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Literature summary for 2.3.2.25 extracted from

  • Xu, H.; Shi, J.; Gao, H.; Liu, Y.; Yang, Z.; Shao, F.; Dong, N.
    The N-end rule ubiquitin ligase UBR2 mediates NLRP1B inflammasome activation by anthrax lethal toxin (2019), EMBO J., 38, e101996 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.2.25

Cloned(Commentary)

Cloned (Comment) Organism
gene UBE2O, recombinant coexpression of Myc-tagged UBE2O and Flag-tagged UBR2 in HEK-293T cells Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information generation of E2-knockdown macrophages, siRNA knockdown of Ube2o expression in engineered RAW-RA cells, Ube2o knockdown efficiency is measured by quantitative PCR Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
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 Mus musculus 5829
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid Mus musculus
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 [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
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 ?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-amino acid Mus musculus NLRP1B inflammasome is ubiquitinylated at the N-terminal Leu248 [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]
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 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q6ZPJ3
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Source Tissue

Source Tissue Comment Organism Textmining
macrophage
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 Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
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 Mus musculus [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
-
 ?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-amino acid NLRP1B inflammasome is ubiquitinylated at the N-terminal Leu248 Mus musculus [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]
-
 ?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-leucine248 NLRP1B inflammasome Mus musculus [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]
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 ?

Synonyms

Synonyms Comment Organism
E2 ubiquitin-conjugating enzyme
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 Mus musculus
UBE2O
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 Mus musculus

General Information

General Information Comment Organism
malfunction knockdown of two E2s, Ube2o or Ube2t (EC 2.3.2.23), appears to be capable of suppressing LT-stimulated caspase-1 activation. siRNA knockdown of Ube2o expression in the engineered RAW-RA cells efficiently blocks RFP-ASC specks formation as well as release of cellular EGFP in response to LT stimulation Mus musculus
metabolism the N-end rule E3 ligase UBR2 is required for LT-induced NLRP1B inflammasome activation. LT is known to cleave NLRP1B after Lys44. The cleaved NLRP1B, bearing an N-terminal leucine, is targeted by UBR2-mediated ubiquitination and degradation. UBR2 partners with the E2 ubiquitin-conjugating enzyme UBE2O in this process. NLRP1B undergoes constitutive autocleavage before the C-terminal CARD domain. UBR2-mediated degradation of LT-cleaved NLRP1B thus triggers release of the noncovalent-bound CARD domain for subsequent caspase-1 activation. Metabolic pathway, overview Mus musculus
physiological function UBE2O can mediate the ubiquitination of many different substrates. It is involved in cancer. UBE2O may also regulate other biological processes through UBR2-dependent or UBR2-independent N-end rule pathways. The E2 ubiquitin-conjugating enzyme UBE2O partners with UBR2, an E3 ubiquitin ligase of the N-end rule degradation pathway. UBR2 functions together with UBE2O mediating NLRP1B inflammasome activation. UBE2O is the bona fide E2 enzyme controlling LT-induced NLRP1B inflammasome activation. UBR2-UBE2O ubiquitination pathway mediates degradation of LT-cleaved NLRP1B, which releases its C-terminal CARD domain for subsequent caspase-1 activation Mus musculus