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Literature summary for 3.4.21.89 extracted from

  • Byun, H.; Halani, N.; Mertz, J.A.; Ali, A.F.; Lozano, M.M.; Dudley, J.P.
    Retroviral Rem protein requires processing by signal peptidase and retrotranslocation for nuclear function (2010), Proc. Natl. Acad. Sci. USA, 107, 12287-12292.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
lactacystin proteasome inhibitor, presence in cells infected with mouse mammary tumor virus results in accumulation of uncleaved Rem relative to SP, consistent with SP retrotranslocation and proteasome escape before nuclear entry Mus musculus
MG132 proteasome inhibitor, presence in cells infected with mouse mammary tumor virus results in accumulation of uncleaved Rem relative to SP, consistent with SP retrotranslocation and proteasome escape before nuclear entry Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
breast tumor cell
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Mus musculus
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HC-11 cell normal mouse mammary cell line Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information GFP-tagged cleavage-site mutants are unstable compared with wild-type rem, suggesting improper folding Mus musculus ?
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?
pro-rem + H2O Rev-like export protein encoded by mouse mammary tumor virus. Mutations at both glycosylation positions eliminate detectable rem glycosylation without effect on SP cleavage. Rem protein expression constructs with mutations at position -1, relative to the predicted cleavage site, i.e. G98R or both positions -1 and -3, V96R/G98R are not cleaved by SP-I Mus musculus signal peptide + rem
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?

Synonyms

Synonyms Comment Organism
SP-I
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Mus musculus