ubiquitin carboxyl-terminal hydrolase 25 isoform X1 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| Peptidase_C19I | cd02665 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-655 | 5.86e-105 | ||||||||
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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 325.28 E-value: 5.86e-105
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| USP25_USP28_C-like super family | cl40424 | carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ... |
838-935 | 4.11e-57 | ||||||||
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar domains; This family contains the C-terminal domain of two deubiquitinases (DUBs), ubiquitin-specific proteases USP25 and USP28, which share high similarity but vary in their cellular functions. USP25 is a regulator of the innate immune system and may play a role in tumorigenesis, while USP28 is known for its tumor-promoting role. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This alignment model represents the C-terminal region that has been implicated in substrate binding for both USP25 and USP28 and harbors the splicing site for isoform-specific sequences. The actual alignment was detected with superfamily member cd20486: Pssm-ID: 394794 Cd Length: 281 Bit Score: 198.13 E-value: 4.11e-57
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| UBA_UBP25 | cd14354 | UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; ... |
15-60 | 4.36e-24 | ||||||||
UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels. : Pssm-ID: 270539 Cd Length: 46 Bit Score: 95.55 E-value: 4.36e-24
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| Name | Accession | Description | Interval | E-value | ||||||||
| Peptidase_C19I | cd02665 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-655 | 5.86e-105 | ||||||||
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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 325.28 E-value: 5.86e-105
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| USP25_C | cd20486 | carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ... |
838-935 | 4.11e-57 | ||||||||
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains the C-terminal domain of ubiquitin-specific protease USP25, a deubiquitinase (DUB), which shares high similarity with USP28 but varies in cellular function; USP25 is a regulator of the innate immune system and may play a role in tumorigenesis, while USP28 is known for its tumor-promoting role. USP25 regulates inflammatory TRAF signaling and USP28 stabilizes c-MYC and other nuclear proteins. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This C-terminal region has been implicated in substrate binding for USP25 and harbors the splicing site for isoform-specific sequences. Structure studies show that the C-terminally extended USP25 is exclusively tetrameric. Pssm-ID: 380451 Cd Length: 281 Bit Score: 198.13 E-value: 4.11e-57
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| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
169-425 | 8.94e-31 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 123.71 E-value: 8.94e-31
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| UBA_UBP25 | cd14354 | UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; ... |
15-60 | 4.36e-24 | ||||||||
UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels. Pssm-ID: 270539 Cd Length: 46 Bit Score: 95.55 E-value: 4.36e-24
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| COG5077 | COG5077 | Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
148-407 | 6.77e-13 | ||||||||
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 72.98 E-value: 6.77e-13
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| Name | Accession | Description | Interval | E-value | ||||||||
| Peptidase_C19I | cd02665 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-655 | 5.86e-105 | ||||||||
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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 325.28 E-value: 5.86e-105
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| USP25_C | cd20486 | carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ... |
838-935 | 4.11e-57 | ||||||||
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains the C-terminal domain of ubiquitin-specific protease USP25, a deubiquitinase (DUB), which shares high similarity with USP28 but varies in cellular function; USP25 is a regulator of the innate immune system and may play a role in tumorigenesis, while USP28 is known for its tumor-promoting role. USP25 regulates inflammatory TRAF signaling and USP28 stabilizes c-MYC and other nuclear proteins. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This C-terminal region has been implicated in substrate binding for USP25 and harbors the splicing site for isoform-specific sequences. Structure studies show that the C-terminally extended USP25 is exclusively tetrameric. Pssm-ID: 380451 Cd Length: 281 Bit Score: 198.13 E-value: 4.11e-57
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| USP28_C | cd20487 | carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ... |
849-934 | 1.21e-33 | ||||||||
carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the C-terminal domain of ubiquitin-specific protease USP28, a deubiquitinase (DUB), which shares high similarity with USP25 but varies in cellular function; USP28 is known for its tumor-promoting role while USP25 is a regulator of the innate immune system and may play a role in tumorigenesis. USP28 stabilizes c-MYC and other nuclear proteins, and USP25 regulates inflammatory TRAF signaling. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This C-terminal region has been implicated in substrate binding for USP28 and harbors the splicing site for isoform-specific sequences. Structure studies suggest that the C-terminal domain forms an independent entity. Pssm-ID: 380452 Cd Length: 280 Bit Score: 131.12 E-value: 1.21e-33
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| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
169-425 | 8.94e-31 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 123.71 E-value: 8.94e-31
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| Peptidase_C19 | cd02257 | Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
170-655 | 1.76e-30 | ||||||||
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: 121.05 E-value: 1.76e-30
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| Peptidase_C19L | cd02668 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-410 | 2.00e-26 | ||||||||
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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 111.36 E-value: 2.00e-26
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| UBA_UBP25 | cd14354 | UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; ... |
15-60 | 4.36e-24 | ||||||||
UBA domain found in ubiquitin carboxyl-terminal hydrolase 25 (UBP25) and similar proteins; UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels. Pssm-ID: 270539 Cd Length: 46 Bit Score: 95.55 E-value: 4.36e-24
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| peptidase_C19C | cd02659 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
169-656 | 1.29e-23 | ||||||||
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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 103.11 E-value: 1.29e-23
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| USP25_USP28_C-like | cd20485 | carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ... |
849-935 | 3.62e-21 | ||||||||
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar domains; This family contains the C-terminal domain of two deubiquitinases (DUBs), ubiquitin-specific proteases USP25 and USP28, which share high similarity but vary in their cellular functions. USP25 is a regulator of the innate immune system and may play a role in tumorigenesis, while USP28 is known for its tumor-promoting role. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This alignment model represents the C-terminal region that has been implicated in substrate binding for both USP25 and USP28 and harbors the splicing site for isoform-specific sequences. Pssm-ID: 380450 Cd Length: 273 Bit Score: 94.28 E-value: 3.62e-21
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| Peptidase_C19J | cd02666 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
168-655 | 7.16e-20 | ||||||||
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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 92.17 E-value: 7.16e-20
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| UBA_UBP25_like | cd14276 | UBA domain found in ubiquitin carboxyl-terminal hydrolase UBP25, UBP28, and similar proteins; ... |
19-56 | 2.08e-14 | ||||||||
UBA domain found in ubiquitin carboxyl-terminal hydrolase UBP25, UBP28, and similar proteins; UBP25, also called deubiquitinating enzyme 25, USP on chromosome 21, ubiquitin thioesterase 25, or ubiquitin-specific-processing protease 25, belongs to the deubiquitinating enzyme (DUB) family that specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. USP25 has one muscular isoform and two ubiquitous isoforms. The longer muscular isoform can bind to muscle-restricted cytoskeletal and sarcomeric proteins, such as myosin binding protein C1 (MyBPC1), actin alpha-1 (ACTA1) and filamin C (FLNC), and further prevent their degradation. USP25 harbors three potential ubiquitin-binding domains (UBDs), one ubiquitin-associated (UBA) domain and two ubiquitin-interacting motifs (UIMs) in the N-terminal region. Its C-terminal tyrosine-rich region is responsible for the binding of the second SH2 domain of SYK, a non-receptor tyrosine kinase that specifically phosphorylates USP25 and alters its cellular levels. UBP28, also called deubiquitinating enzyme 28, ubiquitin thioesterase 28, or ubiquitin-specific-processing protease 28, is also an ubiquitin-specific protease belonging to the DUB family. UBP28 can form a ternary complex with nucleoplasmic Fbw7alpha, an F-box protein that is part of an SCF-type ubiquitin ligase, and MYC, a transcription factor encoded by MYC proto-oncogene. UBP28 is required for the stability of MYC, and this stabilization is necessary for tumour-cell proliferation. Besides, UBP28 plays a critical role in the regulation of the Chk2-p53-PUMA pathway. It specifically interacts with 53BP1 and is essential to stabilize Chk2 and 53BP1 in response to DNA damage. Pssm-ID: 270462 Cd Length: 38 Bit Score: 67.83 E-value: 2.08e-14
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| USP25_USP28_C-like | cd20485 | carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ... |
819-946 | 6.70e-14 | ||||||||
carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar domains; This family contains the C-terminal domain of two deubiquitinases (DUBs), ubiquitin-specific proteases USP25 and USP28, which share high similarity but vary in their cellular functions. USP25 is a regulator of the innate immune system and may play a role in tumorigenesis, while USP28 is known for its tumor-promoting role. These two closely related DUBs contain an N-terminal domain harboring a Ub-associated domain (UBA) and two Ub-interacting motifs (UIMs), a central catalytic USP domain, and a C-terminal region of unknown function and variable size due to alternative splicing. In general, USP catalytic domains are around 350 amino acids in length; however, in USP25 and 28, the catalytic domains span around 550 amino acids due to a large, conserved insertion at a common insertion point called USP25/28 catalytic domain inserted domain (UCID). This alignment model represents the C-terminal region that has been implicated in substrate binding for both USP25 and USP28 and harbors the splicing site for isoform-specific sequences. Pssm-ID: 380450 Cd Length: 273 Bit Score: 73.10 E-value: 6.70e-14
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| Peptidase_C19H | cd02664 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-401 | 1.96e-13 | ||||||||
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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 72.52 E-value: 1.96e-13
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| COG5077 | COG5077 | Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
148-407 | 6.77e-13 | ||||||||
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 72.98 E-value: 6.77e-13
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| Peptidase_C19A | cd02657 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-399 | 2.90e-11 | ||||||||
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 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: 239122 [Multi-domain] Cd Length: 305 Bit Score: 65.43 E-value: 2.90e-11
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| Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
168-405 | 3.12e-10 | ||||||||
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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 62.29 E-value: 3.12e-10
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| Peptidase_C19K | cd02667 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-422 | 3.53e-10 | ||||||||
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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 62.02 E-value: 3.53e-10
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| Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
591-655 | 9.28e-09 | ||||||||
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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 56.91 E-value: 9.28e-09
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| UBA_UBP28 | cd14355 | UBA domain found in ubiquitin carboxyl-terminal hydrolase 28 (UBP28) and similar proteins; ... |
21-60 | 1.85e-08 | ||||||||
UBA domain found in ubiquitin carboxyl-terminal hydrolase 28 (UBP28) and similar proteins; UBP28, also called deubiquitinating enzyme 28, ubiquitin thioesterase 28, or ubiquitin-specific-processing protease 28, is an ubiquitin-specific protease that belongs to the deubiquitinating enzyme (DUB) family which specifically hydrolyzes ubiquitin chains on ubiquitin-conjugated proteins. UBP28 can form a ternary complex with nucleoplasmic Fbw7alpha, an F-box protein that is part of an SCF-type ubiquitin ligase, and MYC, a transcription factor encoded by MYC proto-oncogene. UBP28 is required for the stability of MYC, and this stabilization is necessary for tumour-cell proliferation. Besides, UBP28 plays a critical role in the regulation of the Chk2-p53-PUMA pathway. It specifically interacts with 53BP1 and is essential to stabilize Chk2 and 53BP1 in response to DNA damage. Pssm-ID: 270540 Cd Length: 42 Bit Score: 51.01 E-value: 1.85e-08
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| COG5533 | COG5533 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
170-394 | 2.64e-08 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 56.35 E-value: 2.64e-08
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| Peptidase_C19D | cd02660 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
591-655 | 1.70e-07 | ||||||||
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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 54.30 E-value: 1.70e-07
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| Peptidase_C19B | cd02658 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-399 | 4.67e-07 | ||||||||
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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 52.71 E-value: 4.67e-07
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| Peptidase_C19D | cd02660 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-402 | 2.78e-06 | ||||||||
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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 50.45 E-value: 2.78e-06
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| Peptidase_C19G | cd02663 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-401 | 3.74e-06 | ||||||||
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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 50.00 E-value: 3.74e-06
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| COG5533 | COG5533 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
591-635 | 5.35e-06 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 49.42 E-value: 5.35e-06
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| Peptidase_C19A | cd02657 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
591-654 | 1.11e-05 | ||||||||
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 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: 239122 [Multi-domain] Cd Length: 305 Bit Score: 48.48 E-value: 1.11e-05
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| Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
582-655 | 8.01e-05 | ||||||||
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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 45.73 E-value: 8.01e-05
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| Peptidase_C19F | cd02662 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
259-400 | 3.00e-04 | ||||||||
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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 43.51 E-value: 3.00e-04
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| UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
578-655 | 5.00e-04 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 44.10 E-value: 5.00e-04
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| Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
170-396 | 1.50e-03 | ||||||||
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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 41.12 E-value: 1.50e-03
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| Peptidase_C19K | cd02667 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
591-654 | 5.07e-03 | ||||||||
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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 40.06 E-value: 5.07e-03
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| UBA_like_SF | cd00194 | UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ... |
24-52 | 6.73e-03 | ||||||||
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains. Pssm-ID: 270455 Cd Length: 28 Bit Score: 35.08 E-value: 6.73e-03
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