ATG12 forms a thioester bond with ATG7 dimer

Stable Identifier
R-HSA-9020616
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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ATG12 forms a thioester bond with ATG7 dimer
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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, Ueno, T, Tanida-Miyake, E, Kominami, E

J. Biol. Chem. 2001
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Orthologous Events
ATG12 forms a thioester bond with ATG7 dimer (Bos taurus)
ATG12 forms a thioester bond with ATG7 dimer (Caenorhabditis elegans)
ATG12 forms a thioester bond with ATG7 dimer (Canis familiaris)
ATG12 forms a thioester bond with ATG7 dimer (Dictyostelium discoideum)
ATG12 forms a thioester bond with ATG7 dimer (Drosophila melanogaster)
ATG12 forms a thioester bond with ATG7 dimer (Gallus gallus)
ATG12 forms a thioester bond with ATG7 dimer (Mus musculus)
ATG12 forms a thioester bond with ATG7 dimer (Plasmodium falciparum)
ATG12 forms a thioester bond with ATG7 dimer (Rattus norvegicus)
ATG12 forms a thioester bond with ATG7 dimer (Saccharomyces cerevisiae)
ATG12 forms a thioester bond with ATG7 dimer (Schizosaccharomyces pombe)
ATG12 forms a thioester bond with ATG7 dimer (Sus scrofa)
ATG12 forms a thioester bond with ATG7 dimer (Xenopus tropicalis)
Authored
Jupe, S  (2015-02-02)
Reviewed
Klionsky, DJ  (2015-09-03)
Tooze, SA  (2015-05-13)
Created
Jupe, S  (2017-09-08)
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