Ubiquitinated geminin is degraded by the proteasome

Stable Identifier
R-HSA-68825
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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Ubiquitinated geminin is degraded by the proteasome
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APC/C-dependent degradation of geminin (GMNN) was first demonstrated in Xenopus (McGarry and Kirschner 1998) and was shown to be proteasome-dependent and sensitive to FBXO5 (Emi1)-mediated inhibition of the APC/C:Cdh1 activity in human cells (Machida and Dutta 2007).
Literature References
PubMed ID Title Journal Year
9635433 Geminin, an inhibitor of DNA replication, is degraded during mitosis.

McGarry, TJ, Kirschner, MW

Cell 1998
17234884 The APC/C inhibitor, Emi1, is essential for prevention of rereplication

Machida, YJ, Dutta, A

Genes Dev 2007
Participants
Input
Output
Participates
as an event of
Catalyst Activity

endopeptidase activity of 26S proteasome [nucleoplasm]

Physical Entity
26S proteasome [nucleoplasm] (Homo sapiens)
Activity
endopeptidase activity (GO:0004175)
Orthologous Events
Ubiquitinated geminin is degraded by the proteasome (Bos taurus)
Ubiquitinated geminin is degraded by the proteasome (Canis familiaris)
Ubiquitinated geminin is degraded by the proteasome (Danio rerio)
Ubiquitinated geminin is degraded by the proteasome (Gallus gallus)
Ubiquitinated geminin is degraded by the proteasome (Mus musculus)
Ubiquitinated geminin is degraded by the proteasome (Rattus norvegicus)
Ubiquitinated geminin is degraded by the proteasome (Sus scrofa)
Ubiquitinated geminin is degraded by the proteasome (Xenopus tropicalis)
Reviewed
Kusic-Tisma, J  (2021-11-05)
Created
Davey, MJ  (2003-06-05)
O'Donnell, M  (2003-06-05)
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