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Literature summary for 2.3.2.27 extracted from

  • Park, J.H.; Kang, C.H.; Nawkar, G.M.; Lee, E.S.; Paeng, S.K.; Chae, H.B.; Chi, Y.H.; Kim, W.Y.; Yun, D.J.; Lee, S.Y.
    EMR, a cytosolic-abundant ring finger E3 ligase, mediates ER-associated protein degradation in Arabidopsis (2018), New Phytol., 220, 163-177 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Arabidopsis thaliana 5829
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana A0A178UZG1 isoform EMR
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [MLO12-Myc]-L-lysine
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Arabidopsis thaliana [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor MLO12-Myc]-N6-ubiquitinyl-L-lysine
-
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Synonyms

Synonyms Comment Organism
At4g26400
-
Arabidopsis thaliana
EMR
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Arabidopsis thaliana
ERAD-mediating RING finger protein
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Arabidopsis thaliana

Expression

Organism Comment Expression
Arabidopsis thaliana EMR is significantly upregulated under endoplasmic reticulum stress conditions up

General Information

General Information Comment Organism
physiological function tobacco leaf-produced EMR mediates mildew resistance locus O-12 degradation in a proteasome-dependent manner. EMR forms a complex with ubiquitin-conjugating enzyme UBC32. Mutation of EMR and RNAi increase the tolerance of plants to endoplasmic reticulum stress. EMR RNAi in a brassinosteroid signaling mutant protein background, leads to partial recovery of the brassinosteroid insensitive phenotypes as compared with the original mutant plants and increased ER stress tolerance Arabidopsis thaliana