Literature summary for 1.5.1.3 extracted from

Maguire, M.; Nield, P.C.; Devling, T.; Jenkins, R.E.; Park, B.K.; Polanski, R.; Vlatkovic, N.; Boyd, M.T.
MDM2 regulates dihydrofolate reductase activity through monoubiquitination (2008), Cancer Res., 68, 3232-3242.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in H-1299 cell	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	dihydrofolate reductase is a substrate of ubiquitin ligase MDM2. MDM2 binds directly to dihydrofolate reductase and catalyzes its monoubiquitination. It reduces dihydrofolate reductase activity in a p53-independent manner, but has no effect on the steady-state level of expression. the ability of MDM2 to inhibit dihydrofolate reductase deoends on an active MDM2 RING-finger domain	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	dihydrofolate reductase is a substrate of ubiquitin ligase MDM2. MDM2 binds directly to dihydrofolate reductase and catalyzes its monoubiquitination. It reduces dihydrofolate reductase activity in a p53-independent manner, but has no effect on the steady-state level of expression. The ability of MDM2 to inhibit dihydrofolate reductase deoends on an active MDM2 RING-finger domain	Homo sapiens

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Release 2023.1 (January 2023)