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2 [gp78-ubiquitin-carrier protein Ub2g2]-S-ubiquitinyl-L-cysteine
[gp78-ubiquitin-carrier protein Ub2g2]-S-[ubiquitinyl-N6-ubiquitinyl-L-lysine46]-L-cysteine
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 + [POX1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-(ubiquitin)n-[POX1]-L-lysine
PIX1 i.e. peroxidase
contrary to substrates PGLU1, bHLH065 and GRP1, POX1 is polyubiquitylated
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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
BNip1 is a Bcl-2 family protein
isoform RNF186 undergoes RING-dependent self-ubiquitination
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S-(ubiquitin)n-[Ubc10]-L-cysteine + [maltose-binding protein]-L-lysine
[Ubc10]-L-cysteine + N6-(ubiquitin)-[maltose-binding protein]-L-lysine
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polyubiquitylation of maltose-binding protein
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S-(ubiquitin)n-[Ubc10]-L-cysteine + [RbcL1]-L-lysine
[Ubc10]-L-cysteine + N6-(ubiquitin)-[RbcL1]-L-lysine
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RbcL1 i.e. a Rubisco subunit
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S-(ubiquitin)n-[Ubc10]-L-cysteine + [RbcS1]-L-lysine
[Ubc10]-L-cysteine + N6-(ubiquitin)-[RbcS1]-L-lysine
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RbcS1 i.e. a Rubisco subunit
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S-(ubiquitin)n-[Ubc13]-L-cysteine + [ubiquitin]-L-lysine
[Ubc13]-L-cysteine + N6-(ubiquitin)n-[ubiquitin]-L-lysine
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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
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S-(ubiquitin)n-[UbcH5]-L-cysteine + [STRF1]-L-lysine
[UbcH5]-L-cysteine + N6-(ubiquitin)n-[STRF1]-L-lysine
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autoubiquitylation reaction leading to polyubiquitylated protein
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S-ubiquinyl-[UbcH13]-L-cysteine + [acceptor protein]-L-lysine
[UbcH13]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
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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
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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
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?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ABI5]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ABI5]-L-lysine
ABI5 i.e. abscisic acid-responsive transcription factor
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ACS4]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ACS4]-L-lysine
ACS4 i.e. aminocyclopropane-1-carboxylic acid synthase 4
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ACS7]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ACS7]-L-lysine
ACS4 i.e. aminocyclopropane-1-carboxylic acid synthase 7
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?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [bHLH065]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[bHLH065]-L-lysine
bHLH065 i.e. ethylene-responsive protein
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [BNip1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[BNip1]-L-lysine
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
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [GRP1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[GRP1]-L-lysine
GRP1 i.e. glycine-rich cell-wall structural protein
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HCI1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[HCI1]-L-lysine
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autoubiquitylation reaction
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[histone H2A]-L-lysine
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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 + [PGLU1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[PGLU1]-L-lysine
PGLU12 i.e periplasmic beta-glucosidase. Isoform HCI1 accepts yeast E1 activating enzyme, and Arabidopsis thaliana E2 conjugating enzymes UBC10 and UBC11
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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
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autoubiquitination reaction, E2 enzymes UbcH5a, b, c or UbcH6 support autoubiquitination
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [SDIRIP1 protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[SDIRIP1 protein]-L-lysine
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [TIP4.1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[TIP4.1]-L-lysine
TIP4 i.e. tonoplast intrinsic protein 4
HIR1 strongly degrads the protein level of TIP4.1 via the ubiquitin 26S proteasome system
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S-ubiquitinyl-[Hip2]-L-cysteine + [acceptor protein]-L-lysine
[Hip2]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
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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
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S-ubiquitinyl-[Ubc10]-L-cysteine + [GIRP1]-L-lysine
[Ubc10]-L-cysteine + N6-ubiquitinyl-[GIRP1]-L-lysine
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autoubiquitylation reaction
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S-ubiquitinyl-[Ubc7]-L-cysteine + [CYP3A4]-L-lysine
[Ubc7]-L-cysteine + N6-ubiquitinyl-[CYP3A4]-L-lysine
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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-[Ubc8]-L-cysteine + [acceptor protein]-L-lysine
[Ubc8]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
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the RING domain of Sis3 is sufficient for E3 ligase activity
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S-ubiquitinyl-[UbcH5a]-L-cysteine + [p21]-L-lysine
[UbcH5a]-L-cysteine + N6-ubiquitinyl-[p21]-L-lysine
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substrate p21 is a protein necessary for the proliferation of a subset of platelet-derived growth factor-transformed proneural glioma cells
UbcH5a is a preferred E2 enzyme for TRIM3-dependent p21 ubiquitination. Ubiquitination is practically eliminated in a p21 K15R/K74R/K91R/K136R quadruple mutant
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S-ubiquitinyl-[UbcH5a]-L-cysteine + [p53]-L-lysine
[UbcH5a]-L-cysteine + N6-ubiquitinyl-[p53]-L-lysine
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S-ubiquitinyl-[UbcH5b]-L-cysteine + [DAF]-L-lysine
[UbcH5b]-L-cysteine + N6-ubiquitinyl-[DAF]-L-lysine
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autoubiquitylation reaction
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S-ubiquitinyl-[UbcH5b]-L-cysteine + [NERF]-L-lysine
[UbcH5b]-L-cysteine + N6-ubiquitinyl-[NERF]-L-lysine
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autoubiquitylation reaction
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S-ubiquitinyl-[UbcH5c]-L-cysteine + [ERF53]-L-lysine
[UbcH5c]-L-cysteine + N6-ubiquitinyl-[ERF53]-L-lysine
ERF53 i.e. ethylene response factor 53
RING E3 ligase RGLG2 mediates ERF53 ubiquitination for proteasomal degradation
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S-ubiquitinyl-[UbcH5]-L-cysteine + [TRIM62]-L-lysine
[UbsH5B]-L-cysteine + N6-ubiquitinyl-[TRIM62]-L-lysine
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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
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S-ubiquitinyl-[UbcM2]-L-cysteine + [acceptor protein]-L-lysine
[UbcM2]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
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S-ubiquitinyl-[Ube2B]-L-cysteine + [March10a]-L-lysine
[Ube2B]-L-cysteine + N6-ubiquitinyl-[March10a]-L-lysine
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[ACRE276-RING domain-E3-ubiquitin-carrier protein HubC5B]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[ACRE276-RING domain-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
[BRCK1-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [BRCK1]-L-lysine
[BRCK1-ubiquitin-carrier protein]-L-cysteine + [BRCK1]-N6-ubiquitinyl-L-lysine
the RING1 finger plays an important role in the self-ubiquitination of RBCK1, leading to mono- and slightly diubiquitinated products. Self-ubiquitinated RBCK1 is processed by the proteasomal degradation
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[BRE1B-ubiquitin-carrier protein UbcH8]-S-ubiquitinyl-L-cysteine + [syntaxin1]-L-lysine
[BRE1B-ubiquitin-carrier protein UbcH8]-L-cysteine + [syntaxin1]-N6-ubiquitinyl-L-lysine
isoform BRE1B binds and recruits the brain-enriched E2 ubiquitin-conjugating enzyme UbcH8 to syntaxin 1 and facilitates the ubiquitination and proteasome-dependent degradation of syntaxin1
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[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
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[CDC34]-S-ubiquitinyl-L-cysteine + [SCF]-L-lysine
[CDC34]-L-cysteine + [SCF]-N6-ubiquitinyl-L-lysine
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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
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[E2 ubiquitin-conjugating enzyme Ubc10]-S-ubiquitinyl-L-cysteine + [AIR1]-L-lysine
[E2 ubiquitin-conjugating enzyme Ubc10]-L-cysteine + [AIR1]-N6-ubiquitinyl-L-lysine
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[E2 ubiquitin-conjugating enzyme UBC10]-S-ubiquitinyl-L-cysteine + [SIRP2]-L-lysine
[E2 ubiquitin-conjugating enzyme UBC10]-L-cysteine + [SIRP2]-N6-ubiquitinyl-L-lysine
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[E2 ubiquitin-conjugating enzyme UBC10]-S-ubiquitinyl-L-cysteine + [TKL1]-L-lysine
[E2 ubiquitin-conjugating enzyme UBC10]-L-cysteine + [TKL1]-N6-ubiquitinyl-L-lysine
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[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
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[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
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[E2 ubiquitin-conjugating enzyme UBCh5b]-S-ubiquitinyl-L-cysteine + [Ring]-L-lysine
[E2 ubiquitin-conjugating enzyme UBCh5b]-L-cysteine + [Ring]-N6-ubiquitinyl-L-lysine
[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
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[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
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[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
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[E2 ubiquitin-conjugating enzyme Ube2e1]-S-ubiquitinyl-L-cysteine + [BRCA1]-L-lysine
[E2 ubiquitin-conjugating enzyme Ube2e1]-L-cysteine + [BRCA1]-N6-ubiquitinyl-L-lysine
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[E2 ubiquitin-conjugating enzyme Ube2w]-S-ubiquitinyl-L-cysteine + [BRCA1]-L-lysine
[E2 ubiquitin-conjugating enzyme Ube2w]-L-cysteine + [BRCA1]-N6-ubiquitinyl-L-lysine
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[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
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [betaC1 protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [betaC1 protein]-N6-ubiquitinyl-L-lysine
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [FANCD2]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [FANCD2]-N6-ubiquitinyl-L-lysine
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [KAT1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [KAT1]-N6-ubiquitinyl-L-lysine
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [MLO12-Myc]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor MLO12-Myc]-N6-ubiquitinyl-L-lysine
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [MYB1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [MYB1]-N6-ubiquitinyl-L-lysine
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[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
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
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[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
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[PirH2-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [PolH]-L-lysine
[PirH2-ubiquitin-carrier protein]-L-cysteine + [PolH]-N6-ubiquitinyl-L-lysine
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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[PUB54-RING domain-ubiquitin-carrier protein Ubc13]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[PUB54-RING domain-ubiquitin-carrier protein Ubc13]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
ubiquitination activity is seen with both family-4/5 UBC enzymes, encoded by At2g16740 and At5g53300 and both family-13 UBC enzymes, encoded by At1g78870 and At16890
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[PUB54-RING domain-ubiquitin-carrier protein Ubc4/5]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[PUB54-RING domain-ubiquitin-carrier protein Ubc4/5]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
ubiquitination activity is seen with both family-4/5 UBC enzymes and both family-13 UBC enzymes
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[RFP1-ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [RFP1]-L-lysine
[RFP1-ubiquitin-carrier protein E2]-L-cysteine + [RFP1]-N6-ubiquitinyl-L-lysine
in the presence of ubiquitin, ATP, rabbit E1, human E2 and recombinant isoform RFP1, accumulation of high molecular weight ubiquitinated RFP1 is detected, indicating its ability to autoubiquitinate
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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
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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
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[RN181-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [RN181]-L-lysine
[RN181-ubiquitin-carrier protein]-L-cysteine + [RN181]-N6-ubiquitinyl-L-lysine
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in the presence of a ubiquitin-activating E1 enzyme, a ubiquitin-conjugating E2 enzyme, ubiquitin monomers and ATP, RN181 is self-ubiquitinated
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[RNF180-ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Zic2]-L-lysine
[RNF180-ubiquitin-carrier protein UbcH6]-L-cysteine + [Zic2]-N6-ubiquitinyl-L-lysine
Zic2, belongs to the Zic family nuclear zinc finger proteins
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[RNF220-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [RF220]-L-lysine
[RNF220-ubiquitin-carrier protein]-L-cysteine + [RNF220]-N6-ubiquitinyl-L-lysine
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isoform RNF220 can bind ubiquitin-conjugating enzyme and mediate auto-ubiquitination of itself
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[RNF220-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [Sin3B]-L-lysine
[RNF220-ubiquitin-carrier protein]-L-cysteine + [Sin3B]-N6-ubiquitinyl-L-lysine
Sin3B, a global regulator of gene transcription, which serves as an essential scaffold protein of the Sin3/HDAC corepressor complex
isoform RNF220 specifically interacts with Sin3B both in vitro and in vivo. Sin3B can be regulated by the ubiquitin-proteasome system. Co-expression of RNF220 and Sin3B promotes the ubiquitination and proteasomal degradation of Sin3B
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[RNF43-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [RNF43]-L-lysine
[RNF43-ubiquitin-carrier protein]-L-cysteine + [RNF43]-N6-ubiquitinyl-L-lysine
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
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formation of a ubiquitin dimer, where residue lysine48 is linked to the C-terminal carboxyl of another ubiquitin. The UBC7-dependent ubiquitinubiquitin 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
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the isolated TEB4 RING domain catalyses ubiquitin ligation in vitro in a reaction that is ubiquitin Lys48-specific and involves ubiquitin-conjugating enzyme UBC7
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[TRIM22-ubiquitin-carrier protein UbcH5B]-S-ubiquitinyl-L-cysteine + [TRIM22]-L-lysine
[TRIM22-ubiquitin-carrier protein UbcH5B]-L-cysteine + [TRIM22]-N6-ubiquitinyl-L-lysine
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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
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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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
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[ACRE276-RING domain-E3-ubiquitin-carrier protein HubC5B]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[ACRE276-RING domain-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
enzyme displays ubiquitination activity in the presence of yeast E1 and human E2 HubC5B
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[ACRE276-RING domain-E3-ubiquitin-carrier protein HubC5B]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[ACRE276-RING domain-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
enzyme displays ubiquitination activity in the presence of yeast E1 and human E2 HubC5B
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[ACRE276-RING domain-E3-ubiquitin-carrier protein HubC5B]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[ACRE276-RING domain-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
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enzyme displays ubiquitination activity in the presence of yeast E1 and human E2 HubC5B
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[E2 ubiquitin-conjugating enzyme UBCh5b]-S-ubiquitinyl-L-cysteine + [Ring]-L-lysine
[E2 ubiquitin-conjugating enzyme UBCh5b]-L-cysteine + [Ring]-N6-ubiquitinyl-L-lysine
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[E2 ubiquitin-conjugating enzyme UBCh5b]-S-ubiquitinyl-L-cysteine + [Ring]-L-lysine
[E2 ubiquitin-conjugating enzyme UBCh5b]-L-cysteine + [Ring]-N6-ubiquitinyl-L-lysine
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isoform ACRE276 is an E3 ubiquitin ligase requiring an intact U-box domain
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isoform ACRE276 is an E3 ubiquitin ligase requiring an intact U-box domain
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isoform RMA2 exhibits a high degree of E3 activity with E2 enzyme UBC8 and a moderate level with E2 enzyme UBC10 and no activity wih E2 enzymes UBC5 and UBC13
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isoform RMA2 exhibits a high degree of E3 activity with E2 enzyme UBC8 and a moderate level with E2 enzyme UBC10 and no activity wih E2 enzymes UBC5 and UBC13
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isoform RMA2 exhibits a high degree of E3 activity with E2 enzyme UBC8 and a moderate level with E2 enzyme UBC10 and no activity wih E2 enzymes UBC5 and UBC13
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ubiquitination activity of the fusion protein CaRING1-maltose-binding protein MBP are not displayed in the absence of E1, E2, E3, ATP or ubiquitin
ubiquitination activity of the fusion protein CaRING1-maltose-binding protein MBP is detected using anti-ubiquitin and anti-MBP antibody
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isoform GRN1 interacts with melanocortin receptor and decreases melanocortin receptors MC1R and MC4R signaling to cAMP. Inhibition of MC1R signaling by MGRN1 is not dependent on receptor down-regulation as a result of internalization or degradation. Receptor ubiquitylation is not a requisite for inhibition of signaling
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isoform GRN1 interacts with melanocortin receptor and decreases melanocortin receptors MC1R and MC4R signaling to cAMP. Inhibition of MC1R signaling by MGRN1 is not dependent on receptor down-regulation as a result of internalization or degradation. Receptor ubiquitylation is not a requisite for inhibition of signaling
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isoform RN181 interacts with the KVGFFKR region of platelet integrin alphaIIbbeta3. The integrin is not an endogenous substrate for RN181-directed ubiquitination
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isoform RN181 interacts with the KVGFFKR region of platelet integrin alphaIIbbeta3. The integrin is not an endogenous substrate for RN181-directed ubiquitination
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isoform RNF43 interacts with HAP95, a chromatin-associated protein interfacing the nuclear envelope. HAP95 is ubiquitinated and subjected to a proteasome-dependent degradation pathway, however, HAP95 is unlikely to serve as a substrate of RNF43 ubiquitin ligase
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in combination with E2 ubiquitin-conjugating enzyme UbcM2, only monoubiquitylation of the final substrate occurs. In presence of ubiquitin mutant K48R and UbcM2, enhanced polyubiquitin synthesizing activity is found. Reaction mixtures containing ubiquitin mutant K6R show a mild suppression of UbcM2 activity
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isoform RING1B acts in complex with polycomb group RING finger proteins PCGF. Complexes with PCGF4/BMI1 and PCGF2/Mel-18 support only low-level intrinsic RING1B activity in auto-ubiquitination or E2 discharge assays. A salt-bridge between K73D77 in RING1BPCGF4 both interferes sterically with the close approach of ubiquitin and limits the capacity of D77 to engage in alternative interactions. The low activity of the PCGF4RING1B heterodimer is offset by a relatively favourable interaction with nucleosome substrates, resulting in an efficient site-specific monoubiquitination
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isoform TRIM69 mediates ubiquitylation in an E2 conjugating enzyme selective fashion in vitro, leading to multiubiquitylated products. E2 enzymes UbcH6, UbcH2, UbcH5A UbcH5C, or UbcH13/UeV1a are required, no products are detected with other E2s tested, and presence of ATP is required. An intact RING finger domain is indispensible for the process. TRIM69 can mediate ubiquitination in vivo, which can be enhanced by a proteasome inhibitor
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additional information
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isoform TRIM69 mediates ubiquitylation in an E2 conjugating enzyme selective fashion in vitro, leading to multiubiquitylated products. E2 enzymes UbcH6, UbcH2, UbcH5A UbcH5C, or UbcH13/UeV1a are required, no products are detected with other E2s tested, and presence of ATP is required. An intact RING finger domain is indispensible for the process. TRIM69 can mediate ubiquitination in vivo, which can be enhanced by a proteasome inhibitor
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Parkin E3 ligase has autoubiquitination activity
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conjugation of RBX1 to NEDD8 substantially stimulates the reaction, by nearly 2000fold, activating both substrate-priming and chain-elongation reactions. Presence of NEDD8 coordinates ubiquitin ligation assembly
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no substrate: [E2 ubiquitin-conjugating enzyme UbcH5b]-S-ubiquitinyl-L-cysteine
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no substrate: [E2 ubiquitin-conjugating enzyme UbcH5b]-S-ubiquitinyl-L-cysteine
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isoform ACRE276 is an E3 ubiquitin ligase requiring an intact U-box domain
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additional information
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isoform ACRE276 is an E3 ubiquitin ligase requiring an intact U-box domain
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additional information
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degradation of the cytoplasmic misfolded protein DELTAssCL*myc, a derivative of signal sequence delted mutated carboxypeptidase yscY
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isoform ACRE276 is an E3 ubiquitin ligase requiring an intact U-box domain
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malfunction
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enzyme-impaired mutants show reduced sensitivity to low ambient temperature in flowering
malfunction
the atatl80 insertion mutant line exhibits an increased tolerance to cold stress
malfunction
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the idf1 mutants show increased tolerance to Fe deficiency, resulting from increased IRT1 protein levels
metabolism
isoform Kf-1 is a short-lived protein specifically destroyed by the ubiquitin proteasome system
metabolism
isoform RBCK1 undergoes efficient phosphorylation by protein kinase Cbeta. The phosphorylated RBCK1 shows no self-ubiquitination activity in vitro. Overexpression of protein kinase Cbeta leads to significant increases in the amounts of intracellular RBCK1, presumably suppressing the proteasomal degradation of RBCK1 through self-ubiquitination
metabolism
isoform TEB4 is an ER degradation substrate itself, promoting its own degradation in a RING finger- and proteasome-dependent manner
metabolism
the cognate E2 co-enzymes of E3 enzyme Parkin regulate the activation, translocation and enzymatic functions of Parkin during mitochondrial quality control. UBE2D family members and UBE2L3 redundantly charge the RING-HECT hybrid ligase Parkin with ubiquitin, resulting in its initial activation and translocation to mitochondria. UBE2N primarily mediates the proper clustering of mitochondria, a prerequisite for degradation. Depletion of UBE2R1 results in enhanced Parkin translocation and clustering upon mitochondrial uncoupling
physiological function
essential for hypersensitive response (HR) production. The CaRING1 expression triggers the hypersensitive cell death response. Transgenic Arabidopsis plants overexpressing CaRING1 also exhibit enhanced bacterial and fungal disease resistance, accompanied by the induction of salicylic acid against pathogen infection
physiological function
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protein quality control and subsequent elimination of terminally misfolded proteins is mediated by the ubiquitin-proteasome system. Ubr1, the N-end rule pathway E3 ligase is responsible for targeting misfolded cytoplasmic proteons to proteasomal degradation
physiological function
isoform ACRE276 RNA interference silencing in tobacco results in loss of hypersensitive response specified by Cf resistance genes. ACRE276 RNAi plants are also compromised for hypersensitive response mediated by the tobacco mosaic virus defense elicitor p50
physiological function
isoform GRN1 interacts with melanocortin receptor and decreases melanocortin receptors MC1R and MC4R signaling to cAMP. Inhibition of MC1R signaling by MGRN1 is not dependent on receptor down-regulation as a result of internalization or degradation. Receptor ubiquitylation is not a requisite for inhibition of signaling
physiological function
isoform TRIM25 is essential not only for retinoic-acid-inducible protein RIG-I ubiquitination but also for RIG-I-mediated interferon-beta production and antiviral activity in response to RNA virus infection
physiological function
overexpression of E3 ligase Pirh2 decreases DNA polymerase PolH protein stability, whereas knockdown of Pirh2 increases it. Pirh2 knockdown leads to accumulation of PolH and, subsequently, enhances the survival of UV-irradiated cells
physiological function
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silencing isoform ACRE276 leads to breakdown of Cf-9specified resistance against Cladosporium fulvum leaf mold
physiological function
transient expression of isoform PUB17 in Cf-9 tobacco silenced for ubiquitin ligase ACRE276 restores hypersensitive response, while mutant PUB17 lacking E3 ligase activity fails to do so. PUB17 ligase activity is crucial for defense signaling. PUB17 knockout plants are compromised in RPM1- and RPS4-mediated resistance against Pseudomonas syringae pv tomato containing avirulence genes AvrB and AvrRPS4, respectively
physiological function
C3H2C3-Type RING E3 ubiquitin ligase AIRP1-overexpressing transgenic plants (35S:AtAIRP1-sGFP) are hypersensitive to exogenous abscisic acid in terms of radicle emergence, cotyledon development, root elongation, and stomatal closure. Overexpressing transgenic plants accumulate higher amounts of hydrogen peroxide in response to exogenous abscisic acid than wild-type and mutant plants. AIRP1 overexpressors are markedly tolerant to severe drought stress, as opposed to mutant plants, which are highly susceptible. The levels of drought stress-related genes and basic leucine zipper transcription factor genes are up-regulated in overexpressing plants relative to wild-type and mutant plants in response to abscisic acid
physiological function
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C3HC4-type RING E3 ubiquitin ligase AIRP2-overexpressing transgenic and loss-of-function mutant plants exhibit hypersensitive and hyposensitive phenotypes, respectively, to abscisic acid in terms of seed germination, root growth, and stomatal movement. Overexpressing transgenic plants are highly tolerant to severe drought stress, and loss-of-function mutant alleles are more susceptible to water stress than are wild-type plants. Higher levels of drought-induced hydrogen peroxide production are detected in overexpressing mutant as compared with loss-of-function mutant plants. Abscisic acid-inducible drought-related genes are up-regulated in overexpressing and down-regulated in loss-of-function progeny. The positive effects of AIRP2 on abscisic acid-induced stress genes are dependent on SNF1-related protein kinases
physiological function
E3 RING ligase KEG acts as an important factor in plant hormone signaling and a positive regulator of jasmonate zim-domain JAZ12 stability. JAZ12 interacts directly with KEG. Abscisic acid treatment promotes JAZ12 degradation, and KEG knockdown leads to a decrease in JAZ12 protein levels
physiological function
heterogeneous overexpression of HIR1 in Arabidopsis thaliana leads to As- and Cd-insensitive phenotypes and results in decreased As and Cd accumulation in the shoots and roots
physiological function
heterogeneous overexpression of OsHCI1 in Arabidopsis highly increases survival rate through acquired thermotolerance
physiological function
in vivo degradation of substrates for integral endoplasmic reticulum membrane E3 ubiquitin ligase Doa10 is inhibitied by mutations in the alpha2 helix of E2 enzyme Ubc7 by preventing the conjugation of donor ubiquitin to the acceptor. Ubiquitin chain formation by mutant Ubc7 is not restored by the E3 enzyme Doa10 RING domain. alpha2 Helix mutations selectively impair the in vivo degradation of Doa10 substrates
physiological function
in vivo degradation of substrates for integral endoplasmic reticulum membrane E3 ubiquitin ligase Hrd1 is not impaired by mutations within helix alpha2 of ubiquitin-conjugating enzyme Ubc7. Ubiquitin-chain formation by mutant Ubc7 is restored selectively by the E3 enzyme Hrd1 RING domain
physiological function
isoform NERF is the cis-natural antisense transcript gene of NFYA5. NERF can produce siRNAs from their overlapping region and affect NFYA5 transcripts by functioning together with miR169. The NERF protein functions as an E3 ligase for ubiquitination. Overexpression of NERF or overlapping region cDNA leads to siRNA-NERF accumulation, miR169 repression, and NFYA5 transcript enhancement. Knockdown of NERF transcripts by an artificial miRNA enhances miR169 abundance and reduces NFYA5 transcripts
physiological function
loss-of-function mutant line shows hyposensitivity to abscisic acid during its germination stage. AIRP3 is idetical to Loss of Gdu2, LOG2, which participates in an amino acid export system. The knockout mutant and RNAi knockdown transgenic plants display impaired abscisic acid-mediated seed germination and stomata closure. Suppression of AIRP3 results in marked hypersensitive phenotypes toward high salinity and water deficit relative to wild-type plants
physiological function
loss-of-function mutant seedlings exhibit accelerated endocytosis in roots, and have altered expression of several genes involved in the membrane trafficking system. Protein trafficking inhibitor, brefeldin A, treatment leads to brefeldin A bodies in the mutant. The mutant also shows increased tolerance to salt, ionic and osmotic stresses, reduced accumulation of reactive oxygen species during salt stress, and increased expression of AtRbohD, which encodes a nicotinamide adenine dinucleotide phosphate oxidase involved in H2O2 production
physiological function
mutant sugar-insensitive3, i.e. Sis3 is resistant to the inhibitory effects of high concentrations of exogenous glucose and sucrose on early seedling development. In contrast to wild-type plants, sis3 mutants develop green, expanded cotyledons and true leaves when sown on medium containing high concentrations (e.g. 270 mM) of sucrose. Mutant Sis3 exhibits wild-type responses to the inhibitory effects of abscisic acid and paclobutrazol, a gibberellic acid biosynthesis inhibitor, on seed germination
physiological function
RING E3 ligase RGLG2 negatively regulates the drought stress response by mediating ERF53 transcriptional activity in Arabidopsis thaliana
physiological function
RING E3 Ligase Xbat32 mutants produce significantly more ethylene than wildtype plants and inhibition of ethylene biosynthesis or perception significantly increases Xbat32 lateral root production. Xbat32 interacts with the ethylene biosynthesis enzymes aminocyclopropane-1-carboxylic acid synthases ACS4 and ACS7 in yeast-two-hybrid assays and may negatively regulate ethylene biosynthesis by modulating the abundance of ACS proteins. Loss of Xbat32 may promote the stabilization of ACSs and lead to increased ethylene synthesis and suppression of lateral root formation. Auxin treatments only partially rescue the lateral root defect of Xbat32 mutants, but they completely restore wild-type levels of Xbat32 lateral root production when coupled with ethylene inhibition. Abscisic acid stimulates rather than inhibits mutant Xbat32 lateral root formation, and abscisic acid acts synergistically with auxin to promote mutant Xbat32 lateral root production
physiological function
RING finger E3 ligase RHA2b expression is induced by abscisic acid and overexpression of RHA2b leads to abscisic acid-associated phenotypes such as abscisic acid hypersensitivity in seed germination and seedling growth, enhanced stomatal closure, reduced water loss, and, therefore, increased drought tolerance. T-DNA insertion mutant Rha2b-1 shows abscisic acid-insensitive phenotypes and reduced drought tolerance. A Rha2a Rha2b-1 double mutant generally enhances abscisic acid insensitivity of mutant Rha2b-1 in seed germination, seedling growth, and stomatal closure, suggesting that Rha2b and Rha2a act redundantly in regulating abscisic acid responses
physiological function
RING finger E3 ligase RNF186 participates in the process of endoplasmic reticulum stress-mediated apoptosis. Overexpression of RNF186 stimulates upregulation of endoplasmic reticulum sensor proteins and rapid transmission of endoplasmic reticulum Ca2+ in Hela cells, while RNF186 knockdown leads to a moderate degree of resistance to endoplasmic reticulum stress. The half-life of substrate RNF186 is prolonged under endoplasmic reticulum stress, and the ubiquitination of BNip1 is greatly enhanced when endoplasmic reticulum stress occurs. Knockdown of BNip1 attenuates the stress signals at endoplasmic reticulum induced by RNF186
physiological function
RING-type E3 ligase KEG interacts directly with abscisic acid-responsive transcription factor ABI5 via its conserved C3 region. Interactions between KEG and ABI5 are observed in the cytoplasm and trans-Golgi network only when the RING domain of KEG is inactivated or when ABI5 is stabilized via mutations. Deletion of the C-terminal region of ABI5 or substituting lysine 344 for alanine prohibits protein turnover
physiological function
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suppression of expression of DAF, i.e. DEFECTIVE IN ANTHER DEHISCENCE1 (DAD1)-activating factor, causes non-dehiscence of the anthers, alters pollen development and causes sterility in 35S:DAF RNAi/antisense Arabidopsis plants. Ectopic expression of the dominant-negative C132S or H137Y mutations causes similar indehiscence of anthers and reduction in DAD1 expression in transgenic Arabidopsis thaliana
physiological function
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the RING domain is necessary for TRIM3-induced growth arrest of cells
physiological function
the RING-finger domain of March10a exhibits an E3 ubiquitin ligase activity along with the E2 ubiquitin-conjugating enzyme Ube2B. March10a undergoes proteasomal degradation by autoubiquitination in transfected COS7 cells, this activity is abolished upon microtubule disassembly
physiological function
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the enzyme activates plant defense responses by inducing proteolysis of the VpWRKY11 transcription factor. Enzyme overexpression in Arabidopsis confers enhanced resistance to the pathogens Golovinomyces cichoracearum and Pseudomonas syringae pv. tomato DC3000
physiological function
the enzyme activity is essential for DNA double-strand break signaling and necessary for downstream recruitment of 53BP1 and BRCA1 proteins
physiological function
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the enzyme acts as a positive regulator of absisic acid-mediated drought avoidance and a negative regulator of salt tolerance in Arabidopsis. Enzyme overexpression plants are hypersensitive to salt and osmotic stresses during seed germination, and show drought avoidance
physiological function
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the enzyme enhances heat tolerance by promoting H2O2-induced stomatal closure
physiological function
the enzyme is negatively correlated not only with phosphorus content and phosphorus utilization efficiency, but also with biomass and seed yield in Arabidopsis. Enzyme overexpression results in the delayed flowering time and decrease in seed yield in sufficient phosphate condition
physiological function
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the enzyme negatively regulates COP1 and SPA1 protein accumulation in darkness
physiological function
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the enzyme plays a role in rice antiviral defense at early stages of rice dwarf virus infection
physiological function
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the enzyme regulates the degradation of iron-regulated transporter1 in Arabidopsis
physiological function
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the enzyme regulates thermosensory flowering by triggering gigantea protein degradation
physiological function
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the enzyme targets SDIR1-interacting protein1 for degradation to modulate the salt stress response and abscisic acid signaling
physiological function
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AIR2 interacts with the 3-ketoacyl-CoA thiolase protein KAT1. AIR2 ubiquitinates KAT1 and promotes the degradation of KAT1 via the 26S proteasome degradation pathway. Overexpression of AIR2 in Arabidopsis improves the seed germination and increases the root length under arsenate stress conditions
physiological function
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cullin E3-ligase activity is necessary for entry into the terminal myogenic differentiation program and myotube formation. Cullin inhibition prevents entry into the terminal myogenic differentiation program, and satellite cells treated with inhibitor MLN4924 fail to differentiate. Protein levels of myogenic repressors Bhlhe41 and Id1, but not that of ZBTB38, are mediated through the activity of cullin E3-ligases
physiological function
DIR1-silenced pepper plants display a drought-tolerant phenotype characterized by a low level of transpirational water loss via increased stomatal closure and elevated leaf temperatures. DIR1-overexpressing Arabidopsis thaliana plants exhibit an abscisic acid-hypersensitive phenotype during the germination stage, but an abscisic acid-hyposensitive phenotype characterized by decreased stomatal closure and reduced leaf temperatures at the adult stage. Adult DIR1-overexpressing plants exhibit a drought-sensitive phenotype characterized by high levels of transpirational water loss
physiological function
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E3 ligase MIEL1 interacts with MYB1, regulator for anthocyanin accumulation. MIEL1 ubiquitinates MYB1 protein, followed by degradation through a 26S proteasome pathway. MIEL1 negatively regulates anthocyanin accumulation by modulating the degradation of MYB1 protein. Arabidopsis thaliana MIEL1 expression lines produce much less anthocyan than wild-type
physiological function
enzyme belongs to a family of E3 ligases with a RING-H2 domain related in sequence to the ATL and BTL RING-H2 domains. This family, named CTL, carries a motif YEELL that expands 21 amino acids next to the RING-H2 domain. E3 ubiquitin ligase BIG BROTHER is a plant CTL that regulates organ size
physiological function
enzyme belongs to a family of E3 ligases with a RING-H2 domain related in sequence to the ATL and BTL RING-H2 domains. This family, named CTL, carries a motif YEELL that expands 21 amino acids next to the RING-H2 domain. RNF111 is a SUMO-targeted ubiquitin ligase
physiological function
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enzyme is an E3 ubiquitin ligase and the RING finger conserved region is required for its activity. Silencing of Ring leads to increased sensitivity to salt stress in wild tomato. Overexpression of Ring in Arabidopsis thaliana results in enhanced salt tolerance during seed germination and early seedling development
physiological function
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heterogeneous overexpression of SIRP2 results in conferring tolerance against salinity and osmotic stress
physiological function
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in Arabidopsis thaliana overexpressing AIR1, the percentage of seedlings with expanded cotyledons is significantly higher in transgenic plants than in control plants in the presence of As-containing media. The root lengths of transgenic plants are significantly greater than those of the control wild-type plants when grown on 150 and 200 microM As-containing mediums, no differences are observed between the plants grown on the control medium
physiological function
isoform RCHY1 is an interacting partner of the viral SARS-unique domain (SUD) and papain-like protease (PLpro). Residues 95-144 of RCHY1 and 389-652 of SUD (SUD-NM) are crucial for interaction. Association with SUD increases the stability of RCHY1 and augments RCHY1-mediated ubiquitination as well as degradation of p53. The calcium/calmodulin-dependent protein kinase II delta (CAMK2D) also binds to SUD. The PLpros from SARSCoV, MERS-CoV, and HCoV-NL63 also physically interact with and stabilize RCHY1, and thus trigger degradation of endogenous p53. A SUD-PLpro fusion interacts with RCHY1 more intensively and causes stronger p53 degradation than SARS-CoV PLpro alone. p53 inhibits replication of infectious SARS-CoV as well as of replicons and human coronavirus NL63
physiological function
RFP1 is a functional RING E3 ubiquitin ligase that mediates ubiquitination of protein betaC1 from Tomato yellow leaf curl China virus-associated betasatellite. betaC1 is ubiquitinated in vivo and degraded by the plant 26S proteasome. After viral infection, plants overexpressing RFP1 develop attenuated symptoms, whereas plants with silenced expression of RFP1 show severe symptoms
physiological function
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RING E3 ligase PIR2 interacts with protein phosphatase PP2CA. A PIR2 knockout mutant does not display altered response to abscisic acid, the PIR1-1/PIR2 double mutant becomes more insensitive to abscisic acid than the wild-type or PIR1-1 and PIR2 single mutants
physiological function
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splicing isoform PIR1.2 exhibits E3 ligase activity and determines protein phosphatase PP2CA's stability in the presence of abscisic acid. The PIR1 knockout mutant displays an abscisic acid-hyposensitive phenotype. A PIR1-1/PIR2 double mutant becomes more insensitive to abscisic acid than the wild-type or PIR1-1 and PIR2 single mutants
physiological function
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the expression of transcription factor WRKY22 and RING-type ubiquitin ligase HOS1 is upregulated in the priming resistance of peach fruit against Rhizopus stolonifer. The two proteins physically interact in vivo
physiological function
the identity of residues at specific positions in the RING domain can tune activity levels up or down. Substitutions may create a structurally intact BRCA1/BARD1 heterodimer that is inactive in vitro with all E2 enzymes. Substitutions in BRCA1 or BARD1 RING domains may result in hyperactivity, as both proteins have evolved attenuated activity. Loss of attenuation results in decreased product specificity
physiological function
the RING domain of E3 ligase ZNRF1 binds Ube2N with a Kd of about 50 nM. ZNRF1 interacts with Ube2D2 with a Kd of about 1 mM. The ubiquitination efficiency of ZNRF1:E2 pairs correlates with their affinity. An excess of ZNRF1 inhibits Ube2N-mediated ubiquitination at concentrations at or above 500 nM instead of showing enhanced ubiquitination
physiological function
tobacco leaf-produced EMR mediates mildew resistance locus O-12 degradation in a proteasome-dependent manner. EMR forms a complex with ubiquitin-conjugating enzyme UBC32. Mutation of EMR and RNAi increase the tolerance of plants to endoplasmic reticulum stress. EMR RNAi in a brassinosteroid signaling mutant protein background, leads to partial recovery of the brassinosteroid insensitive phenotypes as compared with the original mutant plants and increased ER stress tolerance
physiological function
Ube4A is required for complete assembly of specific DNA damage repair factors at double-strand break sites and proper internal organization of double-strand break-associated protein foci. UBE4A's recruitment to sites of DNA damage is dependent on primary E3 ligases in the DNA damage repair and promotes enhancement and sustainment of K48- and K63-linked ubiquitin chains at these sites. This step is required for timely recruitment of the RAP80 and BRCA1 proteins and proper organization of RAP80- and BRCA1-associated protein complexes at double-strand break sites. The pathway is required for optimal end-resection at double-strand breaks, and its abrogation leads to up-regulation of the highly mutagenic alternative end-joining repair at the expense of error-free homologous recombination repair
physiological function
UFD-2 is a mediator of DNA-damage-induced apoptosis. After initiation of homologous recombination by RAD-51, UFD-2 forms foci that contain substrate-processivity factors including the ubiquitin-selective segregase CDC-48 (p97), the deubiquitination enzyme ATX-3 (Ataxin-3) and the proteasome. In the absence of UFD-2, RAD-51 foci persist, and DNA damage-induced apoptosis is prevented. UFD-2 foci are retained until recombination intermediates are removed by the Holliday-junction-processing enzymes GEN-1, MUS-81 or XPF-1. Formation of UFD-2 foci also requires proapoptotic CEP-1 (p53) signaling
physiological function
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enzyme is an E3 ubiquitin ligase and the RING finger conserved region is required for its activity. Silencing of Ring leads to increased sensitivity to salt stress in wild tomato. Overexpression of Ring in Arabidopsis thaliana results in enhanced salt tolerance during seed germination and early seedling development
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Plant Cell
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Homo sapiens (P38398), Homo sapiens (Q00987), Homo sapiens (Q13489)
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Suisse, A.; Bekes, M.; Huang, T.T.; Treisman, J.E.
The COP9 signalosome inhibits Cullin-RING E3 ubiquitin ligases independently of its deneddylase activity
Fly
12
118-126
2018
Mus musculus
brenda
Joo, H.; Lim, C.; Han, S.; Lee, S.
The pepper RING finger E3 ligase, CaDIR1, regulates the drought stress response via ABA-mediated signaling
Front. Plant Sci.
8
690
2017
Capsicum annuum (A0A2Z2GVU4)
brenda
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
brenda
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
brenda
An, J.; Liu, X.; Song, L.; You, C.; Wang, X.; Hao, Y.
Apple RING finger E3 ubiquitin ligase MdMIEL1 negatively regulates salt and oxidative stresses tolerance
J. Plant Biol.
60
137-145
2017
Malus domestica
brenda
Hwang, S.; Park, H.; Han, A.; Jang, C.
Molecular characterization of Oryza sativa arsenic-induced RING E3 ligase 1 (OsAIR1) Expression patterns, localization, functional interaction, and heterogeneous overexpression
J. Plant Physiol.
191
140-148
2016
Oryza sativa Japonica Group
brenda
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)
brenda
Shen, Q.; Hu, T.; Bao, M.; Cao, L.; Zhang, H.; Song, F.; Xie, Q.; Zhou, X.
Tobacco RING E3 ligase NtRFP1 mediates ubiquitination and proteasomal degradation of a geminivirus-encoded betaC1
Mol. Plant
9
911-925
2016
Nicotiana tabacum (R4SB05), Nicotiana tabacum
brenda
Ackermann, L.; Schell, M.; Pokrzywa, W.; Kevei, E.; Gartner, A.; Schumacher, B.; Hoppe, T.
E4 ligase-specific ubiquitination hubs coordinate DNA double-strand-break repair and apoptosis
Nat. Struct. Mol. Biol.
23
995-1002
2016
Caenorhabditis elegans (Q09349), Caenorhabditis elegans
brenda
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)
brenda
Park, J.H.; Kang, C.H.; Nawkar, G.M.; Lee, E.S.; Paeng, S.K.; Chae, H.B.; Chi, Y.H.; Kim, W.Y.; Yun, D.J.; Lee, S.Y.
EMR, a cytosolic-abundant ring finger E3 ligase, mediates ER-associated protein degradation in Arabidopsis
New Phytol.
220
163-177
2018
Arabidopsis thaliana (A0A178UZG1)
brenda
Hwang, S.G.; Chapagain, S.; Han, A.R.; Park, Y.C.; Park, H.M.; Kim, Y.H.; Jang, C.S.
Molecular characterization of rice arsenic-induced RING finger E3 ligase 2 (OsAIR2) and its heterogeneous overexpression in Arabidopsis thaliana
Physiol. Plant.
161
372-384
2017
Oryza sativa Japonica Group
brenda
Qi, S.; Lin, Q.; Zhu, H.; Gao, F.; Zhang, W.; Hua, X.
The RING finger E3 Ligase SpRing is a positive regulator of salt stress signaling in salt-tolerant wild tomato species
Plant Cell Physiol.
57
528-539
2016
Solanum pimpinellifolium, Solanum pimpinellifolium PI365967
brenda
Baek, W.; Lim, C.; Luan, S.; Lee, S.
The RING finger E3 ligases PIR1 and PIR2 mediate PP2CA degradation to enhance abscisic acid response in Arabidopsis
Plant J.
100
473-486
2019
Arabidopsis thaliana
brenda
Chapagain, S.; Park, Y.; Kim, J.; Jang, C.
Oryza sativa salt-induced RING E3 ligase 2 (OsSIRP2) acts as a positive regulator of transketolase in plant response to salinity and osmotic stress
Planta
247
925-939
2018
Oryza sativa
brenda
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
Arabidopsis thaliana (Q8L649), Homo sapiens (Q6ZNA4)
brenda
Li, C.; Wang, J.; Ji, N.; Lei, C.; Zhou, D.; Zheng, Y.; Wang, K.
PpHOS1, a RING E3 ubiquitin ligase, interacts with PpWRKY22 in the BABA-induced priming defense of peach fruit against Rhizopus stolonifer
Postharvest Biol. Technol.
159
111029
2020
Prunus persica
-
brenda
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)
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brenda
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
brenda
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
brenda
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)
brenda