AKT1 E17K mutant phosphorylates MDM2

Stable Identifier
R-HSA-2399981
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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AKT1 E17K mutant phosphorylates MDM2
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AKT1 E17K gain-of-function mutant is expected to phosphorylate MDM2, like the wild-type AKT (Zhou et al. 2001, Feng et al. 2004, Milne et al. 2004), but this has not been experimentally tested.

Literature References
PubMed ID Title Journal Year
15527798 A novel site of AKT-mediated phosphorylation in the human MDM2 onco-protein

Kampanis, P, Campbell, DG, Nicol, S, Milne, D, Meek, D, Fuller-Pace, F, Dias, S

FEBS Lett. 2004
15169778 Stabilization of Mdm2 via decreased ubiquitination is mediated by protein kinase B/Akt-dependent phosphorylation

Yang, Z, Hess, D, Tamaskovic, R, Merlo, A, Feng, J, Brazil, DP, Hemmings, BA

J. Biol. Chem. 2004
11715018 HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation

Zou, Y, Xia, W, Zhou, BP, Hung, MC, Spohn, B, Liao, Y

Nat Cell Biol 2001
Participants
Input
Output
Participates
as an event of
Catalyst Activity

protein serine/threonine kinase activity of p-T308,S473-AKT1 E17K [cytosol]

Physical Entity
p-T308,S473-AKT1 E17K [cytosol] (Homo sapiens)
Activity
protein serine/threonine kinase activity (GO:0004674)
Normal reaction
AKT phosphorylates MDM2 (Homo sapiens)
Functional status

Gain of function of p-T308,S473-AKT1 E17K [cytosol]

Normal Entity
Disease Entity
Status
Disease
Name Identifier Synonyms
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
Authored
Orlic-Milacic, M  (2012-07-18)
Reviewed
Zhao, JJ  (2012-08-13)
Yuzugullu, H  (2012-08-13)
Thorpe, L  (2012-08-13)
Created
Orlic-Milacic, M  (2012-07-13)
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