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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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additional information
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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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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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isoform ACRE276 is an E3 ubiquitin ligase requiring an intact U-box domain
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additional information
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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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additional information
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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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additional information
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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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additional information
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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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additional information
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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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additional information
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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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additional information
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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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additional information
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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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additional information
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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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additional information
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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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additional information
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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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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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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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additional information
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Parkin E3 ligase has autoubiquitination activity
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additional information
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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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additional information
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no substrate: [E2 ubiquitin-conjugating enzyme UbcH5b]-S-ubiquitinyl-L-cysteine
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additional information
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no substrate: [E2 ubiquitin-conjugating enzyme UbcH5b]-S-ubiquitinyl-L-cysteine
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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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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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additional information
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isoform ACRE276 is an E3 ubiquitin ligase requiring an intact U-box domain
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