ubiquitin carboxyl-terminal hydrolase CYLD isoform 3 [Homo sapiens]
Protein Classification
CAP-Gly domain-containing protein; TBCE family protein( domain architecture ID 11279563)
CAP (cytoskeleton-associated protein)-Gly domain-containing protein similar to Schizosaccharomyces pombe Tip elongation protein 1 that has a role in stabilizing and targeting the growing tips of the microtubules along the long axis of the cell, directing them to the ends of the cell| TBCE (tubulin-specific chaperone E) family protein similar to Homo sapiens tubulin-specific chaperone E, a tubulin-folding protein involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| CYLD_phos_site | pfam16607 | Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ... |
304-450 | 2.09e-101 | ||||||
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, pfam01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyzes both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction. : Pssm-ID: 465194 Cd Length: 157 Bit Score: 313.04 E-value: 2.09e-101
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| Peptidase_C19N | cd02670 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
580-935 | 8.72e-78 | ||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. : Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 253.60 E-value: 8.72e-78
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| CAP_GLY | smart01052 | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
459-527 | 6.68e-21 | ||||||
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. : Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 87.26 E-value: 6.68e-21
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| CAP_GLY | smart01052 | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
127-203 | 1.05e-17 | ||||||
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. : Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 78.01 E-value: 1.05e-17
|
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| CAP_GLY | smart01052 | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
232-302 | 4.01e-11 | ||||||
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. : Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 59.52 E-value: 4.01e-11
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| Name | Accession | Description | Interval | E-value | ||||||
| CYLD_phos_site | pfam16607 | Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ... |
304-450 | 2.09e-101 | ||||||
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, pfam01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyzes both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction. Pssm-ID: 465194 Cd Length: 157 Bit Score: 313.04 E-value: 2.09e-101
|
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| Peptidase_C19N | cd02670 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
580-935 | 8.72e-78 | ||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 253.60 E-value: 8.72e-78
|
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| CAP_GLY | smart01052 | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
459-527 | 6.68e-21 | ||||||
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 87.26 E-value: 6.68e-21
|
||||||||||
| CAP_GLY | smart01052 | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
127-203 | 1.05e-17 | ||||||
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 78.01 E-value: 1.05e-17
|
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| CAP_GLY | pfam01302 | CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
465-526 | 7.29e-16 | ||||||
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 72.82 E-value: 7.29e-16
|
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| CAP_GLY | pfam01302 | CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
127-202 | 1.88e-12 | ||||||
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 62.81 E-value: 1.88e-12
|
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| CAP_GLY | smart01052 | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
232-302 | 4.01e-11 | ||||||
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 59.52 E-value: 4.01e-11
|
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| CAP_GLY | pfam01302 | CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
232-290 | 1.50e-06 | ||||||
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 46.24 E-value: 1.50e-06
|
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| NIP100 | COG5244 | Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
472-573 | 5.58e-04 | ||||||
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 43.91 E-value: 5.58e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| CYLD_phos_site | pfam16607 | Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ... |
304-450 | 2.09e-101 | ||||||
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, pfam01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyzes both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction. Pssm-ID: 465194 Cd Length: 157 Bit Score: 313.04 E-value: 2.09e-101
|
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| Peptidase_C19N | cd02670 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
580-935 | 8.72e-78 | ||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 253.60 E-value: 8.72e-78
|
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| Bbox1_CYLD | cd19816 | B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; ... |
772-828 | 1.79e-25 | ||||||
B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; CYLD, also termed ubiquitin carboxyl-terminal hydrolase CYLD, or deubiquitinating enzyme CYLD, or ubiquitin thioesterase CYLD, or ubiquitin-specific-processing protease CYLD, is a microtubule-associated deubiquitinase that specifically cleaves Lys-63-linked polyubiquitin chains. It plays a pivotal role in a wide range of cellular activities, including innate immunity, cell division, and ciliogenesis. CYLD antagonizes NF-kappaB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesized in response to cytokine stimulation. Structural characterization reveals a small zinc-binding B-box inserted within the ubiquitin specific protease (USP) domain of CYLD. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs) and is responsible for its intermolecular interaction and cytoplasmic localization. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. Pssm-ID: 380874 Cd Length: 56 Bit Score: 99.85 E-value: 1.79e-25
|
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| CAP_GLY | smart01052 | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
459-527 | 6.68e-21 | ||||||
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 87.26 E-value: 6.68e-21
|
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| CAP_GLY | smart01052 | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
127-203 | 1.05e-17 | ||||||
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 78.01 E-value: 1.05e-17
|
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| CAP_GLY | pfam01302 | CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
465-526 | 7.29e-16 | ||||||
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 72.82 E-value: 7.29e-16
|
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| CAP_GLY | pfam01302 | CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
127-202 | 1.88e-12 | ||||||
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 62.81 E-value: 1.88e-12
|
||||||||||
| CAP_GLY | smart01052 | Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
232-302 | 4.01e-11 | ||||||
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 59.52 E-value: 4.01e-11
|
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| Peptidase_C19 | cd02257 | Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
580-935 | 4.33e-11 | ||||||
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 64.43 E-value: 4.33e-11
|
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| CAP_GLY | pfam01302 | CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
232-290 | 1.50e-06 | ||||||
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 46.24 E-value: 1.50e-06
|
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| Bbox1_HOIP | cd19815 | B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, ... |
774-825 | 3.31e-04 | ||||||
B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, also termed RING finger protein 31 (RNF31), or zinc in-between-RING-finger ubiquitin-associated domain protein, together with HOIL-1 and SHARPIN, forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis. It also interacts with the atypical mammalian orphan receptor DAX-1, trigger DAX-1 ubiquitination and stabilization, and participate in repressing steroidogenic gene expression. HOIP contains a B-box motif that shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif. Pssm-ID: 380873 Cd Length: 43 Bit Score: 38.86 E-value: 3.31e-04
|
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| NIP100 | COG5244 | Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
472-573 | 5.58e-04 | ||||||
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 43.91 E-value: 5.58e-04
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