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Literature summary for 2.3.2.26 extracted from

  • Braganza, A.; Li, J.; Zeng, X.; Yates, N.; Dey, N.; Andrews, J.; Clark, J.; Zamani, L.; Wang, X.; St Croix, C.; OSullivan, R.; Garcia-Exposito, L.; Brodsky, J.; Sobol, R.
    UBE3B is a calmodulin-regulated, mitochondrion-associated E3 ubiquitin ligase (2017), J. Biol. Chem., 292, 2470-2484 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Ca2+ when the concentration of calcium is increased, calmodulin is released from UBE3B, resulting in an increase in ubiquitylation activity Homo sapiens

Protein Variants

Protein Variants Comment Organism
C1036A loss of ubiquitylation activity Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Calmodulin UBE3B interacts with calmodulin via its N-terminal isoleucine-glutamine motif. Deletion of the motif (amino acids 29-58) results in loss of calmodulin binding and a significant increase in the in vitro ubiquitylation activity of UBE3B. Changes in calcium levels in vitro disrupt the calmodulin-UBE3B interaction Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion mitochondrion-associated protein Homo sapiens 5739
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q7Z3V4 isoform UBE3B
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information UBE3B shows HECT E3 ubiquitin ligase activity and exhibits time-dependent auto-ubiquitylation activity Homo sapiens ?
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-

Synonyms

Synonyms Comment Organism
UBE3B
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Homo sapiens

General Information

General Information Comment Organism
physiological function mutating the catalytic cysteine or deleting the entire HECT domain (amino acids 758-1068) results in loss of UBE3B's ubiquitylation activity. Knockdown of UBE3B in human cells induces changes in mitochondrial morphology and physiology, a decrease in mitochondrial volume, and a severe suppression of cellular proliferation Homo sapiens