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Literature summary for 2.3.2.27 extracted from

  • Eisele, F.; Wolf, D.H.
    Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1 (2008), FEBS Lett., 582, 4143-4146.
    View publication on PubMed
Search for more literature for 2.3.2.27

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Reaction

Reaction Comment Organism Reaction ID
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine Ubr1 is an ubiquitin ligase, which is able to recignize N-end rule substrates. These substrates occur at two sites, type1 and type-2, specific for reecognition of basic N-terminal amino acid residues and responsible for recognition of bulky hydrophobic amino acid residues of proteins Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information degradation of the cytoplasmic misfolded protein DELTAssCL*myc, a derivative of signal sequence delted mutated carboxypeptidase yscY Saccharomyces cerevisiae ?
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Synonyms

Synonyms Comment Organism
E3 ligase
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 Saccharomyces cerevisiae
E3-enzyme
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 Saccharomyces cerevisiae
RING-finger ubiquitin ligase Ubr1
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 Saccharomyces cerevisiae
ubiquitin ligase E3
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 Saccharomyces cerevisiae
ubiquitin ligase Ubr1
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 Saccharomyces cerevisiae
UBR1
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function protein quality control and subsequent elimination of terminally misfolded proteins is mediated by the ubiquitin-proteasome system. Ubr1, the N-end rule pathway E3 ligase is responsible for targeting misfolded cytoplasmic proteons to proteasomal degradation Saccharomyces cerevisiae