THO complex subunit 1 isoform 1 [Mus musculus]
Protein Classification
efThoc1 and Death_NMPP84 domain-containing protein( domain architecture ID 10571689)
efThoc1 and Death_NMPP84 domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| efThoc1 | pfam11957 | THO complex subunit 1 transcription elongation factor; The THO complex plays a role in ... |
74-539 | 3.34e-164 | ||||||||
THO complex subunit 1 transcription elongation factor; The THO complex plays a role in coupling transcription elongation to mRNA export. It is composed of subunits THP2, HPR1, THO2 and MFT1. The THO complex is a nuclear complex that is required for transcription elongation through genes containing tandemly repeated DNA sequences. The THO complex is also part of the TREX (TRanscription EXport) complex that is involved in coupling transcription to export of mRNAs to the cytoplasm. : Pssm-ID: 463412 Cd Length: 464 Bit Score: 478.80 E-value: 3.34e-164
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| Death_NMPP84 | cd08318 | Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ... |
565-650 | 5.32e-47 | ||||||||
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: 160.38 E-value: 5.32e-47
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| Name | Accession | Description | Interval | E-value | ||||||||
| efThoc1 | pfam11957 | THO complex subunit 1 transcription elongation factor; The THO complex plays a role in ... |
74-539 | 3.34e-164 | ||||||||
THO complex subunit 1 transcription elongation factor; The THO complex plays a role in coupling transcription elongation to mRNA export. It is composed of subunits THP2, HPR1, THO2 and MFT1. The THO complex is a nuclear complex that is required for transcription elongation through genes containing tandemly repeated DNA sequences. The THO complex is also part of the TREX (TRanscription EXport) complex that is involved in coupling transcription to export of mRNAs to the cytoplasm. Pssm-ID: 463412 Cd Length: 464 Bit Score: 478.80 E-value: 3.34e-164
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| Death_NMPP84 | cd08318 | Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ... |
565-650 | 5.32e-47 | ||||||||
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: 160.38 E-value: 5.32e-47
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| Death | pfam00531 | Death domain; |
572-651 | 3.10e-20 | ||||||||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 85.49 E-value: 3.10e-20
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| DEATH | smart00005 | DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ... |
570-652 | 9.92e-18 | ||||||||
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: 78.22 E-value: 9.92e-18
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| Name | Accession | Description | Interval | E-value | ||||||||
| efThoc1 | pfam11957 | THO complex subunit 1 transcription elongation factor; The THO complex plays a role in ... |
74-539 | 3.34e-164 | ||||||||
THO complex subunit 1 transcription elongation factor; The THO complex plays a role in coupling transcription elongation to mRNA export. It is composed of subunits THP2, HPR1, THO2 and MFT1. The THO complex is a nuclear complex that is required for transcription elongation through genes containing tandemly repeated DNA sequences. The THO complex is also part of the TREX (TRanscription EXport) complex that is involved in coupling transcription to export of mRNAs to the cytoplasm. Pssm-ID: 463412 Cd Length: 464 Bit Score: 478.80 E-value: 3.34e-164
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| Death_NMPP84 | cd08318 | Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ... |
565-650 | 5.32e-47 | ||||||||
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: 160.38 E-value: 5.32e-47
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| Death | pfam00531 | Death domain; |
572-651 | 3.10e-20 | ||||||||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 85.49 E-value: 3.10e-20
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| Death | cd01670 | Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ... |
573-649 | 8.53e-18 | ||||||||
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: 78.09 E-value: 8.53e-18
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| DEATH | smart00005 | DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ... |
570-652 | 9.92e-18 | ||||||||
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: 78.22 E-value: 9.92e-18
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| Death_ank | cd08317 | Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ... |
577-644 | 8.88e-10 | ||||||||
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: 55.73 E-value: 8.88e-10
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| Death_FADD | cd08306 | Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ... |
579-647 | 4.30e-06 | ||||||||
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: 45.36 E-value: 4.30e-06
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| Death_TRADD | cd08780 | Death Domain of Tumor Necrosis Factor Receptor 1-Associated Death Domain protein; Death domain ... |
570-649 | 6.10e-05 | ||||||||
Death Domain of Tumor Necrosis Factor Receptor 1-Associated Death Domain protein; Death domain (DD) of TRADD (TNF Receptor 1-Associated Death Domain or TNFRSF1A-associated via death domain) protein. TRADD is a central signaling adaptor for TNF-receptor 1 (TNFR1), mediating activation of Nuclear Factor -kappaB (NF-kB) and c-Jun N-terminal kinase (JNK), as well as caspase-dependent apoptosis. It also carries important immunological roles including germinal center formation, DR3-mediated T-cell stimulation, and TNFalpha-mediated 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 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: 260050 Cd Length: 90 Bit Score: 42.18 E-value: 6.10e-05
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| Death_PIDD | cd08779 | Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ... |
576-652 | 1.51e-04 | ||||||||
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: 40.76 E-value: 1.51e-04
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| Death_TNFR1 | cd08313 | Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ... |
584-649 | 5.46e-04 | ||||||||
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis factor receptor-1 (TNFR-1). TNFR-1 has many names including TNFRSF1A, CD120a, p55, p60, and TNFR60. It activates two major intracellular signaling pathways that lead to the activation of the transcription factor NF-kB and the induction of cell death. Upon binding of its ligand TNF, TNFR-1 trimerizes which leads to the recruitment of an adaptor protein named TNFR-associated death domain protein (TRADD) through a DD/DD interaction. Mutations in the TNFRSF1A gene causes TNFR-associated periodic syndrome (TRAPS), a rare disorder characterized recurrent fever, myalgia, abdominal pain, conjunctivitis and skin eruptions. 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: 176729 Cd Length: 80 Bit Score: 38.91 E-value: 5.46e-04
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| Death_ank2 | cd08804 | Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ... |
572-645 | 1.24e-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: 38.14 E-value: 1.24e-03
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| Death_RIP1 | cd08777 | Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ... |
570-651 | 1.26e-03 | ||||||||
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal DD, which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. 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: 260048 Cd Length: 86 Bit Score: 38.18 E-value: 1.26e-03
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| Death_RAIDD | cd08319 | Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ... |
570-640 | 1.32e-03 | ||||||||
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: 38.08 E-value: 1.32e-03
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