ATG12 forms a thioester bond with ATG7 dimer

Stable Identifier
R-HSA-9020616
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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The amino-acid sequence of ATG12 ends with a glycine residue that does not require protease activation. ATG12 is activated by the formation of a thioester bond between the ATG12 C-terminal Gly-140 and Cys-572 of ATG7, which is functionally analogous to E1 enzymes in ubiquitination (Tanida et al. 1999, 2001). ATG7 has been shown to function in the form of a homodimer (Komatsu et al. 2001).

Literature References
PubMed ID Title Journal Year
11096062 The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3

Tanida, I, Tanida-Miyake, E, Ueno, T, Kominami, E

J. Biol. Chem. 2001
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