Literature summary extracted from

Lee, P.C.; Nguyen, A.D.; Debose-Boyd, R.A.
Mutations within membrane domain of HMG CoA reductase confer resistance to sterol-accelerated degradation (2006), J. Lipid Res., 48, 318-327.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.1.1.34	A333P	mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation	Cricetulus griseus
1.1.1.34	G87R	mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation	Cricetulus griseus
1.1.1.34	S60N	mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation	Cricetulus griseus

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.34	Cricetulus griseus	P00347	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.1.1.34	CHO-7 cell	-	Cricetulus griseus	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.1.1.34	HMG-CoA reductase	-	Cricetulus griseus

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Release 2023.1 (January 2023)