ubiquitin carboxyl-terminal hydrolase 25 isoform X6 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| USP25_C | cd20486 | carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ... |
434-714 | 0e+00 | |||||
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: 541.35 E-value: 0e+00
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| Peptidase_C19 super family | cl02553 | Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
163-251 | 4.02e-40 | |||||
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. The actual alignment was detected with superfamily member cd02665: Pssm-ID: 470612 [Multi-domain] Cd Length: 228 Bit Score: 147.32 E-value: 4.02e-40
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| Name | Accession | Description | Interval | E-value | |||||
| USP25_C | cd20486 | carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ... |
434-714 | 0e+00 | |||||
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: 541.35 E-value: 0e+00
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| Peptidase_C19I | cd02665 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-251 | 4.02e-40 | |||||
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: 147.32 E-value: 4.02e-40
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| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
187-250 | 2.78e-12 | |||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 68.24 E-value: 2.78e-12
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| COG5077 | COG5077 | Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
187-303 | 1.75e-10 | |||||
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 64.51 E-value: 1.75e-10
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| Name | Accession | Description | Interval | E-value | |||||
| USP25_C | cd20486 | carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25); This subfamily contains ... |
434-714 | 0e+00 | |||||
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: 541.35 E-value: 0e+00
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| USP25_USP28_C-like | cd20485 | carboxyl-terminal domain of ubiquitin-specific protease 25 (USP25) and 28 (USP28), and similar ... |
445-714 | 8.52e-111 | |||||
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: 336.57 E-value: 8.52e-111
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| USP28_C | cd20487 | carboxyl-terminal domain of ubiquitin-specific protease 28 (USP28); This family contains the ... |
445-716 | 2.96e-109 | |||||
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: 332.96 E-value: 2.96e-109
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| Peptidase_C19I | cd02665 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
163-251 | 4.02e-40 | |||||
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: 147.32 E-value: 4.02e-40
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| Peptidase_C19 | cd02257 | Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
174-251 | 7.31e-19 | |||||
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: 86.77 E-value: 7.31e-19
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| Peptidase_C19J | cd02666 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
148-251 | 4.33e-15 | |||||
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: 77.15 E-value: 4.33e-15
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| peptidase_C19C | cd02659 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
187-252 | 1.11e-14 | |||||
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: 75.76 E-value: 1.11e-14
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| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
187-250 | 2.78e-12 | |||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 68.24 E-value: 2.78e-12
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| COG5077 | COG5077 | Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
187-303 | 1.75e-10 | |||||
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 64.51 E-value: 1.75e-10
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| Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
187-251 | 8.40e-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: 56.53 E-value: 8.40e-09
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| Peptidase_C19D | cd02660 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
187-251 | 1.89e-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: 53.53 E-value: 1.89e-07
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| COG5533 | COG5533 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
187-231 | 2.59e-06 | |||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 49.80 E-value: 2.59e-06
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| Peptidase_C19A | cd02657 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
187-250 | 7.04e-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 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: 7.04e-06
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| Peptidase_C19H | cd02664 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
161-250 | 7.01e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 45.56 E-value: 7.01e-05
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| Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
178-251 | 9.66e-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: 44.96 E-value: 9.66e-05
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| Peptidase_C19L | cd02668 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
187-226 | 2.25e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 43.95 E-value: 2.25e-04
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| UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
174-251 | 4.90e-04 | |||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 43.72 E-value: 4.90e-04
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| Peptidase_C19K | cd02667 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
187-250 | 5.37e-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: 39.29 E-value: 5.37e-03
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