
116-186 | 6.61e-04 | |||
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. 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. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. 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: 260029 Cd Length: 84 Bit Score: 37.24 E-value: 6.61e-04
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Death_PIDD | cd08779 | Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ... |
123-170 | 8.12e-03 | |||
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. 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, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260049 Cd Length: 86 Bit Score: 34.21 E-value: 8.12e-03
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Blast search parameters | ||||
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