Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme.
NCU04302 E2 comparison results
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The report supports the Ubc9 assignment in combination with PAINT and UBC-domain evidence, and explains why homology to an Arabidopsis ubiquitin E2 does not support retaining ubiquitin-transfer specificity.
"The much broader E2 fold also encompasses ubiquitin E2s, explaining why a homologous donor does not justify retaining its modifier specificity."
Characterization of SUMO-conjugating enzyme mutants in Schizosaccharomyces pombe identifies a dominant-negative allele that severely reduces SUMO conjugation.
SUMO modification of Rad22, the Schizosaccharomyces pombe homologue of the recombination protein Rad52.
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Purified fission-yeast Hus5 (Ubc9) is the conjugator required, with the Rad31/Fub2 E1, for in vitro Pmt3 (SUMO) modification, and hus5 mutants are sensitive to DNA damaging agents.
"The Pmt3 modification that we detect requires the presence of added Pmt3-GG (the mature form of Pmt3), the activator (Rad31 + Fub2) and the conjugator, Hus5."
SUMO modification is involved in the maintenance of heterochromatin stability in fission yeast.
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Fission-yeast Hus5/Ubc9 binds Swi6, Chp2 and Clr4 and is enriched at heterochromatin by ChIP in a heterochromatin-dependent manner.
"Hus5 was highly enriched in heterochromatic regions in a heterochromatin-dependent manner"
Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction.