nuclear factor NF-kappa-B p105 subunit isoform 1 [Homo sapiens]
Protein Classification
ankyrin repeat domain-containing protein( domain architecture ID 12958902)
ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| RHD-n_NFkB1 | cd07935 | N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ... |
43-244 | 2.20e-143 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa B1); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B1 is involved in the canonical NF-kappa B signaling pathway which is activated by many agonists and is essential in immune and inflammatory responses, as well as cell survival. p105 is involved in its own specific NF-kappa B signaling pathway which is also implicated in immune and inflammatory responses. p105 may also act as an I-kappa B due to its C-terminal ankyrin repeats. It is also involved in mitogen-activated protein kinase (MAPK) signaling as its degradation leads to the activation of TPL-2, a MAPK kinase kinase which activates ERK pathways. : Pssm-ID: 143651 Cd Length: 202 Bit Score: 425.08 E-value: 2.20e-143
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| IPT_NFkappaB | cd01177 | IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ... |
251-352 | 2.17e-62 | |||||
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation. : Pssm-ID: 238582 Cd Length: 102 Bit Score: 206.02 E-value: 2.17e-62
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| Death_NFkB1_p105 | cd08797 | Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ... |
816-891 | 2.89e-44 | |||||
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the Nuclear Factor-KappaB1 (NF-kB1) precursor protein p105. 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). NF-kB1 (or p50) is produced from the processing of the precursor protein p105, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the classical (or canonical) NF-kB pathway. In the cytosol, p50 forms an inactive complex with RelA (or p65) and the Inhibitor of NF-kB (IkB). Activation is triggered by the phosphorylation and degradation of IkB, resulting in the active DNA-binding p50-RelA dimer to migrate to the nucleus. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. 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: 260063 Cd Length: 76 Bit Score: 154.29 E-value: 2.89e-44
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
499-759 | 1.49e-34 | |||||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.93 E-value: 1.49e-34
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| Name | Accession | Description | Interval | E-value | |||||
| RHD-n_NFkB1 | cd07935 | N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ... |
43-244 | 2.20e-143 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa B1); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B1 is involved in the canonical NF-kappa B signaling pathway which is activated by many agonists and is essential in immune and inflammatory responses, as well as cell survival. p105 is involved in its own specific NF-kappa B signaling pathway which is also implicated in immune and inflammatory responses. p105 may also act as an I-kappa B due to its C-terminal ankyrin repeats. It is also involved in mitogen-activated protein kinase (MAPK) signaling as its degradation leads to the activation of TPL-2, a MAPK kinase kinase which activates ERK pathways. Pssm-ID: 143651 Cd Length: 202 Bit Score: 425.08 E-value: 2.20e-143
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| RHD_DNA_bind | pfam00554 | Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ... |
45-243 | 9.76e-84 | |||||
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain. Pssm-ID: 425749 Cd Length: 169 Bit Score: 266.86 E-value: 9.76e-84
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| IPT_NFkappaB | cd01177 | IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ... |
251-352 | 2.17e-62 | |||||
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation. Pssm-ID: 238582 Cd Length: 102 Bit Score: 206.02 E-value: 2.17e-62
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| RHD_dimer | pfam16179 | Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ... |
252-353 | 7.56e-57 | |||||
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain. Pssm-ID: 465045 Cd Length: 102 Bit Score: 190.85 E-value: 7.56e-57
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| Death_NFkB1_p105 | cd08797 | Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ... |
816-891 | 2.89e-44 | |||||
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the Nuclear Factor-KappaB1 (NF-kB1) precursor protein p105. 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). NF-kB1 (or p50) is produced from the processing of the precursor protein p105, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the classical (or canonical) NF-kB pathway. In the cytosol, p50 forms an inactive complex with RelA (or p65) and the Inhibitor of NF-kB (IkB). Activation is triggered by the phosphorylation and degradation of IkB, resulting in the active DNA-binding p50-RelA dimer to migrate to the nucleus. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. 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: 260063 Cd Length: 76 Bit Score: 154.29 E-value: 2.89e-44
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
499-759 | 1.49e-34 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.93 E-value: 1.49e-34
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
587-681 | 3.27e-17 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.46 E-value: 3.27e-17
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| IPT | smart00429 | ig-like, plexins, transcription factors; |
250-351 | 1.29e-13 | |||||
ig-like, plexins, transcription factors; Pssm-ID: 214657 [Multi-domain] Cd Length: 90 Bit Score: 67.06 E-value: 1.29e-13
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
576-727 | 4.07e-13 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 4.07e-13
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| DEATH | smart00005 | DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ... |
814-892 | 2.55e-12 | |||||
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: 63.58 E-value: 2.55e-12
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| Death | pfam00531 | Death domain; |
817-893 | 2.15e-11 | |||||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 60.84 E-value: 2.15e-11
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
544-733 | 1.68e-10 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 64.65 E-value: 1.68e-10
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
576-680 | 7.55e-06 | |||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.08 E-value: 7.55e-06
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
585-609 | 4.64e-03 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 4.64e-03
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| Name | Accession | Description | Interval | E-value | |||||
| RHD-n_NFkB1 | cd07935 | N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa ... |
43-244 | 2.20e-143 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa B1 (NF-kappa B1); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B1 is involved in the canonical NF-kappa B signaling pathway which is activated by many agonists and is essential in immune and inflammatory responses, as well as cell survival. p105 is involved in its own specific NF-kappa B signaling pathway which is also implicated in immune and inflammatory responses. p105 may also act as an I-kappa B due to its C-terminal ankyrin repeats. It is also involved in mitogen-activated protein kinase (MAPK) signaling as its degradation leads to the activation of TPL-2, a MAPK kinase kinase which activates ERK pathways. Pssm-ID: 143651 Cd Length: 202 Bit Score: 425.08 E-value: 2.20e-143
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| RHD-n_NFkB | cd07883 | N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light ... |
43-244 | 2.34e-129 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of kappa light polypeptide gene enhancer in B-cells (NF-kappa B); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B1 and B2 families of transcription factors, also referred to as class I members of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. Family members include NF-kappa B1 and NF-kappa B2. NF-kappa B1 is commonly referred to as p105 or p50 (proteolytically processed form), while NF-kappa B2 is called p100 or p52 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). p105 and p100 may also act as I-kappa Bs due to their C-terminal ankyrin repeats. Pssm-ID: 143643 Cd Length: 197 Bit Score: 388.37 E-value: 2.34e-129
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| RHD_DNA_bind | pfam00554 | Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are ... |
45-243 | 9.76e-84 | |||||
Rel homology DNA-binding domain; Proteins containing the Rel homology domain (RHD) are eukaryotic transcription factors. The RHD is composed of two structural domains. This is the N-terminal DNA-binding domain that is similar to that found in P53. The C-terminal domain has an immunoglobulin-like fold (See pfam16179) that functions as a dimerization domain. Pssm-ID: 425749 Cd Length: 169 Bit Score: 266.86 E-value: 9.76e-84
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| RHD-n_NFkB2 | cd07934 | N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2) ... |
43-244 | 4.29e-80 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor kappa B2 (NF-kappa B2); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NF-kappa B2 family of transcription factors, a class I member of the NF-kappa B family. In class I NF-kappa Bs, the RHD domain co-occurs with C-terminal ankyrin repeats. NF-kappa B2 is commonly referred to as p100 or p52 (proteolytically processed form). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and REL). NF-kappa B2 is involved in the alternative NF-kappa B signaling pathway which is activated by few agonists and plays an important role in secondary lymphoid organogenesis, maturation of B-cells, and adaptive humoral immunity. p100 may also act as an I-kappa B due to its C-terminal ankyrin repeats. Pssm-ID: 143650 Cd Length: 185 Bit Score: 257.90 E-value: 4.29e-80
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| IPT_NFkappaB | cd01177 | IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is ... |
251-352 | 2.17e-62 | |||||
IPT domain of the transcription factor NFkappaB and related transcription factors. NFkappaB is considered a central regulator of stress responses, activated by different stressful conditions, including physical stress, oxidative stress, and exposure to certain chemicals. NFkappaB blocking cell apoptosis in several cell types, gives it an important role in cell proliferation and differentiation. Pssm-ID: 238582 Cd Length: 102 Bit Score: 206.02 E-value: 2.17e-62
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| RHD-n | cd07827 | N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology ... |
43-244 | 1.72e-59 | |||||
N-terminal sub-domain of the Rel homology domain (RHD); Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal sub-domain, which may be distantly related to the DNA-binding domain found in P53. The C-terminal sub-domain has an immunoglobulin-like fold and serves as a dimerization module that also binds DNA (see cd00102). The RHD is found in NF-kappa B, nuclear factor of activated T-cells (NFAT), the tonicity-responsive enhancer binding protein (TonEBP), and the arthropod proteins Dorsal and Relish (Rel). Pssm-ID: 143640 Cd Length: 174 Bit Score: 201.06 E-value: 1.72e-59
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| RHD_dimer | pfam16179 | Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural ... |
252-353 | 7.56e-57 | |||||
Rel homology dimerization domain; The Rel homology domain (RHD) is composed of two structural domains, an N-terminal DNA_binding domain (pfam00554) and a C-terminal dimerization domain. This is the dimerization domain. Pssm-ID: 465045 Cd Length: 102 Bit Score: 190.85 E-value: 7.56e-57
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| RHD-n_c-Rel | cd07933 | N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel ... |
43-244 | 1.52e-48 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of c-Rel; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the c-Rel family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). c-Rel plays an important role in B cell proliferation and survival. Pssm-ID: 143649 Cd Length: 172 Bit Score: 170.06 E-value: 1.52e-48
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| RHD-n_Dorsal_Dif | cd07887 | N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; ... |
43-244 | 2.72e-45 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Dorsal; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Dorsal and Dif (Dorsal-related immunity factor), and similar proteins. Dorsal and Dif are Rel-like transcription factors, which play roles in mediating innate immunity in Drosophila. They are activated via the Toll pathway. Cytoplasmic Dorsal/Dif are inactivated via forming a complex with Cactus, the Drosophila homologue of mammalian I-kappa B proteins. In response to signals, Cactus is degraded and Dorsal/Dif can be transported into the nucleus, where they act as transcription factors. Dorsal is also an essential gene in establishing the proper dorsal/ventral polarity in the developing embryo. Pssm-ID: 143647 Cd Length: 173 Bit Score: 160.73 E-value: 2.72e-45
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| IPT_TF | cd00602 | IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated ... |
251-352 | 3.81e-45 | |||||
IPT domain of eukaryotic transcription factors NF-kappaB/Rel, nuclear factor of activated Tcells (NFAT), and recombination signal J-kappa binding protein (RBP-Jkappa). The IPT domains in these proteins are involved in DNA binding. Most NF-kappaB/Rel proteins form homo- and heterodimers, while NFAT proteins are largely monomeric (with TonEBP being an exception). While the majority of sequence-specific DNA binding elements are found in the N-terminal domain, several are found in the IPT domain in loops adjacent to, and including, the linker region. Pssm-ID: 238336 Cd Length: 101 Bit Score: 157.44 E-value: 3.81e-45
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| Death_NFkB1_p105 | cd08797 | Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ... |
816-891 | 2.89e-44 | |||||
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the Nuclear Factor-KappaB1 (NF-kB1) precursor protein p105. 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). NF-kB1 (or p50) is produced from the processing of the precursor protein p105, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the classical (or canonical) NF-kB pathway. In the cytosol, p50 forms an inactive complex with RelA (or p65) and the Inhibitor of NF-kB (IkB). Activation is triggered by the phosphorylation and degradation of IkB, resulting in the active DNA-binding p50-RelA dimer to migrate to the nucleus. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. 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: 260063 Cd Length: 76 Bit Score: 154.29 E-value: 2.89e-44
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| RHD-n_Relish | cd07884 | N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; ... |
43-244 | 2.31e-36 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of the arthropod protein Relish; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the arthropod Relish protein, in which the RHD domain co-occurs with C-terminal ankyrin repeats. Family members are sometimes referred to as p110 or p68 (proteolytically processed form). Relish is an NF-kappa B-like transcription factor, which plays a role in mediating innate immunity in Drosophila. It is activated via the Imd (immune deficiency) pathway, which triggers phosphorylation of Relish. IKK-dependent proteolytic cleavage of Relish (which involves Dredd) results in a smaller active form (without the C-terminal ankyrin repeats), which is transported into the nucleus and functions as a transactivator. Pssm-ID: 143644 Cd Length: 159 Bit Score: 134.87 E-value: 2.31e-36
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| RHD-n_RelA | cd07885 | N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel ... |
43-244 | 6.49e-36 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of RelA; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD domain of the RelA family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). RelA (also called p65) forms heterodimers with NF-kappa B1 (p50) and B2 (p52). RelA also forms homodimers. Pssm-ID: 143645 Cd Length: 169 Bit Score: 133.84 E-value: 6.49e-36
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
499-759 | 1.49e-34 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.93 E-value: 1.49e-34
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| RHD-n_RelB | cd07886 | N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral ... |
43-244 | 1.69e-33 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of the reticuloendotheliosis viral oncogene homolog B (RelB) protein; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the RelB family of transcription factors, categorized as class II NF-kappa B family members. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD). NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel). RelB, is unable to homodimerize but is a potent transactivator in a heterodimer with NF-kappa B1 (p50) or B2 (p52). It is involved in the regulation of genes that play roles in inflammatory processes and the immune response. Pssm-ID: 143646 Cd Length: 172 Bit Score: 126.90 E-value: 1.69e-33
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
499-745 | 1.02e-32 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 128.53 E-value: 1.02e-32
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| Death_NFkB-like | cd08310 | Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ... |
816-890 | 1.12e-25 | |||||
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: 100.78 E-value: 1.12e-25
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
516-722 | 3.65e-24 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 103.88 E-value: 3.65e-24
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
587-681 | 3.27e-17 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.46 E-value: 3.27e-17
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| IPT | smart00429 | ig-like, plexins, transcription factors; |
250-351 | 1.29e-13 | |||||
ig-like, plexins, transcription factors; Pssm-ID: 214657 [Multi-domain] Cd Length: 90 Bit Score: 67.06 E-value: 1.29e-13
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
576-727 | 4.07e-13 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 4.07e-13
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| DEATH | smart00005 | DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ... |
814-892 | 2.55e-12 | |||||
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: 63.58 E-value: 2.55e-12
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| IPT | cd00102 | Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ... |
251-352 | 1.85e-11 | |||||
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers. Pssm-ID: 238050 [Multi-domain] Cd Length: 89 Bit Score: 60.94 E-value: 1.85e-11
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| Death | pfam00531 | Death domain; |
817-893 | 2.15e-11 | |||||
Death domain; Pssm-ID: 459845 [Multi-domain] Cd Length: 86 Bit Score: 60.84 E-value: 2.15e-11
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| Death_NFkB2_p100 | cd08798 | Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ... |
820-889 | 2.36e-11 | |||||
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the Nuclear Factor-KappaB2 (NF-kB2) precursor protein p100. 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). NF-kB2 (or p52) is produced from the processing of the precursor protein p100, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the non-canonical NF-kB pathway. The p100 precursor is cytosolic and interacts with RelB. Upon phosphorylation by IKKalpha, p100 is processed to its 52kDa active, DNA-binding form and the p52/RelB complex is translocated into the nucleus. The non-canonical pathway plays a role in adaptive immunity and lymphorganogenesis. 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: 176776 Cd Length: 76 Bit Score: 60.22 E-value: 2.36e-11
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
576-728 | 2.45e-11 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.00 E-value: 2.45e-11
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
576-726 | 4.54e-11 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 66.20 E-value: 4.54e-11
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
544-733 | 1.68e-10 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 64.65 E-value: 1.68e-10
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
656-732 | 3.67e-10 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.43 E-value: 3.67e-10
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
539-724 | 5.57e-10 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 62.73 E-value: 5.57e-10
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
545-709 | 1.22e-09 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.55 E-value: 1.22e-09
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
584-724 | 1.59e-09 | |||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.81 E-value: 1.59e-09
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
548-638 | 3.67e-09 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 54.74 E-value: 3.67e-09
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
513-734 | 4.25e-09 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.04 E-value: 4.25e-09
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
539-653 | 5.62e-09 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 58.43 E-value: 5.62e-09
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
543-727 | 6.82e-09 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 59.21 E-value: 6.82e-09
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| PHA02736 | PHA02736 | Viral ankyrin protein; Provisional |
613-734 | 2.53e-08 | |||||
Viral ankyrin protein; Provisional Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 54.11 E-value: 2.53e-08
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
652-706 | 2.53e-08 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 2.53e-08
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
512-727 | 2.65e-08 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 57.77 E-value: 2.65e-08
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
539-613 | 3.05e-08 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.04 E-value: 3.05e-08
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
596-733 | 4.39e-08 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 55.73 E-value: 4.39e-08
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
564-731 | 3.05e-07 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.81 E-value: 3.05e-07
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
616-672 | 3.69e-06 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 3.69e-06
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
585-636 | 5.10e-06 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 5.10e-06
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
570-671 | 5.67e-06 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 50.05 E-value: 5.67e-06
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| Death_UNC5-like | cd08781 | Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ... |
816-890 | 5.86e-06 | |||||
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: 45.34 E-value: 5.86e-06
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
576-680 | 7.55e-06 | |||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.08 E-value: 7.55e-06
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
584-638 | 1.75e-05 | |||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 1.75e-05
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| PHA02741 | PHA02741 | hypothetical protein; Provisional |
616-727 | 3.09e-05 | |||||
hypothetical protein; Provisional Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 45.42 E-value: 3.09e-05
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| PHA02743 | PHA02743 | Viral ankyrin protein; Provisional |
646-727 | 3.29e-05 | |||||
Viral ankyrin protein; Provisional Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 45.19 E-value: 3.29e-05
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
690-733 | 3.58e-05 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 43.18 E-value: 3.58e-05
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
586-727 | 4.55e-05 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 47.18 E-value: 4.55e-05
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
526-614 | 4.66e-05 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.97 E-value: 4.66e-05
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
544-659 | 5.27e-05 | |||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.00 E-value: 5.27e-05
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
517-679 | 7.19e-05 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.52 E-value: 7.19e-05
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
686-734 | 1.14e-04 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.14e-04
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| TRPV | cd21882 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
544-621 | 1.19e-04 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic). Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 46.03 E-value: 1.19e-04
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
513-637 | 1.26e-04 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 45.79 E-value: 1.26e-04
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
555-731 | 1.55e-04 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 45.44 E-value: 1.55e-04
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
585-733 | 1.80e-04 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.98 E-value: 1.80e-04
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| RHD-n_NFAT_like | cd07927 | N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells ... |
43-117 | 2.30e-04 | |||||
N-terminal sub-domain of the Rel homology domain (RHD) of nuclear factor of activated T-cells (NFAT) proteins and similar proteins; Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains; this model characterizes the N-terminal RHD sub-domain of the NFAT family of transcription factors. NFAT transcription complexes are a target of calcineurin, a calcium dependent phosphatase, and activate genes that are mainly involved in cell-cell interaction. Upon de-phosphorylation of the nuclear localization signal, NFAT enters the nucleus and acts as a transcription factor; its export from the nucleus is triggered by phosphorylation via export kinases. NFATs play important roles in mediating the immune response, and are found in T cells, B Cells, NK cells, mast cells, and monocytes. NFATs are also found in various non-hematopoietic cell types, where they play roles in development. This group also contains the N-terminal RHD sub-domain of the non-calcium regulated tonicity-responsive enhancer binding protein (TonEBP), also called NFAT5. Mammalian TonEBP regulates the expression of genes in response to tonicity. It plays a pivotal role in urinary concentrating mechanisms in kidney medulla, by triggering the accumulation of osmolytes that enable renal medullary cells to tolerate high levels of urea and salt. Pssm-ID: 143648 Cd Length: 161 Bit Score: 42.65 E-value: 2.30e-04
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| Death_DAPK1 | cd08782 | Death domain found in death-associated protein kinase 1; Death domain (DD) found in ... |
816-889 | 2.79e-04 | |||||
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: 40.40 E-value: 2.79e-04
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| TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
544-659 | 4.03e-04 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 44.36 E-value: 4.03e-04
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
544-603 | 6.00e-04 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 6.00e-04
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
671-727 | 7.60e-04 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 7.60e-04
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| TRPV | cd21882 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
616-726 | 9.47e-04 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic). Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 42.94 E-value: 9.47e-04
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
519-625 | 9.78e-04 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 42.64 E-value: 9.78e-04
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
584-614 | 2.51e-03 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 2.51e-03
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
576-623 | 2.53e-03 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 2.53e-03
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| TRPV2 | cd22197 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
544-621 | 3.52e-03 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 40.99 E-value: 3.52e-03
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
541-680 | 3.90e-03 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.20 E-value: 3.90e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
585-609 | 4.64e-03 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 4.64e-03
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
585-726 | 4.80e-03 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 40.77 E-value: 4.80e-03
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
658-728 | 5.70e-03 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 40.38 E-value: 5.70e-03
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