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Literature summary extracted from

  • Bacac, M.; Fusco, C.; Planche, A.; Santodomingo, J.; Demaurex, N.; Leemann-Zakaryan, R.; Provero, P.; Stamenkovic, I.
    Securin and separase modulate membrane traffic by affecting endosomal acidification (2011), Traffic, 12, 615-626.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.22.49 cytoplasm separase is abundantly expressed within the cytoplasm of a broad range of human tumor cell lines, including MDA-MB-231 breast carcinoma cells Homo sapiens 5737
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3.4.22.49 membrane
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 Homo sapiens 16020
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Organism

EC Number Organism UniProt Comment Textmining
3.4.22.49 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.49 HEK-293T cell
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 Homo sapiens
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3.4.22.49 HeLa cell
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 Homo sapiens
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3.4.22.49 Hep-G2 cell
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 Homo sapiens
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3.4.22.49 MDA-MB-231 cell
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 Homo sapiens
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General Information

EC Number General Information Comment Organism
3.4.22.49 malfunction cells depleted of securin or separase display defective acidification of early endosomes and increased membrane recruitment of vacuolar ATPase complexes, mimicking the effect of the specific V-ATPase inhibitor Bafilomycin A1. Securin and separase depletion causes trans-Golgi network and endosome swelling independent of cell cycle. Endosome-mediated receptor degradation and recycling are also significantly impaired by securin and separase depletion, although not receptor internalization or Rab5 activity and autophagy Homo sapiens
3.4.22.49 physiological function functional role of securin and separase in the modulation of membrane traffic and protein secretion implicating regulation of V-ATPase assembly and function. Separase activity is controlled by securin, i.e. pituitary tumor transforming gene 1, PTTG1, a member of a divergent class of anaphase inhibitors whose proteosomal degradation by the anaphase promoting complex, APC, is required to release separase and allow its activation Homo sapiens