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Details on Person ATG7 acts as an E1-like enzyme for ATG12. It binds to and ac...

Class:IdSummation:5681978
_displayNameATG7 acts as an E1-like enzyme for ATG12. It binds to and ac...
_timestamp2017-09-08 15:11:12
created[InstanceEdit:5681983] Jupe, Steve, 2015-03-04
literatureReference[LiteratureReference:5682007] Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy
[LiteratureReference:5682651] The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3
[LiteratureReference:5681996] The C-terminal region of an Apg7p/Cvt2p is required for homodimerization and is essential for its E1 activity and E1-E2 complex formation
modified[InstanceEdit:5682015] Jupe, Steve, 2015-03-04
[InstanceEdit:5682672] Jupe, Steve, 2015-03-10
[InstanceEdit:5682876] Jupe, Steve, 2015-03-11
[InstanceEdit:5683921] Jupe, Steve, 2015-03-17
[InstanceEdit:9020618] Jupe, Steve, 2017-09-08
textATG7 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).
(summation)[Reaction:5681980] ATG12 binds ATG7 dimer [Homo sapiens]
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