Securin

Securin

Securin is a protein involved in anaphase triggering. It has two identified roles; the first one is to help the transport of separase to the nucleus and the second role is to inhibit the catalytic activity of separase. Securin is ubiquitinated by the Anaphase Promoting Complex (APC), and then degraded by the Proteasome, releasing separase.

In yeast securin is known as Pds1p.

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Last updated on Friday October 10, 2008 at 12:44:16 PDT (GMT -0700)
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Securin, low in fetal brain, correlates with lack of adult neural proliferation.
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Research from University of Sevilla yields new findings on enzyme research.
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Research from University Hospital in the Area of Glucosyltransferases Published.
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