proteolysis 6 [Arabidopsis thaliana]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| PRT6_C | pfam18995 | Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. ... |
1522-1984 | 1.79e-98 | ||||||||
Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. Proteolysis 6 (PRT6) encodes a ubiquitin E3 ligase belonging to the N-end rule pathway of targeted protein degradation, which is a specialized subset of the ubiquitin proteasome system. In Arabidopsis, at least two N-recognins (E3 ubiquitin ligases) with different substrate specificities exist, namely PROTEOLYSIS1 (PRT1) and PRT6. : Pssm-ID: 465944 Cd Length: 444 Bit Score: 325.38 E-value: 1.79e-98
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| UBR-box_UBR3 | cd19673 | UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ... |
119-188 | 4.81e-40 | ||||||||
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1. : Pssm-ID: 439071 Cd Length: 72 Bit Score: 142.72 E-value: 4.81e-40
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| RING-H2_UBR1-like | cd16482 | RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 ... |
1388-1448 | 7.90e-21 | ||||||||
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar proteins; Two UBR family members, UBR1 and UBR2, are major N-recognin ubiquitin ligases that both function in the N-end rule degradation pathway. They can recognize substrate proteins with type-1 (basic) and type-2 (bulky hydrophobic) N-terminal residues as part of N-degrons and an internal lysine residue for ubiquitin conjugation. They also function in a quality control pathway for degradation of unfolded cytosolic proteins. Their action is stimulated by Hsp70. Moreover, UBR1 and UBR2 are negative regulators of the leucine-mTOR signaling pathway. Leucine might activate this pathway in part through inhibition of their ubiquitin ligase activity. In yeast, only one E3, encoded by UBR1, mediates the recognition of substrates by the N-end rule pathway. Saccharomyces cerevisiae UBR1 also functions as an additional E3 ligase in the endoplasmic reticulum-associated protein degradation (ERAD). It can provide ubiquitin ligation activity for the ERAD substrate mutated Ste6 (sterile). Schizosaccharomyces pombe UBR1 is a critical regulator that influences the oxidative stress response via degradation of active Pap1 basic leucine zipper (bZIP) transcription factor in the nucleus. Both UBR1 and UBR2 contain an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain. : Pssm-ID: 438145 Cd Length: 67 Bit Score: 87.78 E-value: 7.90e-21
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| Name | Accession | Description | Interval | E-value | ||||||||
| PRT6_C | pfam18995 | Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. ... |
1522-1984 | 1.79e-98 | ||||||||
Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. Proteolysis 6 (PRT6) encodes a ubiquitin E3 ligase belonging to the N-end rule pathway of targeted protein degradation, which is a specialized subset of the ubiquitin proteasome system. In Arabidopsis, at least two N-recognins (E3 ubiquitin ligases) with different substrate specificities exist, namely PROTEOLYSIS1 (PRT1) and PRT6. Pssm-ID: 465944 Cd Length: 444 Bit Score: 325.38 E-value: 1.79e-98
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| UBR-box_UBR3 | cd19673 | UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ... |
119-188 | 4.81e-40 | ||||||||
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1. Pssm-ID: 439071 Cd Length: 72 Bit Score: 142.72 E-value: 4.81e-40
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| zf-UBR | pfam02207 | Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ... |
121-187 | 1.67e-29 | ||||||||
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases that recognize N-recognins. Pssm-ID: 460491 Cd Length: 68 Bit Score: 112.77 E-value: 1.67e-29
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| ZnF_UBR1 | smart00396 | Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ... |
120-188 | 1.29e-21 | ||||||||
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain is involved in recognition of N-end rule substrates in yeast Ubr1p Pssm-ID: 197698 Cd Length: 71 Bit Score: 90.19 E-value: 1.29e-21
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| RING-H2_UBR1-like | cd16482 | RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 ... |
1388-1448 | 7.90e-21 | ||||||||
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar proteins; Two UBR family members, UBR1 and UBR2, are major N-recognin ubiquitin ligases that both function in the N-end rule degradation pathway. They can recognize substrate proteins with type-1 (basic) and type-2 (bulky hydrophobic) N-terminal residues as part of N-degrons and an internal lysine residue for ubiquitin conjugation. They also function in a quality control pathway for degradation of unfolded cytosolic proteins. Their action is stimulated by Hsp70. Moreover, UBR1 and UBR2 are negative regulators of the leucine-mTOR signaling pathway. Leucine might activate this pathway in part through inhibition of their ubiquitin ligase activity. In yeast, only one E3, encoded by UBR1, mediates the recognition of substrates by the N-end rule pathway. Saccharomyces cerevisiae UBR1 also functions as an additional E3 ligase in the endoplasmic reticulum-associated protein degradation (ERAD). It can provide ubiquitin ligation activity for the ERAD substrate mutated Ste6 (sterile). Schizosaccharomyces pombe UBR1 is a critical regulator that influences the oxidative stress response via degradation of active Pap1 basic leucine zipper (bZIP) transcription factor in the nucleus. Both UBR1 and UBR2 contain an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain. Pssm-ID: 438145 Cd Length: 67 Bit Score: 87.78 E-value: 7.90e-21
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| Name | Accession | Description | Interval | E-value | ||||||||
| PRT6_C | pfam18995 | Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. ... |
1522-1984 | 1.79e-98 | ||||||||
Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. Proteolysis 6 (PRT6) encodes a ubiquitin E3 ligase belonging to the N-end rule pathway of targeted protein degradation, which is a specialized subset of the ubiquitin proteasome system. In Arabidopsis, at least two N-recognins (E3 ubiquitin ligases) with different substrate specificities exist, namely PROTEOLYSIS1 (PRT1) and PRT6. Pssm-ID: 465944 Cd Length: 444 Bit Score: 325.38 E-value: 1.79e-98
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| UBR-box_UBR3 | cd19673 | UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ... |
119-188 | 4.81e-40 | ||||||||
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1. Pssm-ID: 439071 Cd Length: 72 Bit Score: 142.72 E-value: 4.81e-40
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| zf-UBR | pfam02207 | Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ... |
121-187 | 1.67e-29 | ||||||||
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases that recognize N-recognins. Pssm-ID: 460491 Cd Length: 68 Bit Score: 112.77 E-value: 1.67e-29
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| UBR-box_UBR1_2_3 | cd19670 | UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ... |
121-188 | 1.68e-27 | ||||||||
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 (UBR3) and similar proteins; This family includes UBR1, UBR2, and UBR3 (all belonging to EC 2.3.2.27). Both UBR1 (also called E3alpha-I or N-recognin-1) and UBR2 (also called E3-alpha-II or N-recognin-2), are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis. UBR3, also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1. Pssm-ID: 439068 Cd Length: 69 Bit Score: 107.07 E-value: 1.68e-27
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| UBR-box_UBR1_like | cd19672 | UBR-box found in ubiquitin-protein ligases, E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar ... |
120-188 | 3.20e-27 | ||||||||
UBR-box found in ubiquitin-protein ligases, E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar proteins; This family includes UBR1 and UBR2 (both EC 2.3.2.27). Both UBR1 (also called E3alpha-I or N-recognin-1) and UBR2 (also called E3-alpha-II or N-recognin-2), are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis. Pssm-ID: 439070 Cd Length: 70 Bit Score: 106.18 E-value: 3.20e-27
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| ZnF_UBR1 | smart00396 | Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ... |
120-188 | 1.29e-21 | ||||||||
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain is involved in recognition of N-end rule substrates in yeast Ubr1p Pssm-ID: 197698 Cd Length: 71 Bit Score: 90.19 E-value: 1.29e-21
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| RING-H2_UBR1-like | cd16482 | RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 ... |
1388-1448 | 7.90e-21 | ||||||||
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar proteins; Two UBR family members, UBR1 and UBR2, are major N-recognin ubiquitin ligases that both function in the N-end rule degradation pathway. They can recognize substrate proteins with type-1 (basic) and type-2 (bulky hydrophobic) N-terminal residues as part of N-degrons and an internal lysine residue for ubiquitin conjugation. They also function in a quality control pathway for degradation of unfolded cytosolic proteins. Their action is stimulated by Hsp70. Moreover, UBR1 and UBR2 are negative regulators of the leucine-mTOR signaling pathway. Leucine might activate this pathway in part through inhibition of their ubiquitin ligase activity. In yeast, only one E3, encoded by UBR1, mediates the recognition of substrates by the N-end rule pathway. Saccharomyces cerevisiae UBR1 also functions as an additional E3 ligase in the endoplasmic reticulum-associated protein degradation (ERAD). It can provide ubiquitin ligation activity for the ERAD substrate mutated Ste6 (sterile). Schizosaccharomyces pombe UBR1 is a critical regulator that influences the oxidative stress response via degradation of active Pap1 basic leucine zipper (bZIP) transcription factor in the nucleus. Both UBR1 and UBR2 contain an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain. Pssm-ID: 438145 Cd Length: 67 Bit Score: 87.78 E-value: 7.90e-21
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| UBR-box_UBR1 | cd19678 | UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins; UBR1 (EC 2.3. ... |
120-188 | 1.49e-19 | ||||||||
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins; UBR1 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-I (E3alpha-I), or N-recognin-1, is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. Pssm-ID: 439076 Cd Length: 71 Bit Score: 84.58 E-value: 1.49e-19
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| UBR-box_UBR2 | cd19679 | UBR-box found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins; UBR2 (EC 2.3. ... |
120-188 | 2.76e-17 | ||||||||
UBR-box found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins; UBR2 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-II (E3alpha-II), or N-recognin-2, is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis. Pssm-ID: 439077 Cd Length: 70 Bit Score: 78.04 E-value: 2.76e-17
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| UBR-box | cd19669 | UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ... |
121-188 | 1.62e-16 | ||||||||
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box is a 70-residue zinc finger domain present in the UBR family of E3 ubiquitin ligases (UBR1-7, also called N-recognins) that directly binds N-terminal degradation signals (N-degrons) in substrate proteins to facilitate substrate ubiquitination and proteasomal degradation via the ubiquitin-proteasome system (UPS). UBR1 and UBR2 bind all type-1 and type-2 N-degrons. They mediate ubiquitination and proteolysis of short-lived regulators and misfolded proteins. UBR4 binds both type-1 and type-2 N-degrons and is involved in proteome-wide turnover of cell surface proteins. UBR5 preferentially binds type-1 N-degrons and mediates ubiquitination of short-lived proteins. UBR3, UBR6 (also called FBXO11), and UBR7 may not bind efficiently to N-degrons. UBR3 is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. UBR6 is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. It does not bind N-terminal signals. UBR7 is a RING-type E3 ubiquitin ligase that may play an important role in spermiogenesis and fertilization. Pssm-ID: 439067 Cd Length: 66 Bit Score: 75.63 E-value: 1.62e-16
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| RING-H2_UBR3 | cd16483 | RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar ... |
1387-1448 | 1.10e-15 | ||||||||
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3, also known as N-recognin-3, E3alpha-III, or zinc finger protein 650, is an E3 ubiquitin-protein ligase targeting the essential DNA repair protein APE1, also known as Ref-1, for ubiquitylation. It regulates cellular levels of APE1 and is required for genome stability. It also plays a regulatory role in sensory pathways, including olfaction. In Drosophila, UBR3 also regulates apoptosis by controlling the activity of Drosophila inhibitor of apoptosis protein 1 (DIAP1), which is required to prevent caspase activation. UBR3 contains an N-terminal ubiquitin-recognin (UBR) box, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain. Pssm-ID: 438146 Cd Length: 63 Bit Score: 73.20 E-value: 1.10e-15
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| RING-H2_UBR2 | cd16686 | RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar ... |
1383-1448 | 5.06e-10 | ||||||||
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins; UBR2, also known as N-recognin-2 or E3alpha-II, is an E3 ubiquitin-protein ligase that plays an important role in maintaining genome integrity and in homologous recombination repair. It regulates the level of the transcription factor Rpn4 (also known as Son1 and Ufd5) through ubiquitylation. The ubiquitin-conjugating enzyme Rad6, another binding partner of URB2, and an additional factor Mub1, are required for the ubiquitin-dependent degradation of Rpn4. UBR2 associates with Mub1 to form a Mub1/Ubr2 complex that regulates the conserved Dsn1 kinetochore protein levels, which is a part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability. As the recognition component of a major cellular proteolytic system, UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both spermatocytes and somatic cells. UBR2 also mediates transcriptional silencing during spermatogenesis via histone ubiquitination. It functions as a scaffold E3 promoting HR6B/UbcH2-dependent ubiquitylation of H2A and H2B, but not H3 and H4. It also binds to Tex19.1, also known as Tex19, a germ cell-specific protein, and metabolically stabilizes it during spermatogenesis. Furthermore, UBR2 is involved in skeletal muscle (SKM) atrophy. Its expression can be modulated by the mouse ether-a-gogo-related gene 1a (MERG1a) potassium channel. In addition, UBR2 up-regulation in cachectic muscle is mediated by the p38beta-CCAAT/enhancer binding protein (C/EBP)-beta signaling pathway responsible for the bulk of tumor-induced muscle proteolysis. UBR2 contains an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain. Pssm-ID: 438347 Cd Length: 116 Bit Score: 58.87 E-value: 5.06e-10
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| RING-H2_UBR1 | cd16685 | RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar ... |
1389-1451 | 2.38e-08 | ||||||||
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins; UBR1, also known as N-recognin-1 or E3alpha-I, is an E3 ubiquitin-protein ligase component of the N-end rule pathway. It also promotes degradation of proteins via distinct mechanism that detects a misfolded conformation. UBR1 associates with the RAD6-encoded E2 enzyme to form an E2-E3 complex that catalyzes the synthesis of a substrate-linked multi-ubiquitin chain and may also mediate the delivery of substrates to the 26S proteasome. Moreover, UBR1 promotes the degradation of misfolded proteins in the cytosol. It promotes protein kinase quality control and sensitizes cells to heat shock protein 90 (Hsp90) inhibition. Furthermore, UBR1 functions as a polyubiquitylation-enhancing component of the UBR1-UFD4 complex in its targeting of ubiquitin-fusion degradation (UFD) substrates. UBR1 harbors at least three distinct substrate-binding sites and functions in association with Ubc2/Rad6 and also Ubc4. It contains an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain. A missense mutation in UBR1 is responsible for Johanson-Blizzard syndrome leads to UBR box unfolding and loss of function. Pssm-ID: 438346 Cd Length: 120 Bit Score: 54.10 E-value: 2.38e-08
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| RING-H2 | cd16448 | H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ... |
1386-1440 | 2.86e-03 | ||||||||
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates. Pssm-ID: 438112 [Multi-domain] Cd Length: 43 Bit Score: 37.38 E-value: 2.86e-03
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| UBR-box_UBR4_5_6_7 | cd19671 | UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ... |
128-174 | 9.21e-03 | ||||||||
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 (EC 2.3.2.27), UBR5 (EC 2.3.2.26), UBR6/FBOX11 and UBR7 (EC 2.3.2.27). Both UBR4 (also called 600 kDa retinoblastoma protein-associated factor, or N-recognin-4, or retinoblastoma-associated factor of 600 kDa, or RBAF600, or p600, or zinc finger UBR1-type protein 1) and UBR7 (also called N-recognin-7) are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR5 (also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia. UBR6 (also called FBOX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)), is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. UBR6 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. UBR6 does not bind N-terminal signals. Pssm-ID: 439069 Cd Length: 67 Bit Score: 36.67 E-value: 9.21e-03
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