E3 ubiquitin-protein ligase UBR4 family protein similar to mammalian E3 ubiquitin-protein ligase UBR4 that is a a component of the N-end rule 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
E3 ubiquitin-protein ligase UBR4 N-terminal; This entry represents the N-terminal of E3 ...
69-1650
0e+00
E3 ubiquitin-protein ligase UBR4 N-terminal; This entry represents the N-terminal of E3 ubiquitin-protein ligases UBR4 (POE or PUSHOVER in Drosophila), which are components of the N-rule pathway, identified as noncanonical N-recognins implicated in bulk lysosomal degradation and autophagy. These are extraordinarily large proteins that recognize and bind to proteins with N-terminal destabilising residues according to the N-end rule leading them to their ubiquitination and degradation. These proteins share a UBR box (pfam02207) with others E3-ligases UBR box proteins but UBR4 lacks the ubiquitylation domain, suggesting that it may interact with other catalytic proteins.
The actual alignment was detected with superfamily member pfam19423:
Pssm-ID: 466074 Cd Length: 1598 Bit Score: 2597.22 E-value: 0e+00
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
1660-1730
6.10e-56
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 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. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival.
:
Pssm-ID: 439078 Cd Length: 71 Bit Score: 189.59 E-value: 6.10e-56
E3 ubiquitin-protein ligase UBR4 N-terminal; This entry represents the N-terminal of E3 ...
69-1650
0e+00
E3 ubiquitin-protein ligase UBR4 N-terminal; This entry represents the N-terminal of E3 ubiquitin-protein ligases UBR4 (POE or PUSHOVER in Drosophila), which are components of the N-rule pathway, identified as noncanonical N-recognins implicated in bulk lysosomal degradation and autophagy. These are extraordinarily large proteins that recognize and bind to proteins with N-terminal destabilising residues according to the N-end rule leading them to their ubiquitination and degradation. These proteins share a UBR box (pfam02207) with others E3-ligases UBR box proteins but UBR4 lacks the ubiquitylation domain, suggesting that it may interact with other catalytic proteins.
Pssm-ID: 466074 Cd Length: 1598 Bit Score: 2597.22 E-value: 0e+00
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
1660-1730
6.10e-56
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 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. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival.
Pssm-ID: 439078 Cd Length: 71 Bit Score: 189.59 E-value: 6.10e-56
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
1660-1727
4.40e-16
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: 75.56 E-value: 4.40e-16
E3 ubiquitin-protein ligase UBR4 N-terminal; This entry represents the N-terminal of E3 ...
69-1650
0e+00
E3 ubiquitin-protein ligase UBR4 N-terminal; This entry represents the N-terminal of E3 ubiquitin-protein ligases UBR4 (POE or PUSHOVER in Drosophila), which are components of the N-rule pathway, identified as noncanonical N-recognins implicated in bulk lysosomal degradation and autophagy. These are extraordinarily large proteins that recognize and bind to proteins with N-terminal destabilising residues according to the N-end rule leading them to their ubiquitination and degradation. These proteins share a UBR box (pfam02207) with others E3-ligases UBR box proteins but UBR4 lacks the ubiquitylation domain, suggesting that it may interact with other catalytic proteins.
Pssm-ID: 466074 Cd Length: 1598 Bit Score: 2597.22 E-value: 0e+00
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
1660-1730
6.10e-56
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 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. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival.
Pssm-ID: 439078 Cd Length: 71 Bit Score: 189.59 E-value: 6.10e-56
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
1660-1730
8.19e-35
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 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. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival. The family also includes Arabidopsis thaliana auxin transport protein BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1). It is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis.
Pssm-ID: 439072 Cd Length: 72 Bit Score: 129.00 E-value: 8.19e-35
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ...
1662-1727
4.61e-31
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: 118.33 E-value: 4.61e-31
UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG ...
1660-1730
9.27e-30
UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1) is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis.
Pssm-ID: 439079 Cd Length: 74 Bit Score: 114.81 E-value: 9.27e-30
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
1662-1724
1.24e-21
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: 91.42 E-value: 1.24e-21
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
1660-1727
4.40e-16
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: 75.56 E-value: 4.40e-16
UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, ...
1662-1718
1.22e-12
UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, 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. FBXO11 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. FBXO11 does not bind N-terminal signals.
Pssm-ID: 439074 Cd Length: 69 Bit Score: 65.99 E-value: 1.22e-12
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
1658-1728
1.54e-11
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3.2.26; 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.
Pssm-ID: 439073 Cd Length: 76 Bit Score: 62.87 E-value: 1.54e-11
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3. ...
1662-1717
1.30e-06
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3.2.27; also called N-recognin-7) 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. UBR7 may play an important role in spermiogenesis and fertilization.
Pssm-ID: 439075 Cd Length: 71 Bit Score: 48.84 E-value: 1.30e-06
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
1662-1717
6.32e-06
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: 46.97 E-value: 6.32e-06
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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