ATG12 binds ATG7 dimer

Stable Identifier
R-HSA-5681980
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

ATG7 acts as an E1-like enzyme for ATG12. It binds to and activates ATG12, allow its transfer to the E2-like ATG10. The amino-acid sequence of ATG12 ends with a glycine residue and does not require protease activation. ATG12 is activated by forming a thioester bond between its C-terminal Gly-140 and Cys-572 of ATG7 (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
Participants
Participant Of
hasEvent
Orthologous Events
Authored
Reviewed
Created