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Information on EC 2.3.2.27 - RING-type E3 ubiquitin transferase and Organism(s) Homo sapiens and UniProt Accession P36406

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.27 RING-type E3 ubiquitin transferase
IUBMB Comments
RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. Unlike EC 2.3.2.26, HECT-type E3 ubiquitin transferase, the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32, cullin-RING-type E3 NEDD8 transferase). cf. EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
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Homo sapiens
UNIPROT: P36406
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine
+
[acceptor protein]-L-lysine
=
[E2 ubiquitin-conjugating enzyme]-L-cysteine
+
[acceptor protein]-N6-ubiquitinyl-L-lysine
Synonyms
brca1, parkin, e3 ubiquitin ligase, e3 ligase, c-cbl, ciap2, trim5alpha, rnf43, trim25, trim5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BRCA1
breast cancer susceptibility protein 1
-
-
breast cancer type 1 susceptibility protein
-
E3 ubiquitin ligase
-
-
E3 ubiquitin-protein ligase Arkadia
-
E3 ubiquitin-protein ligase Mdm2
-
E3 ubiquitin-protein ligase RNF25
-
HHARI
Human Homologue of Drosophila Ariadne
-
mahogunin ring finger-1
-
Parkin
Parkinson juvenile disease protein 2
-
RING E3 ubiquitin ligase
-
Ring finger protein 186
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ring-finer protein 55
-
RING-IBR-RING ubiquitin ligase
-
TRIM5alpha
-
tripartite motif-containing protein 5
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. Unlike EC 2.3.2.26, HECT-type E3 ubiquitin transferase, the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32, cullin-RING-type E3 NEDD8 transferase). cf. EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 [gp78-ubiquitin-carrier protein Ub2g2]-S-ubiquitinyl-L-cysteine
[gp78-ubiquitin-carrier protein Ub2g2]-S-[ubiquitinyl-N6-ubiquitinyl-L-lysine46]-L-cysteine
show the reaction diagram
use of mouse Ube2g2 ubiquitin conjugating enzyme. Ube2g2/gp78-mediated polyubiquitination involves preassembly of Lys 48-linked ubiquitin chains at the catalytic cysteine residue C89 of Ube2g2. The growth of Ube2g2-anchored ubiquitin chains seems to be mediated by an aminolysis-based transfer reaction between two Ube2g2 molecules that each carries a ubiquitin moiety in its active site. Polyubiquitination of a substrate can be achieved by transferring preassembled ubiquitin chains from Ube2g2 to a lysine residue in a substrate
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-
?
S-(ubiquitin)n-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [RNF186]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-(ubiquitin)n-[RNF186]-L-lysine
show the reaction diagram
BNip1 is a Bcl-2 family protein
isoform RNF186 undergoes RING-dependent self-ubiquitination
-
?
S-(ubiquitin)n-[Ubc13]-L-cysteine + [ubiquitin]-L-lysine
[Ubc13]-L-cysteine + N6-(ubiquitin)n-[ubiquitin]-L-lysine
show the reaction diagram
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-
human T lymphotropic virus type 1 trans-activator/oncoprotein Tax greatly stimulates RNF8 and Ubc13:Uev1A/Uev2 to assemble long K63-polyubiquitin chains
-
?
S-ubiquinyl-[UbcH13]-L-cysteine + [acceptor protein]-L-lysine
[UbcH13]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme Ubc13]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme Ubc13]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme UbcH7]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme UbcH7]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
-
-
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [BNip1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[BNip1]-L-lysine
show the reaction diagram
BNip1 is a Bcl-2 family protein
BNip1 is polyubiquitinated by isoform RNF186 through K29 and K63 linkage in vivo. This modification promotes BNip1 transportation to mitochondria but has no influence on its protein level
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[histone H2A]-L-lysine
show the reaction diagram
-
E3-ligase activity of isoform Ring1b on histone H2A is enhanced by polycomb group protein Bmi1 in vitro. The N-terminal Ring-domains are sufficient for this activity and Ring1a can replace Ring1b. E2 enzymes UbcH5a, b, c or UbcH6 support this activity with varying processivity and selectivity
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?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [Ring1b]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[Ring1b]-L-lysine
show the reaction diagram
-
autoubiquitination reaction, E2 enzymes UbcH5a, b, c or UbcH6 support autoubiquitination
-
?
S-ubiquitinyl-[Hip2]-L-cysteine + [acceptor protein]-L-lysine
[Hip2]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
-
isoform RNF2 interacts with E2 protein Hip2, i.e. Huntingtin-interacting protein-2, and with Ubc4, UbcH5. RNF2 shows ubiquitin transferase E3 activity in the presence of Hip2
-
?
S-ubiquitinyl-[Ubc7]-L-cysteine + [CYP3A4]-L-lysine
[Ubc7]-L-cysteine + N6-ubiquitinyl-[CYP3A4]-L-lysine
show the reaction diagram
-
human liver endoplasmic reticulum-anchored cytochrome P450 enzyme CYP3A4 is degradedvia ubiquitylation by E2 ubiquitin-conjugating enzyme Ubc7/E3 ubiquitin-ligase gp78. CYP3A4 Asp/Glu/Ser(P)/Thr(P) surface clusters are important for its intermolecular electrostatic interactions with each of these E2-E3 subcomponents. By imparting additional negative charge to these Asp/Glu clusters, such Ser/Thr phosphorylation would generate P450 phosphodegrons for molecular recognition by the E2-E3 complexes, thereby controlling the timing of CYP3A4 ubiquitination and endoplasmic reticulum-associated degradation
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?
S-ubiquitinyl-[UbcH5a]-L-cysteine + [p53]-L-lysine
[UbcH5a]-L-cysteine + N6-ubiquitinyl-[p53]-L-lysine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[UbcH5]-L-cysteine + [TRIM62]-L-lysine
[UbsH5B]-L-cysteine + N6-ubiquitinyl-[TRIM62]-L-lysine
show the reaction diagram
-
TRIM62, in association with the E2 enzyme UbcH5B, catalyzes self-ubiquitination in vitro. The process requires an intact RING finger domain. The treatment of HEK-293T cells with a proteasome inhibitor stabilizes poly-ubiquitinated TRIM62, indicating that self-ubiquitination promotes the proteasomal degradation of TRIM62
-
?
S-ubiquitinyl-[UbcM2]-L-cysteine + [acceptor protein]-L-lysine
[UbcM2]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
-
-
-
?
[c-Cbl-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [epidermal growth factor receptor]-L-lysine
[c-Cbl-ubiquitin-carrier protein]-L-cysteine + [epidermal growth factor receptor]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[CDC34]-S-ubiquitinyl-L-cysteine + [SCF]-L-lysine
[CDC34]-L-cysteine + [SCF]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
acceptor protein SCF consists of the cullin Cul1, the RING subunit Rbx1/Roc1/Hrt1, the adaptor protein Skp1, and an F-box protein such as Skp2 or TrCP that binds substrates
the I44A mutation in ubiquitin profoundly inhibits its ability to serve as a donor for ubiquitin chain initiation or elongation, but can be rescued by compensatory mutations in the E2 Cdc34
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?
[E2 ubiquitin-conjugating enzyme Ub2k/Ube2w]-S-ubiquitinyl-L-cysteine + [BRCA1]-L-lysine
[E2 ubiquitin-conjugating enzyme Ube2k/Ube2w]-L-cysteine + [BRCA1]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[E2 ubiquitin-conjugating enzyme Ubc13/Ube2w]-S-ubiquitinyl-L-cysteine + [BRCA1]-L-lysine
[E2 ubiquitin-conjugating enzyme Ubc13/Ube2w]-L-cysteine + [BRCA1]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[E2 ubiquitin-conjugating enzyme UbcH5b]-S-ubiquitinyl-L-cysteine + [Ring finger domain of MEX3C]-L-lysine
[E2 ubiquitin-conjugating enzyme UbcH5b]-L-cysteine + [Ring finger domain of MEX3C]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[E2 ubiquitin-conjugating enzyme Ube2B]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme Ube2B]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[E2 ubiquitin-conjugating enzyme Ube2D]-S-ubiquitinyl-L-cysteine + [beta-catenin phosphoprotein]-L-lysine
[E2 ubiquitin-conjugating enzyme Ube2D]-L-cysteine + [beta-catenin phosphoprotein]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[E2 ubiquitin-conjugating enzyme Ube2D]-S-ubiquitinyl-L-cysteine + [protein IkappaBalpha]-L-lysine
[E2 ubiquitin-conjugating enzyme Ube2D]-L-cysteine + [protein IkappaBalpha]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[E2 ubiquitin-conjugating enzyme Ube2e1]-S-ubiquitinyl-L-cysteine + [BRCA1]-L-lysine
[E2 ubiquitin-conjugating enzyme Ube2e1]-L-cysteine + [BRCA1]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[E2 ubiquitin-conjugating enzyme Ube2w]-S-ubiquitinyl-L-cysteine + [BRCA1]-L-lysine
[E2 ubiquitin-conjugating enzyme Ube2w]-L-cysteine + [BRCA1]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[E2 ubiquitin-conjugating enzyme UbeD2]-S-ubiquitinyl-L-cysteine + [p53 transactivation domain]-L-lysine
[E2 ubiquitin-conjugating enzyme UbeD2]-L-cysteine + [p53 transactivation domain]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [FANCD2]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [FANCD2]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
-
-
?
[gp78-ubiquitin-carrier protein Ub2g2]-S-(ubiquitin)x-L-cysteine + HERP-L-lysine
[gp78-ubiquitin-carrier protein Ub2g2]-L-cysteine + HERP-N6-(ubiquitin)x-L-lysine
show the reaction diagram
HERP, ER-associated, short-lived protein that interacts with several E3 enzymes. Use of mouse Ube2g2 ubiquitin conjugating enzyme. Ube2g2/gp78-mediated polyubiquitination involves preassembly of Lys 48-linked ubiquitin chains at the catalytic cysteine of Ube2g2. The growth of Ube2g2-anchored ubiquitin chains seems to be mediated by an aminolysis-based transfer reaction between two Ube2g2 molecules that each carries a ubiquitin moiety in its active site. Polyubiquitination of a substrate can be achieved by transferring preassembled ubiquitin chains from Ube2g2 to a lysine residue in a substrate
-
-
?
[gp78-ubiquitin-carrier protein Ub2g2]-S-[ubiquitinyl-N6-ubiquitinyl-L-lysine46]-L-cysteine + x-2 [gp78-ubiquitin-carrier protein Ub2g2]-S-ubiquitinyl-L-cysteine
[gp78-ubiquitin-carrier protein Ub2g2]-S-(ubiquitin)x-L-cysteine
show the reaction diagram
-
-
-
?
[PirH2-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [PolH]-L-lysine
[PirH2-ubiquitin-carrier protein]-L-cysteine + [PolH]-N6-ubiquitinyl-L-lysine
show the reaction diagram
PolH, DNA polymerase eta, a Y family translesion polymerase and a target of the p53 tumor suppressor. PolH interacts with Pirh2 E3 ligase, via the polymerase-associated domain in PolH and the RING finger domain in Pirh2. PolH is recruited by Pirh2 and degraded by 20S proteasome in a ubiquitin-independent manner
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-
?
[RING-E3-ubiquitin-carrier protein TRIM25]-S-ubiquitinyl-L-cysteine + [RIG-I]-L-lysine
[RING-E3-ubiquitin-carrier protein TRIM25]-L-cysteine + [RIG-I]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
the amino-terminal caspase recruitment domains CARDs of retinoic-acid-inducible gene RIG-I undergo robust ubiquitination induced by TRIM25 in mammalian cells. The carboxy-terminal SPRY domain of TRIM25 interacts with the N-terminal CARDs of RIG-I, this interaction effectively delivers the Lys 63-linked ubiquitin moiety to the N-terminal CARDs of RIG-I, resulting in a marked increase in RIG-I downstream signalling activity. The Lys 172 residue of RIG-I is critical for efficient TRIM25-mediated ubiquitination and for mitochondrial signaling protein MAVS binding, as well as the ability of RIG-I to induce antiviral signal transduction, the amino-terminal caspase recruitment domains CARDs of retinoic-acid-inducible protein RIG-I undergo robust ubiquitination induced by TRIM25 in mammalian cells. The carboxy-terminal SPRY domain of TRIM25 interacts with the N-terminal CARDs of RIG-I, this interaction effectively delivers the Lys 63-linked ubiquitin moiety to the N-terminal CARDs of RIG-I, resulting in a marked increase in RIG-I downstream signalling activity. The Lys 172 residue of RIG-I is critical for efficient TRIM25-mediated ubiquitination and for mitochondrial signaling protein MAVS binding, as well as the ability of RIG-I to induce antiviral signal transduction
-
?
[RN181-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [RN181]-L-lysine
[RN181-ubiquitin-carrier protein]-L-cysteine + [RN181]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
in the presence of a ubiquitin-activating E1 enzyme, a ubiquitin-conjugating E2 enzyme, ubiquitin monomers and ATP, RN181 is self-ubiquitinated
-
?
[RNF43-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [RNF43]-L-lysine
[RNF43-ubiquitin-carrier protein]-L-cysteine + [RNF43]-N6-ubiquitinyl-L-lysine
show the reaction diagram
isoform RNF43 has autoubiquitylation activity. RNF43 is a RING finger-dependent E3 ligase that is selective for E2 enzymes UbcH5b and UbcH5c
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-
?
[TEB4-UBC7]-S-ubiquitinyl-L-cysteine + ubiquitin-L-lysine48
[TEB4-UBC7]-L-cysteine + ubiquitin-N6-ubiquitinyl-L-lysine48
show the reaction diagram
-
formation of a ubiquitin dimer, where residue lysine48 is linked to the C-terminal carboxyl of another ubiquitin. The UBC7-dependent ubiquitin–ubiquitin linkage reaction requires the presence of the ubiquitin-activating enzyme E1 and ATP, suggesting that the activity requires the intermediate formation of an UBC7-ubiquitin thioester
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?
[TEB4-UBC7]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[TEB4-UBC7]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
the isolated TEB4 RING domain catalyses ubiquitin ligation in vitro in a reaction that is ubiquitin Lys48-specific and involves ubiquitin-conjugating enzyme UBC7
-
?
[TRIM22-ubiquitin-carrier protein UbcH5B]-S-ubiquitinyl-L-cysteine + [TRIM22]-L-lysine
[TRIM22-ubiquitin-carrier protein UbcH5B]-L-cysteine + [TRIM22]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
isoform undergoes self-ubiq­uitylation in vitro in combination with the E2 enzyme UbcH5B, the ubiq­uitylation is dependent on its RING finger domain. TRIM22 is conjugated with poly-ubiq­uitin chains and stabilized by proteasome inhibitor in 293T cells
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?
[TRIM5-ubiquitin-carrier protein UbcH5B]-S-ubiquitinyl-L-cysteine + [TRIM5]-L-lysine
[TRIM5-ubiquitin-carrier protein UbcH5B]-L-cysteine + [TRIM5]-N6-ubiquitinyl-L-lysine
show the reaction diagram
TRIM5 functions as a RING-finger-type E3 ubiquitin ligase both in vitro and in vivo and ubiquitinates itself in cooperation with the E2 ubiquitin-conjugating enzyme UbcH5B. TRIM5 is monoubiquitinated, and ubiquitination does not lead to proteasomal degradation. Monoubiquitination may be a signal for TRIM5 to translocate from cytoplasmic bodies to the cytoplasm
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-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme Ubc13]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme Ubc13]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme UbcH7]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme UbcH7]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
-
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
-
-
-
-
?
[RING-E3-ubiquitin-carrier protein TRIM25]-S-ubiquitinyl-L-cysteine + [RIG-I]-L-lysine
[RING-E3-ubiquitin-carrier protein TRIM25]-L-cysteine + [RIG-I]-N6-ubiquitinyl-L-lysine
show the reaction diagram
-
the amino-terminal caspase recruitment domains CARDs of retinoic-acid-inducible gene RIG-I undergo robust ubiquitination induced by TRIM25 in mammalian cells. The carboxy-terminal SPRY domain of TRIM25 interacts with the N-terminal CARDs of RIG-I, this interaction effectively delivers the Lys 63-linked ubiquitin moiety to the N-terminal CARDs of RIG-I, resulting in a marked increase in RIG-I downstream signalling activity. The Lys 172 residue of RIG-I is critical for efficient TRIM25-mediated ubiquitination and for mitochondrial signaling protein MAVS binding, as well as the ability of RIG-I to induce antiviral signal transduction
-
?
additional information
?
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Parkin E3 ligase has autoubiquitination activity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
ubiquitination in the platelet is modulated by elevated intracellular calcium level
Zinc
two Zn2+-binding sites are present involving four cysteine residues found in the loops between beta1-beta2 and beta3-beta4 at site I, residues C344, C347, C362, C367, and three cysteines and a histidine in the extended loop after beta4 at site II, residues C372, C375, H382, C389
Zn2+
absolutely required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
As3+
As3+ can bind to the PHD/RING finger domain of FANCL in vitro and in cells. This binding leads to compromised ubiquitination of FANCD2 in cells and diminishes recruitment of FANCD2 to chromatin and DNA damage sites induced by 4,5',8-trimethylpsoralen plus UVA irradiation
DTPA
treatment leads to inactivation
EDTA
treatment leads to inactivation
RAPTA-EA1
the IC50 value for inactivation of E3 ubiquitin ligase activity by RAPTA-EA1 is markedly lower than the corresponding values for RAPTA-C, RAPTA-T and cisplatin
additional information
binding of the RAPTA compounds, i.e. Ru(h6-arene)(1,3,5-triaza-7-phosphaadamantane)Cl2, to the BRCA1 protein results in a release of Zn2+ ions in a dose- and time-dependent manner, as well as thermal alteration of ruthenated-BRCA1 proteins. The preferential binding sites of the RAPTA complexes on the BRCA1 zinc finger RING domain are at a short peptide stretch, Cys24-Lys25-Phe26-Cys27-Met28-Leu29 and Lys35 (residues 44-49 and 55 on full length BRCA1). Binding results in inactivation of the RING heterodimer BRCA1/BARD1-mediated E3 ubiquitin ligase function
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
presence of ATP is required for catalysis
PINK1
-
Parkin activation as an E3 ubiquitin ligase is regulated by PTEN-induced putative kinase 1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Trim23
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
sequence contains 13 predicted transmembrane domains. The N-terminal region of TEB4 is located in the cytoplasm, whereas the C-terminus of TEB4 has a luminal deposition
Manually annotated by BRENDA team
additional information
isoform TEB4 is notexpressed at the cell surface
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TRI23_HUMAN
574
0
64067
Swiss-Prot
Secretory Pathway (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
97000
x * 97000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 97000, SDS-PAGE
dimer
crystallization data
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the E3 ubiquitin ligase activity of isoform c-Cbl is negatively regulated by other domains present in the amino-terminal half of the protein, i.e. the TKB and linker helix domains, and this negative regulation is removed when the protein is phosphorylated on tyrosine residues. Tyrosine phosphorylation alters the conformation of c-Cbl. Mutation of certain conserved tyrosine residues to glutamate can constitutively activate the E3 activity of c-Cbl
ubiquitination
additional information
enzyme is N-terminally mono-ubiquitinated by the ubiquitin conjugating enzyme Ubc16
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of the TRIM23 RING domain in isolation and in complex with an E2-ubiquitin conjugate. TRIM23 enzymatic activity requires RING dimerization. The two RING domains have distinct interactions with the E2-ubiquitin conjugate and cooperate in facilitating the ubiquitination reaction
crystal structure of ZNRF1 C-terminal domain in complex with Ube2N. The domain binds Ube2N exclusively via its RING domain. The ZNRF1:Ube2N interface contains three salt-bridges/H-bonds involving Glu183 of ZNRF1 and Arg14/Lys10 of Ube2N
crystallization of isoform parkin protein residues 141-465 including RING 0 and RING-between-RING domains. The protein is assembled into two compact domain groups separated by linkers. The catalytic network consists of residues C431 and H433. Parkin functions as a RING/HECT hybrid ubiquitin ligase
hanging drop vapor diffusion method, using either 1.0-1.4 M potassium/sodium tartrate /0.1M CHES pH 9.5 /0.2M LiSO4, or 0.5-0.55 M trisodium citrate/0.1 M citric acid pH 5.2/0.2 M lithium acetate, at room temperature
heterodimeric structure of the complex of Ring1b and Bmi1. Complex formation depends on an N-terminal arm of Ring1b that embraces the Bmi1 Ring-domain. Catalytic activity resides in Ring1b and not in Bmi1
in complex with polycomb group RING finger proteins PCGF5 or PCGF4 and E2 enzyme UbcH5. RING1B binds directly to UbcH5c, with the PCGF partner making no contacts with the E2. The catalytically critical hydrogen bond between RING1B R91 and the backbone carbonyl of UbcH5c Q92 is present in both the structures, consistent with an activated conformation of the E2. Differences between the PCGF4 and PCGF5 ternary complex structures are found at the N termini of the PCGF and RING1B
RNF8(345-485)/Ubc13-Ub complex, hanging drop vapor diffusion method, using
solution structure of the isoform HHARI RING2 domain, the key portion of this E3 ligase required for the RING/HECT hybrid mechanism. The domain possesses two Zn2+-binding sites and a single exposed cysteine used for ubiquitin catalysis. A structural comparison of the RING2 domain with the HECT E3 ligase NEDD4 reveals a near mirror image of the cysteine and histidine residues in the catalytic site. A tandem pair of aromatic residues exists near the C-terminus of the HHARI RING2 domain that is conserved in other RING-in-Between-RING E3 ligases
structure of dimeric Ring finger domain of MEX3C and comparison with the complex structure of MDM2/MDMX-UbcH5b-Ub. The Ring finger domain of MEX3C acts as a ubiquitin E3 ligase in vitro, cooperating with E2 enzymes UbcH5b and UbcH5c to mediate ubiquitination
structure of the RING domain (residues 907-975) at a resolution of 1.8 A. The core RING domain resembles other RING domains, with two zinc ions coordinated in a cross-braced arrangement by one His and seven Cys side chains. Residues in the core RING domain, the N-terminal alpha-helix, and the C-terminal tail comprise the dimer interface
structures of MUL1-RING domain and of its complex with the cognate E2 enzyme UbeD2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A46P
-
the mutant shows barely detectable autoubiquitination activity compared to the wild type
C11A
mutation introduced to reduce the stability of the RING domain, poor activity
C15A
mutation in the conserved RING-finger domain, loss of autoubiquitination ability
C431A
mutation eliminates parkin-catalyzed degradation of mitochondria
C431S
C53A
mutation in Zn2+ coordination site of BARD1, increases E3 ligase activity
C608S/C611S
mutation in Zn2+ coordination site, almost complete loss ofactivity
C61A/C64A
mutation of two adjacent cysteine residues at the conserved zinc-binding position, mutant shows weak activity
C632S
mutation in Zn2+ coordination site, almost complete loss of activity
C71A
mutation in Zn2+ coordination site of BARD1, increases E3 ligase activity
C9A
mutation within the RING domain of TEB4, strongly impairs its own degradation
D67E
-
mutation identified in Thai familial breast cancer patients. The mutation is located in the vicinity of Zn2+ binding site II. The D67E BRCA1 RING protein assumes a preformed structure in the absence of Zn2+. The Zn2+-bound mutant protein is more folded than wild-type, resulting in enhanced proteolytic resistance and dimerization. The mutation retains Zn2+ binding, and barely perturbs the native global structure of the BRCA1 RING domain. The D67E mutation might be a neutral or mild cancer-risk modifier of other defective mechanisms underlying BRCA1-mutation-related breast cancer
I26A/L63A/K65A
mutations in BRCA1, complete elimination of BRCA1 activity without disrupting its structure
I53A
the Ring1b/Bmi1 complex with an I53A mutation in Ring1b has almost no catalytic activity
I610A
mutation abolishes selfubiquitination activity. Residue may play key role to interact with E2 and stabilize ubiquitin in the closed active E2-Ub conformation
I636A
mutation abolishes selfubiquitination activity
K27N
-
the mutant shows barely detectable autoubiquitination activity compared to the wild type
K48A
-
the mutant has higher autoubiquitination activity than the wild type
K639A
mutation reduces selfubiquitination activity
K65R
activating mutation in BRCA1
L451D
the mutation causes a drastic decrease in the ability of the enzyme to stimulate Ubc13
L51W
activating mutation in BRCA1
L51W/K65R
mutant of BRCA1, much more active than either of the individual activating mutants
P645A
mutation abolishes selfubiquitination activity
Q648A
mutation abolishes selfubiquitination activity. Residue may play key role to interact with E2 and stabilize ubiquitin in the closed active E2-Ub conformation
R33Q
-
the mutant shows barely detectable autoubiquitination activity compared to the wild type
R42P
-
the mutant has higher autoubiquitination activity than the wild type
R441A
the mutation has little effect on the enzyme activity
S17D
phosphomimetic mutation, stimulates MDM2-mediated polyubiquitination of p53. The stimulation is independent of p53 substrate. Mutation alters the conformation of the isolated N-terminus, it induces increased thermostability of the isolated N-terminal domain, it stimulates the allosteric interaction of MDM2 with the DNA-binding domain of p53 and it stimulates a protein-protein interaction with the E2-ubiquitin complex in the absence of substrate p53 that, in turn, increases hydrolysis of the E2-ubiquitin thioester bond
T240R
-
the mutant shows barely detectable autoubiquitination activity compared to the wild type
V609A
mutation reduces selfubiquitination activity
V609E
mutation abolishes selfubiquitination activity
V646E
mutation abolishes selfubiquitination activity
Y268E
no increased activity compared to unphosphorylated wild-type
Y268F
residue Y268 is not required for phosphorylation-induced activation
Y274E
slightly increased activity compared to unphosphorylated wild-type
Y291E
no increased activity compared to unphosphorylated wild-type
Y307E
strongly increased activity compared to unphosphorylated wild-type
Y337E
strongly increased activity compared to unphosphorylated wild-type
Y371E
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in HEK-293T and HeLa cells
-
expression in COS-7 cell and 293-T cell
expression in Escherichia coli
expression in HEK-293T cell
expression in HEK-293T cell and HBL human melanoma cell
expression in HeLa cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
human melanoma cells express four MGRN isoforms
TEB4 expression does not increase in response to the various stress conditions
the gene encoding RNF43 is upregulated in colon adenocarcinoma as well as in colon adenoma
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
development of a structure decomposition method that utilizes network analysis and computational thermodynamic measures of fold stability changes upon amino acids alterations
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gack, M.U.; Shin, Y.C.; Joo, C.H.; Urano, T.; Liang, C.; Sun, L.; Takeuchi, O.; Akira, S.; Chen, Z.; Inoue, S.; Jung, J.U.
TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
Nature
446
916-920
2007
Homo sapiens (Q14258)
Manually annotated by BRENDA team
Brophy, T.M.; Raab, M.; Daxecker, H.; Culligan, K.G.; Lehmann, I.; Chubb, A.J.; Treumann, A.; Moran, N.
RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3
Biochem. Biophys. Res. Commun.
369
1088-1093
2008
Homo sapiens (Q9P0P0), Homo sapiens
Manually annotated by BRENDA team
Duan, Z.; Gao, B.; Xu, W.; Xiong, S.
Identification of TRIM22 as a RING finger E3 ubiquitin ligase
Biochem. Biophys. Res. Commun.
374
502-506
2008
Homo sapiens (Q8IYM9)
Manually annotated by BRENDA team
Sugiura, T.; Yamaguchi, A.; Miyamoto, K.
A cancer-associated RING finger protein, RNF43, is a ubiquitin ligase that interacts with a nuclear protein, HAP95
Exp. Cell Res.
314
1519-1528
2008
Homo sapiens (Q68DV7)
Manually annotated by BRENDA team
Yamauchi, K.; Wada, K.; Tanji, K.; Tanaka, M.; Kamitani, T.
Ubiquitination of E3 ubiquitin ligase TRIM5alpha and its potential role
FEBS J.
275
1540-1555
2008
Homo sapiens (Q9C035), Homo sapiens
Manually annotated by BRENDA team
Tatham, M.H.; Geoffroy, M.C.; Shen, L.; Plechanovova, A.; Hattersley, N.; Jaffray, E.G.; Palvimo, J.J.; Hay, R.T.
RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
Nat. Cell Biol.
10
538-546
2008
Homo sapiens (Q9UNE7)
Manually annotated by BRENDA team
Perez-Oliva, A.B.; Olivares, C.; Jimenez-Cervantes, C.; Garcia-Borron, J.C.
Mahogunin ring finger-1 (MGRN1) E3 ubiquitin ligase inhibits signaling from melanocortin receptor by competition with Galphas
J. Biol. Chem.
284
31714-31725
2009
Homo sapiens (O60921), Homo sapiens
Manually annotated by BRENDA team
Hassink, G.; Kikkert, M.; Van Voorden, S.; Lee, S.; Spaapen, R.; Van Laar, T.; Coleman, C.; Bartee, E.; Frh, K.; Chau, V.; Wiertz, E.
TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
Biochem. J.
388
647-655
2005
Homo sapiens (O60337)
Manually annotated by BRENDA team
Kassenbrock, C.; Anderson, S.
Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations
J. Biol. Chem.
279
28017-28027
2004
Homo sapiens (P22681)
Manually annotated by BRENDA team
Atipairin, A.; Canyuk, B.; Ratanaphan, A.
Substitution of aspartic acid with glutamic acid at position 67 of the BRCA1 RING domain retains ubiquitin ligase activity and zinc(II) binding with a reduced transition temperature
J. Biol. Inorg. Chem.
16
217-226
2011
Homo sapiens
Manually annotated by BRENDA team
Jung, Y.; Liu, G.; Chen, X.
Pirh2 E3 ubiquitin ligase targets DNA polymerase eta for 20S proteasomal degradation
Mol. Cell. Biol.
30
1041-1048
2010
Homo sapiens (Q96PM5), Homo sapiens
Manually annotated by BRENDA team
Saha, A.; Lewis, S.; Kleiger, G.; Kuhlman, B.; Deshaies, R.J.
Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate
Mol. Cell
42
75-83
2011
Homo sapiens
Manually annotated by BRENDA team
Riley, B.E.; Lougheed, J.C.; Callaway, K.; Velasquez, M.; Brecht, E.; Nguyen, L.; Shaler, T.; Walker, D.; Yang, Y.; Regnstrom, K.; Diep, L.; Zhang, Z.; Chiou, S.; Bova, M.; Artis, D.R.; Yao, N.; Baker, J.; Yednock, T.; Johnston, J.A.
Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases
Nat. Commun.
4
1982
2013
Homo sapiens (O60260)
Manually annotated by BRENDA team
Li, W.; Tu, D.; Brunger, A.; Ye, Y.
A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate
Nature
446
333-337
2007
Homo sapiens (Q9UKV5)
Manually annotated by BRENDA team
Spratt, D.E.;, Mercier, P.; Shaw, G.S.
Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase
PLoS One
15
e74047
2013
Homo sapiens (Q9Y4X5), Homo sapiens
Manually annotated by BRENDA team
Han, Y.; Li, R.; Gao, J.; Miao, S.; Wang, L.
Characterisation of human RING finger protein TRIM69, a novel testis E3 ubiquitin ligase and its subcellular localisation
Biochem. Biophys. Res. Commun.
429
6-11
2012
Homo sapiens (Q86WT6), Homo sapiens
Manually annotated by BRENDA team
Huang, F.; Xiao, H.; Sun, B.L.; Yang, R.G.
Characterization of TRIM62 as a RING finger E3 ubiquitin ligase and its subcellular localization
Biochem. Biophys. Res. Commun.
432
208-213
2013
Arabidopsis thaliana (Q8GYT9), Homo sapiens (Q9BVG3)
Manually annotated by BRENDA team
Nguyen, L.; Plafker, K.S.; Starnes, A.; Cook, M.; Klevit, R.E.; Plafker, S.M.
The ubiquitin-conjugating enzyme, UbcM2, is restricted to monoubiquitylation by a two-fold mechanism that involves backside residues of E2 and Lys48 of ubiquitin
Biochemistry
53
4004-4014
2014
Homo sapiens (Q96BH1)
Manually annotated by BRENDA team
Wang, P.; Wu, Y.; Li, Y.; Zheng, J.; Tang, J.
A novel RING finger E3 ligase RNF186 regulate ER stress-mediated apoptosis through interaction with BNip1
Cell. Signal.
25
2320-2333
2013
Homo sapiens (Q9NXI6), Homo sapiens
Manually annotated by BRENDA team
Buchwald, G.; van der Stoop, P.; Weichenrieder, O.; Perrakis, A.; van Lohuizen, M.; Sixma, T.K.
Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b
EMBO J.
25
2465-2474
2006
Homo sapiens (Q99496)
Manually annotated by BRENDA team
Lee, S.J.; Choi, J.Y.; Sung, Y.M.; Park, H.; Rhim, H.; Kang, S.
E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme
FEBS Lett.
503
61-64
2001
Homo sapiens (Q99496), Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Kim, S.M.; Trnka, M.J.; Liu, Y.; Burlingame, A.L.; Correia, M.A.
Human liver cytochrome P450 3A4 ubiquitination: molecular recognition by UBC7-gp78 autocrine motility factor receptor and UbcH5a-CHIP-Hsc70-Hsp40 E2-E3 ubiquitin ligase complexes
J. Biol. Chem.
290
3308-3332
2015
Homo sapiens (Q9UKV5)
Manually annotated by BRENDA team
Fiesel, F.; Moussaud-Lamodiere, E.; Ando, M.; Springer, W.
A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently
J. Cell Sci.
127
3488-3504
2014
Homo sapiens (O60260)
Manually annotated by BRENDA team
Fraser, J.; Worrall, E.; Lin, Y.; Landre, V.; Pettersson, S.; Blackburn, E.; Walkinshaw, M.; Muller, P.; Vojtesek, B.; Ball, K.; Hupp, T.
Phosphomimetic mutation of the N-terminal lid of MDM2 enhances the polyubiquitination of p53 through stimulation of E2-ubiquitin thioester hydrolysis
J. Mol. Biol.
427
1728-1747
2014
Homo sapiens (P51668)
-
Manually annotated by BRENDA team
Taherbhoy, A.; Huang, O.; Cochran, A.
BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase
Nat. Commun.
6
7621
2015
Homo sapiens (Q99496)
Manually annotated by BRENDA team
Ho, Y.K.; Zhi, H.; Bowlin, T.; Dorjbal, B.; Philip, S.; Zahoor, M.A.; Shih, H.M.; Semmes, O.J.; Schaefer, B.; Glover, J.N.; Giam, C.Z.
HTLV-1 tax stimulates ubiquitin E3 ligase, ring finger protein 8, to assemble lysine 63-linked polyubiquitin chains for TAK1 and IKK activation
PLoS Pathog.
11
e1005102
2015
Homo sapiens
Manually annotated by BRENDA team
Ham, S.J.; Lee, S.Y.; Song, S.; Chung, J.R.; Choi, S.; Chung, J.
Interaction between RING1 (R1) and the ubiquitin-like (UBL) domains is critical for the regulation of parkin activity
J. Biol. Chem.
291
1803-1816
2016
Homo sapiens
Manually annotated by BRENDA team
Hodge, C.D.; Ismail, I.H.; Edwards, R.A.; Hura, G.L.; Xiao, A.T.; Tainer, J.A.; Hendzel, M.J.; Glover, J.N.
RNF8 E3 ubiquitin ligase stimulates Ubc13 E2 conjugating activity that is essential for DNA double-strand break signaling and BRCA1 tumor suppressor recruitment
J. Biol. Chem.
291
9396-9410
2016
Homo sapiens (O76064)
Manually annotated by BRENDA team
Duda, D.M.; Olszewski, J.L.; Schuermann, J.P.; Kurinov, I.; Miller, D.J.; Nourse, A.; Alpi, A.F.; Schulman, B.A.
Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism
Structure
21
1030-1041
2013
Homo sapiens (Q9Y4X5), Homo sapiens
Manually annotated by BRENDA team
Jiang, J.; Bellani, M.; Li, L.; Wang, P.; Seidman, M.M.; Wang, Y.
Arsenite binds to the RING finger domain of FANCL E3 ubiquitin ligase and inhibits DNA interstrand crosslink repair
ACS Chem. Biol.
12
1858-1866
2017
Homo sapiens (Q9NW38), Homo sapiens
Manually annotated by BRENDA team
Lee, S.; Lee, C.; Ryu, K.; Chi, S.
The RING domain of mitochondrial E3 ubiquitin ligase 1 and its complex with Ube2D2 Crystallization and X-ray diffraction
Acta Crystallogr. Sect. F
76
1-7
2020
Homo sapiens (Q969V5)
Manually annotated by BRENDA team
Temboot, P.; Lee, R.F.S.; Menin, L.; Patiny, L.; Dyson, P.J.; Ratanaphan, A.
Biochemical and biophysical characterization of ruthenation of BRCA1 RING protein by RAPTA complexes and its E3 ubiquitin ligase activity
Biochem. Biophys. Res. Commun.
488
355-361
2017
Homo sapiens (P38398)
Manually annotated by BRENDA team
Behera, A.P.; Naskar, P.; Agarwal, S.; Banka, P.A.; Poddar, A.; Datta, A.B.
Structural insights into the nanomolar affinity of RING E3 ligase ZNRF1 for Ube2N and its functional implications
Biochem. J.
475
1569-1582
2018
Homo sapiens (Q8ND25)
Manually annotated by BRENDA team
Chasapis, C.T.
Hierarchical core decomposition of RING structure as a method to capture novel functional residues within RING-type E3 ligases a structural systems biology approach
Comput. Biol. Med.
100
86-91
2018
Homo sapiens (P38398), Homo sapiens (Q00987), Homo sapiens (Q13489)
Manually annotated by BRENDA team
Woodfield, S.E.; Guo, R.J.; Liu, Y.; Major, A.M.; Hollingsworth, E.F.; Indiviglio, S.; Whittle, S.B.; Mo, Q.; Bean, A.J.; Ittmann, M.; Lopez-Terrada, D.; Zage, P.E.
Neuroblastoma patient outcomes, tumor differentiation, and ERK activation are correlated with expression levels of the ubiquitin ligase UBE4B
Genes Cancer
7
13-26
2016
Homo sapiens (O95155), Homo sapiens
Manually annotated by BRENDA team
Foglizzo, M.; Middleton, A.; Day, C.
Structure and function of the RING domains of RNF20 and RNF40, dimeric E3 ligases that monoubiquitylate Histone H2B
J. Mol. Biol.
428
4073-4086
2016
Homo sapiens (Q5VTR2), Homo sapiens
Manually annotated by BRENDA team
Baranes-Bachar, K.; Levy-Barda, A.; Oehler, J.; Reid, D.A.; Soria-Bretones, I.; Voss, T.C.; Chung, D.; Park, Y.; Liu, C.; Yoon, J.B.; Li, W.; Dellaire, G.; Misteli, T.; Huertas, P.; Rothenberg, E.; Ramadan, K.; Ziv, Y.; Shiloh, Y.
The ubiquitin E3/E4 ligase UBE4A adjusts protein ubiquitylation and accumulation at sites of DNA damage, facilitating double-strand break repair
Mol. Cell
69
866-878.e7
2018
Homo sapiens (Q14139)
Manually annotated by BRENDA team
Baek, K.; Krist, D.T.; Prabu, J.R.; Hill, S.; Kluegel, M.; Neumaier, L.M.; von Gronau, S.; Kleiger, G.; Schulman, B.A.
NEDD8 nucleates a multivalent cullin-RING-UBE2D ubiquitin ligation assembly
Nature
578
461-466
2020
Homo sapiens (P62877)
Manually annotated by BRENDA team
Jimenez-Lopez, D.; Aguilar-Henonin, L.; Gonzalez-Prieto, J.M.; Aguilar-Hernandez, V.; Guzman, P.
CTLs, a new class of RING-H2 ubiquitin ligases uncovered by YEELL, a motif close to the RING domain that is present across eukaryotes
PLoS ONE
13
e0190969
2018
Homo sapiens (Q6ZNA4), Arabidopsis thaliana (Q8L649)
Manually annotated by BRENDA team
Ma-Lauer, Y.; Carbajo-Lozoya, J.; Hein, M.; Mueller, M.; Deng, W.; Lei, J.; Meyer, B.; Kusov, Y.; Von Brunn, B.; Bairad, D.; Huenten, S.; Drosten, C.; Hermeking, H.; Leonhardt, H.; Mann, M.; Hilgenfeld, R.; Von Brunn, A.
P53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1
Proc. Natl. Acad. Sci. USA
113
E5192-E5201
2016
Homo sapiens (Q96PM5)
-
Manually annotated by BRENDA team
Stewart, M.; Duncan, E.; Coronado, E.; DaRosa, P.; Pruneda, J.; Brzovic, P.; Klevit, R.
Tuning BRCA1 and BARD1 activity to investigate RING ubiquitin ligase mechanisms
Protein Sci.
26
475-483
2017
Homo sapiens (P38398 and Q99728), Homo sapiens
Manually annotated by BRENDA team
Moududee, S.A.; Jiang, Y.; Gilbert, N.; Xie, G.; Xu, Z.; Wu, J.; Gong, Q.; Tang, Y.; Shi, Y.
Structural and functional characterization of hMEX-3C Ring finger domain as an E3 ubiquitin ligase
Protein Sci.
27
1661-1669
2018
Homo sapiens (Q5U5Q3), Homo sapiens
Manually annotated by BRENDA team
Dawidziak, D.M.; Sanchez, J.G.; Wagner, J.M.; Ganser-Pornillos, B.K.; Pornillos, O.
Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase
Proteins
85
1957-1961
2017
Homo sapiens (P36406)
Manually annotated by BRENDA team