Chain A, Tumor necrosis factor alpha-induced protein 3
OTU family ubiquitin thioesterase( domain architecture ID 17785040)
OTU family ubiquitin thioesterase catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
OTU_TNFAIP3 | cd22766 | OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis ... |
41-261 | 8.83e-146 | ||||
OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3) is also called OTU domain-containing protein 7C (OTUD7C), DNA-binding protein A20, or zinc finger protein A20. It is a ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). It can also inhibit IKK through a non-catalytic mechanism which involves polyubiquitin. In vitro, TNFAIP3 is able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. TNFAIP3 contains several A20-type zinc fingers that mediate the ubiquitin ligase activity and an OTU (ovarian tumor) domain that contains the DUB activity. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS. : Pssm-ID: 438603 Cd Length: 220 Bit Score: 411.27 E-value: 8.83e-146
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Name | Accession | Description | Interval | E-value | ||||
OTU_TNFAIP3 | cd22766 | OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis ... |
41-261 | 8.83e-146 | ||||
OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3) is also called OTU domain-containing protein 7C (OTUD7C), DNA-binding protein A20, or zinc finger protein A20. It is a ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). It can also inhibit IKK through a non-catalytic mechanism which involves polyubiquitin. In vitro, TNFAIP3 is able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. TNFAIP3 contains several A20-type zinc fingers that mediate the ubiquitin ligase activity and an OTU (ovarian tumor) domain that contains the DUB activity. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS. Pssm-ID: 438603 Cd Length: 220 Bit Score: 411.27 E-value: 8.83e-146
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OTU | pfam02338 | OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ... |
98-257 | 1.18e-32 | ||||
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases. Pssm-ID: 426728 [Multi-domain] Cd Length: 127 Bit Score: 118.71 E-value: 1.18e-32
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Name | Accession | Description | Interval | E-value | ||||
OTU_TNFAIP3 | cd22766 | OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis ... |
41-261 | 8.83e-146 | ||||
OTU (ovarian tumor) domain of tumor necrosis factor alpha induced protein 3; Tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3) is also called OTU domain-containing protein 7C (OTUD7C), DNA-binding protein A20, or zinc finger protein A20. It is a ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). It can also inhibit IKK through a non-catalytic mechanism which involves polyubiquitin. In vitro, TNFAIP3 is able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. TNFAIP3 contains several A20-type zinc fingers that mediate the ubiquitin ligase activity and an OTU (ovarian tumor) domain that contains the DUB activity. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS. Pssm-ID: 438603 Cd Length: 220 Bit Score: 411.27 E-value: 8.83e-146
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OTU_C64 | cd22750 | OTU (ovarian tumor) domain of family C64 cysteine proteases; This group includes proteins ... |
71-261 | 1.78e-84 | ||||
OTU (ovarian tumor) domain of family C64 cysteine proteases; This group includes proteins classified as family C64 cysteine protease by MEROPS, such as tumor necrosis factor (TNF) alpha-induced protein 3 (TNFAIP3), ZRANB1, OTU domain-containing protein 7A (OTUD7A), and OTUD7B. It also includes VCIP135. These proteins are deubiquitinases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12) that mediates the deubiquitination of protein substrates. TNFAIP3 also contains ubiquitin ligase activity. It antagonizes IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). ZRANB1 binds, deubiquitinates, and stabilizes EZH2, which is the catalytic component of the Polycomb repressive complex 2 (PRC2) that silences gene transcription by methylating histone H3 at lysine 27 and is mutated or highly expressed in many types of cancer, including lymphoma, melanoma, prostate cancer, ovarian cancer, and breast cancer. OTUD7A has been identified as a critical gene for brain function, while OTUD7B functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. This group belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. Pssm-ID: 438587 Cd Length: 185 Bit Score: 254.19 E-value: 1.78e-84
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OTU_OTUD7 | cd22768 | OTU (ovarian tumor) domain of OTU domain-containing proteins 7A, 7B, and similar proteins; ... |
76-261 | 1.19e-65 | ||||
OTU (ovarian tumor) domain of OTU domain-containing proteins 7A, 7B, and similar proteins; This subfamily consists of OTU domain-containing protein 7A (OTUD7A), OTUD7B, and similar proteins. OTUD7A and OTUD7B are deubiquitinases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12) that specifically target Lys11-linked polyubiquitin. OTUD7A, also called zinc finger protein Cezanne 2, has been identified as a critical gene for brain function. It localizes to dendritic and spine compartments in cortical neurons, and its reduced levels contributed to dendritic spine and dendrite outgrowth deficits. OTUD7B, also called zinc finger protein Cezanne, functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. OTUD7 proteins belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. They are classified as family C64 cysteine proteases by MEROPS. Pssm-ID: 438605 Cd Length: 208 Bit Score: 206.77 E-value: 1.19e-65
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OTU_OTUD7B | cd22772 | OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein ... |
77-262 | 1.18e-56 | ||||
OTU (ovarian tumor) domain of OTU domain-containing protein 7B; OTU domain-containing protein 7B (OTUD7B) is also called cellular zinc finger anti-NF-kappa-B protein, zinc finger A20 domain-containing protein 1, or zinc finger protein Cezanne. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically targets Lys11-linked polyubiquitin. It functions as a negative regulator of the non-canonical NF-kappaB pathway by mediating the deubiquitination of TRAF3, an inhibitor of the NF-kappaB pathway, resulting in preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappaB. OTUD7B also deubiquitinates ZAP70, and thus, regulates T cell receptor (TCR) signaling. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS. Pssm-ID: 438609 Cd Length: 207 Bit Score: 183.70 E-value: 1.18e-56
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OTU_OTUD7A | cd22773 | OTU (ovarian tumor) domain of OTU domain-containing protein 7A; OTU domain-containing protein ... |
77-262 | 1.60e-51 | ||||
OTU (ovarian tumor) domain of OTU domain-containing protein 7A; OTU domain-containing protein 7A (OTUD7A), also called zinc finger protein Cezanne 2, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically targets Lys11-linked polyubiquitin. OTUD7A has been identified as a critical gene for brain function. It localizes to dendritic and spine compartments in cortical neurons, and its reduced levels contributed to dendritic spine and dendrite outgrowth deficits. A homozygous OTUD7A missense variant located within the OTU catalytic domain is linked to early-onset epileptic encephalopathy and proteasome dysfunction. OTUD7A belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C64 cysteine protease by MEROPS. Pssm-ID: 438610 Cd Length: 207 Bit Score: 170.63 E-value: 1.60e-51
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OTU_ZRANB1 | cd22767 | OTU (ovarian tumor) domain of Ubiquitin thioesterase ZRANB1 and similar proteins; ZRANB1 is ... |
71-261 | 4.00e-40 | ||||
OTU (ovarian tumor) domain of Ubiquitin thioesterase ZRANB1 and similar proteins; ZRANB1 is also called TRAF-binding domain-containing protein, Trabid, or zinc finger Ran-binding domain-containing protein 1. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin; it also cleaves 'Lys-63'-linked chains with less efficiency. ZRANB1 binds, deubiquitinates, and stabilizes EZH2, which is the catalytic component of the Polycomb repressive complex 2 (PRC2) that silences gene transcription by methylating histone H3 at lysine 27 and is mutated or highly expressed in many types of cancer, including lymphoma, melanoma, prostate cancer, ovarian cancer, and breast cancer. Drosophila Trabid interacts with TGF-beta Activating Kinase 1 (TAK1), which triggers both immunity and apoptosis, resulting in reduced immune signaling output and K63-linked ubiquitination. ZRANB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. ZRANB1 does not contain the conserved aspartate, and uses cysteine and histidine as a catalytic dyad. It is classified as a family C64 cysteine protease by MEROPS. Pssm-ID: 438604 Cd Length: 185 Bit Score: 140.13 E-value: 4.00e-40
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OTU | pfam02338 | OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ... |
98-257 | 1.18e-32 | ||||
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases. Pssm-ID: 426728 [Multi-domain] Cd Length: 127 Bit Score: 118.71 E-value: 1.18e-32
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OTU_VCIP135 | cd22769 | OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein ... |
73-261 | 1.11e-14 | ||||
OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein VCIP135 is also called valosin-containing protein p97/p47 complex-interacting protein 1, valosin-containing protein p97/p47 complex-interacting protein p135, or VCP/p47 complex-interacting 135-kDa protein. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. It is necessary for VCP-mediated reassembly of Golgi stacks after mitosis, and may play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. It belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. Not all members of this subfamily contain the active site. It is closely related to proteins classified as family C64 cysteine protease by MEROPS, such as TNFAIP3, ZRANB1, and OTUD7A/B. Pssm-ID: 438606 Cd Length: 197 Bit Score: 71.94 E-value: 1.11e-14
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OTU | cd22744 | OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ... |
99-260 | 1.87e-06 | ||||
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. Pssm-ID: 438581 [Multi-domain] Cd Length: 128 Bit Score: 46.66 E-value: 1.87e-06
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Blast search parameters | ||||
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