Information on EC 2.3.2.27 - RING-type E3 ubiquitin transferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.2.27
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RECOMMENDED NAME
GeneOntology No.
RING-type E3 ubiquitin transferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
protein ubiquitylation
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SYSTEMATIC NAME
IUBMB Comments
S-ubiquitinyl-[ubiquitin-conjugating E2 enzyme]-L-cysteine:acceptor protein ubiquitin transferase (isopeptide bond-forming; RING-type)
The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopetide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein. The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
isoform CHIP
UniProt
Manually annotated by BRENDA team
isoform RFP1
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
isoform ACRE276
SwissProt
Manually annotated by BRENDA team
Chinese wild grapevine, cultivar Carignane
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 [gp78-ubiquitin-carrier protein Ub2g2]-S-ubiquitinyl-L-cysteine
[gp78-ubiquitin-carrier protein Ub2g2]-S-[ubiquitinyl-N6-ubiquitinyl-L-lysine46]-L-cysteine
show the reaction diagram
use of mouse Ube2g2 ubiquitin conjugating enzyme. Ube2g2/gp78-mediated polyubiquitination involves preassembly of Lys 48-linked ubiquitin chains at the catalytic cysteine residue C89 of Ube2g2. The growth of Ube2g2-anchored ubiquitin chains seems to be mediated by an aminolysis-based transfer reaction between two Ube2g2 molecules that each carries a ubiquitin moiety in its active site. Polyubiquitination of a substrate can be achieved by transferring preassembled ubiquitin chains from Ube2g2 to a lysine residue in a substrate
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?
S-(ubiquitin)n-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [POX1]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-(ubiquitin)n-[POX1]-L-lysine
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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human T lymphotropic virus type 1 trans-activator/oncoprotein Tax greatly stimulates RNF8 and Ubc13:Uev1A/Uev2 to assemble long K63-polyubiquitin chains
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?
S-(ubiquitin)n-[UbcH5]-L-cysteine + [STRF1]-L-lysine
[UbcH5]-L-cysteine + N6-(ubiquitin)n-[STRF1]-L-lysine
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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
show the reaction diagram
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ACS4]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ACS4]-L-lysine
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
BNip1 is a Bcl-2 family protein
BNip1 is polyubiquitinated by isoform RNF186 through K29 and K63 linkage in vivo. This modification promotes BNip1 transportation to mitochondria but has no influence on its protein level
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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
show the reaction diagram
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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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?
S-ubiquitinyl-[UbcH5b]-L-cysteine + [DAF]-L-lysine
[UbcH5b]-L-cysteine + N6-ubiquitinyl-[DAF]-L-lysine
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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
show the reaction diagram
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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
show the reaction diagram
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?
S-ubiquitinyl-[Ube2B]-L-cysteine + [March10a]-L-lysine
[Ube2B]-L-cysteine + N6-ubiquitinyl-[March10a]-L-lysine
show the reaction diagram
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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
show the reaction diagram
[BRCK1-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [BRCK1]-L-lysine
[BRCK1-ubiquitin-carrier protein]-L-cysteine + [BRCK1]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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?
[CDC34]-S-ubiquitinyl-L-cysteine + [SCF]-L-lysine
[CDC34]-L-cysteine + [SCF]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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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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[gp78-ubiquitin-carrier protein Ub2g2]-S-(ubiquitin)x-L-cysteine + HERP-L-lysine
[gp78-ubiquitin-carrier protein Ub2g2]-L-cysteine + HERP-N6-(ubiquitin)x-L-lysine
show the reaction diagram
HERP, ER-associated, short-lived protein that interacts with several E3 enzymes. Use of mouse Ube2g2 ubiquitin conjugating enzyme. Ube2g2/gp78-mediated polyubiquitination involves preassembly of Lys 48-linked ubiquitin chains at the catalytic cysteine of Ube2g2. The growth of Ube2g2-anchored ubiquitin chains seems to be mediated by an aminolysis-based transfer reaction between two Ube2g2 molecules that each carries a ubiquitin moiety in its active site. Polyubiquitination of a substrate can be achieved by transferring preassembled ubiquitin chains from Ube2g2 to a lysine residue in a substrate
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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
show the reaction diagram
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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
show the reaction diagram
PolH, DNA polymerase eta, a Y family translesion polymerase and a target of the p53 tumor suppressor. PolH interacts with Pirh2 E3 ligase, via the polymerase-associated domain in PolH and the RING finger domain in Pirh2. PolH is recruited by Pirh2 and degraded by 20S proteasome in a ubiquitin-independent manner
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[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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
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
show the reaction diagram
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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
show the reaction diagram
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
show the reaction diagram
isoform RNF43 has autoubiquitylation activity. RNF43 is a RING finger-dependent E3 ligase that is selective for E2 enzymes UbcH5b and UbcH5c
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[TEB4-UBC7]-S-ubiquitinyl-L-cysteine + ubiquitin-L-lysine48
[TEB4-UBC7]-L-cysteine + ubiquitin-N6-ubiquitinyl-L-lysine48
show the reaction diagram
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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 ubiquitin–ubiquitin linkage reaction requires the presence of the ubiquitin-activating enzyme E1 and ATP, suggesting that the activity requires the intermediate formation of an UBC7-ubiquitin thioester
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[TEB4-UBC7]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[TEB4-UBC7]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
show the reaction diagram
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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
show the reaction diagram
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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
show the reaction diagram
TRIM5 functions as a RING-finger-type E3 ubiquitin ligase both in vitro and in vivo and ubiquitinates itself in cooperation with the E2 ubiquitin-conjugating enzyme UbcH5B. TRIM5 is monoubiquitinated, and ubiquitination does not lead to proteasomal degradation. Monoubiquitination may be a signal for TRIM5 to translocate from cytoplasmic bodies to the cytoplasm
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additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme Ubc13]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme Ubc13]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
show the reaction diagram
O76064
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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
show the reaction diagram
Q9Y4X5
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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
show the reaction diagram
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [SDIRIP1 protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[SDIRIP1 protein]-L-lysine
show the reaction diagram
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[RING-E3-ubiquitin-carrier protein TRIM25]-S-ubiquitinyl-L-cysteine + [RIG-I]-L-lysine
[RING-E3-ubiquitin-carrier protein TRIM25]-L-cysteine + [RIG-I]-N6-ubiquitinyl-L-lysine
show the reaction diagram
Q14258
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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
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additional information
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Parkin E3 ligase has autoubiquitination activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
ubiquitination in the platelet is modulated by elevated intracellular calcium level
Zinc
two Zn2+-binding sites are present involving four cysteine residues found in the loops between beta1-beta2 and beta3-beta4 at site I, residues C344, C347, C362, C367, and three cysteines and a histidine in the extended loop after beta4 at site II, residues C372, C375, H382, C389
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
E3 ubiquitin ligase activity of isoform RBCK1 is inhibited by interaction with splice variant RBCK2
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
presence of ATP is required for catalysis
PINK1
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Parkin activation as an E3 ubiquitin ligase is regulated by PTEN-induced putative kinase 1
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
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calculated from amino acid sequence
6.8
calculated
8.86
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
abundantly expressed
Manually annotated by BRENDA team
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highest expression
Manually annotated by BRENDA team
developing lens
Manually annotated by BRENDA team
abundantly expressed
Manually annotated by BRENDA team
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weakest expression
Manually annotated by BRENDA team
March10 is specifically expressed in elongating and elongated spermatids
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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cytosol of chloroplast
Manually annotated by BRENDA team
mainly associated with the Golgi apparatus and moves rapidly and extensively along the cytoskeleton
Manually annotated by BRENDA team
upon overexpression in COS7 cell
Manually annotated by BRENDA team
additional information
isoform TEB4 is notexpressed at the cell surface
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20570
calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
ubiquitination
additional information
enzyme is N-terminally mono-ubiquitinated by the ubiquitin conjugating enzyme Ubc16
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.9 A crystal structure of the ubiquitin ligase CHIP U-box domain complexed with UbcH5a. CHIP binds to UbcH5 and Ubc13 through similar specificity determinants located on the long loops and central helix of the CHIP U-box, and on the N-terminal helix and loops L4 and L7 of its cognate E2 enzymes including a key S-P-A motif. The determinants make different relative contributions to the overall interactions between CHIP and the two E2 enzymes. CHIP undergoes auto-ubiquitination by UbcH5 but not by Ubc13-Uev1a. Instead, CHIP drives the formation of unanchored polyubiquitin by Ubc13-Uev1a. CHIP also interacts productively with the class III E2 enzyme Ube2e2
crystallization of isoform parkin protein residues 141-465 including RING 0 and RING-between-RING domains. The protein is assembled into two compact domain groups separated by linkers. The catalytic network consists of residues C431 and H433. Parkin functions as a RING/HECT hybrid ubiquitin ligase
hanging drop vapor diffusion method, using either 1.0-1.4 M potassium/sodium tartrate /0.1M CHES pH 9.5 /0.2M LiSO4, or 0.5-0.55 M trisodium citrate/0.1 M citric acid pH 5.2/0.2 M lithium acetate, at room temperature
heterodimeric structure of the complex of Ring1b and Bmi1. Complex formation depends on an N-terminal arm of Ring1b that embraces the Bmi1 Ring-domain. Catalytic activity resides in Ring1b and not in Bmi1
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in complex with polycomb group RING finger proteins PCGF5 or PCGF4 and E2 enzyme UbcH5. RING1B binds directly to UbcH5c, with the PCGF partner making no contacts with the E2. The catalytically critical hydrogen bond between RING1B R91 and the backbone carbonyl of UbcH5c Q92 is present in both the structures, consistent with an activated conformation of the E2. Differences between the PCGF4 and PCGF5 ternary complex structures are found at the N termini of the PCGF and RING1B
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RNF8(345-485)/Ubc13-Ub complex, hanging drop vapor diffusion method, using
solution structure of the isoform HHARI RING2 domain, the key portion of this E3 ligase required for the RING/HECT hybrid mechanism. The domain possesses two Zn2+-binding sites and a single exposed cysteine used for ubiquitin catalysis. A structural comparison of the RING2 domain with the HECT E3 ligase NEDD4 reveals a near mirror image of the cysteine and histidine residues in the catalytic site. A tandem pair of aromatic residues exists near the C-terminus of the HHARI RING2 domain that is conserved in other RING-in-Between-RING E3 ligases
the K3 N-terminal domain is a variant member of the RING domain family and not a plant homeodomain. The domain interacts with the cellular ubiquitin-conjugating enzymes UbcH5A to -C and UbcH13, which dock to the equivalent surface as on classical cellular RING domains. May be involved in catalyzing Lys63-linked ubiquitination
isoform Rnf4 trimeric complex with UbcH5a and ubiquitin. E2 enzyme UbcH5a is linked by an isopeptide bond to ubiquitin. UbcH5a contacts a single protomer of the RING, and ubiquitin is folded back onto the UbcH5a by contacts from both RING protomers. The C-terminal tail of ubiquitin is locked into an active site groove on UbcH5a by an intricate network of interactions, resulting in changes at the UbcH5a active site
structure of fragment Prp19(1-133), which contains both the N-terminal U-box and central coiled-coil domain, to 1.38 A resolution. The Prp19 U-box domain exists in a dimeric state in the context of intact Prp19. The hydrophobic character of the dimer interface is due to residues Leu15, Ile22, Val51, and Ile53. All four positions are conserved long-chain hydrophobic residues
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose bead chromatography
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recombinant fusion protein CaRING1-maltose-binding protein MBP, cell lysis, affinity chromatography of the the soluble fraction
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in a wheat germ cell-free system
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expressed in Escherichia coli (BL21) as a fusion protein with maltose-binding protein MBP
expressed in Escherichia coli Rosetta cells
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expressed in HEK-293T and HeLa cells
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expressed in Nicotiana benthamiana and Escherichia coli Rosetta (DE3) cells
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expressed in onion epidermal cells and Arabidopsis thaliana
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expressed in yeast or Xenopus laevis oocytes
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expression in COS-7 cell and 293-T cell
expression in Escherichia coli
expression in Eschericia coli
expression in HEK-293 cell
expression in HEK-293T cell
expression in HEK-293T cell and HBL human melanoma cell
expression in HeLa cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced by powdery mildew
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expression is highly induced by heat and cold
expression is induced by avirulent Xanthomonas campestris pv vesicatoria infection
expression is induced by drought stress
expression is markedly induced by abscisic acid and dehydration stress
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expression is significantly induced by abscisic acid and drought stress
expression is up-regulated by gamma rays irradiation
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expression of isoform ACRE276 is transiently induced in wounded leaves within 15 min, but upon Avr9 elicitor treatment, this upregulation is enhanced and maintained until cell death onset
human melanoma cells express four MGRN isoforms
Rha2b expression is induced by abscisic acid and drought stress
TEB4 expression does not increase in response to the various stress conditions
the enzyme expression is induced strongly (22fold) by 0.1 mM abscisic acid after 12 h. The enzyme is slightly induced (2-4fold) by heat (45°C), cold (4°C), NaCl (250 mM), PEG (20% (w/v)), and H2O2 (100 mM) treatments
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the enzyme is upregulated by 10 days low phosphate (0-02 mM KH2PO4) conditions
the gene encoding RNF43 is upregulated in colon adenocarcinoma as well as in colon adenoma
the transcription level can be induced by absisic acid (0.1 mM), heat (37°C), osmotic (300 mM mannitol) and oxidative stresses (20 mM H2O2)
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trancription is downregulated by cold and drought treatments
trancription is upregulated by abscisic acid and salt stress
transcript levels of AIRP3 are up-regulated by drought, high salinity, and abscisic acid
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C132S
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mutation in the RING domain, loss of E3 ubiquitin ligase activity
C367S
mutation within RING finger domain, mutant protein does not display significant ubiquitin ligase activity
C36S
mutation in conserved residue of RING motif. Ser substitution strongly diminishes the ubiquitin ligase activity
C59S
mutation of conserved residue of RING motif. Ser substitution strongly diminishes the ubiquitin ligase activity
C63S
mutation of conserved residue of RING motif. Ser substitution strongly diminishes the ubiquitin ligase activity
H137Y
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mutation in the RING domain, loss of E3 ubiquitin ligase activity
H348Y
mutation within RING finger domain, mutant protein does not display significant ubiquitin ligase activity
W266H
mutation results in loss of activity with family 13 Ubc enzymes
C194S
mutation in highly conserved residue, loss of ubiqitin ligase activity
C197S
mutation in highly conserved residue, loss of ubiqitin ligase activity
A46P
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the mutant shows barely detectable autoubiquitination activity compared to the wild type
C11A
mutation introduced to reduce the stability of the RING domain, poor activity
C15A
mutation in the conserved RING-finger domain, loss of autoubiquitination ability
C431A
mutation eliminates parkin-catalyzed degradation of mitochondria
C61A/C64A
mutation of two adjacent cysteine residues at the conserved zinc-binding position, mutant shows weak activity
C9A
mutation within the RING domain of TEB4, strongly impairs its own degradation
D67E
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mutation identified in Thai familial breast cancer patients. The mutation is located in the vicinity of Zn2+ binding site II. The D67E BRCA1 RING protein assumes a preformed structure in the absence of Zn2+. The Zn2+-bound mutant protein is more folded than wild-type, resulting in enhanced proteolytic resistance and dimerization. The mutation retains Zn2+ binding, and barely perturbs the native global structure of the BRCA1 RING domain. The D67E mutation might be a neutral or mild cancer-risk modifier of other defective mechanisms underlying BRCA1-mutation-related breast cancer
I53A
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the Ring1b/Bmi1 complex with an I53A mutation in Ring1b has almost no catalytic activity
K27N
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the mutant shows barely detectable autoubiquitination activity compared to the wild type
K48A
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the mutant has higher autoubiquitination activity than the wild type
L451D
the mutation causes a drastic decrease in the ability of the enzyme to stimulate Ubc13
R33Q
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the mutant shows barely detectable autoubiquitination activity compared to the wild type
R42P
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the mutant has higher autoubiquitination activity than the wild type
R441A
the mutation has little effect on the enzyme activity
S17D
phosphomimetic mutation, stimulates MDM2-mediated polyubiquitination of p53. The stimulation is independent of p53 substrate. Mutation alters the conformation of the isolated N-terminus, it induces increased thermostability of the isolated N-terminal domain, it stimulates the allosteric interaction of MDM2 with the DNA-binding domain of p53 and it stimulates a protein-protein interaction with the E2-ubiquitin complex in the absence of substrate p53 that, in turn, increases hydrolysis of the E2-ubiquitin thioester bond
T240R
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the mutant shows barely detectable autoubiquitination activity compared to the wild type
Y268E
no increased activity compared to unphosphorylated wild-type
Y268F
residue Y268 is not required for phosphorylation-induced activation
Y274E
slightly increased activity compared to unphosphorylated wild-type
Y291E
no increased activity compared to unphosphorylated wild-type
Y307E
strongly increased activity compared to unphosphorylated wild-type
Y337E
strongly increased activity compared to unphosphorylated wild-type
Y371E
mutant shows constitutive E3 ubiquitin ligase activity while retaining the ability to bind epidermal growth factor receptor. The Y371E mutant also has altered protease sensitivity, resembling the proteolytic pattern seen with tyrosine-phosphorylated c-Cbl wild-type; strongly increased activity compared to unphosphorylated wild-type
C172A
mutation in the RING domain, mutant does not show autoubiquitylation
C196A
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amino acid substitution of the RING domain, complete loss of E3 ligase activity
K118R
residue Lys118 is required for Ubc7 activity. Mutant is very poor in assembly of polyubiquitin chains. Lys118 is both essential and sufficient for Doa10-mediated degradation of substrates; residue Lys118 is required for Ubc7 activity. Mutant is very poor in assembly of polyubiquitin chains. Lys118 is both essential and sufficient for Doa10-mediated degradation of substrates
L15E
mutant in U-box domain interface, abrogates U-box dimer formation and is lethal in vivo
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
Show Disease (13655 entries)
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