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complex(p(HGNC:ATG12), p(HGNC:ATG5))

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Components

Appears in Networks 1

Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection v1.0.0

In-Edges 1

composite(p(HGNC:ATG10), p(HGNC:ATG7)) increases complex(p(HGNC:ATG12), p(HGNC:ATG5)) View Subject | View Object

In the first arm of the Atg conjugation system, phagophore membrane elongation is triggered through the sequential action of an E1-like protein (Atg7) and an E2-like protein (Atg10) leading to an isopeptide linkage between the C-terminal glycine the UBL protein Atg12 and a lysine residue of Atg5 (Figure 2b). PubMed:18930136

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Out-Edges 4

complex(p(HGNC:ATG12), p(HGNC:ATG5)) hasComponent p(HGNC:ATG12) View Subject | View Object

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complex(p(HGNC:ATG12), p(HGNC:ATG5)) hasComponent p(HGNC:ATG5) View Subject | View Object

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complex(p(HGNC:ATG12), p(HGNC:ATG5)) increases complex(p(HGNC:ATG12), p(HGNC:ATG16L1), p(HGNC:ATG5)) View Subject | View Object

These Atg12-Atg5 conjugates are further cross-linked to Atg16 to form a large (~350 kDa) multimeric complex, which has been thought to act as a structural support for membrane expansion [15]. PubMed:18930136

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complex(p(HGNC:ATG12), p(HGNC:ATG5)) increases p(HGNC:GABARAPL2, pmod(GO:"protein lipidation")) View Subject | View Object

More recent work has demonstrated that the Atg12-Atg5 conjugate can function as an E3-like enzyme in the second arm of the Atg conjugation cascade to promote lipidation of Atg8 [16] PubMed:18930136

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.