BAIT

ATG16L1

APG16L, ATG16A, ATG16L, IBD10, WDR30, hCG_1817841
autophagy related 16-like 1 (S. cerevisiae)
GO Process (3)
GO Function (2)
GO Component (3)
Homo sapiens
PREY

ATG16L1

APG16L, ATG16A, ATG16L, IBD10, WDR30, hCG_1817841
autophagy related 16-like 1 (S. cerevisiae)
GO Process (3)
GO Function (2)
GO Component (3)
Homo sapiens

Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

Publication

The N-terminal region of the human autophagy protein ATG16L1 contains a domain that folds into a helical structure consistent with formation of a coiled-coil.

Parkhouse R, Ebong IO, Robinson CV, Monie TP

Autophagy is a fundamental cellular process required for organelle degradation and removal of invasive pathogens. Autophagosome formation involves the recruitment of, and interaction between, multiple proteins produced from autophagy-related (ATG) genes. One of the key complexes in autophagosome formation is the ATG12-ATG5-ATG16L1 complex. ATG16L1 functions as a molecular scaffold mediating protein-protein interactions necessary for formation of the autophagosome in response ... [more]

PLoS ONE Oct. 03, 2013; 8(9);e76237 [Pubmed: 24086718]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ATG16L1 ATG16L1
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High-BioGRID
-
ATG16L1 ATG16L1
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
-
ATG16L1 ATG16L1
Co-purification
Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Low-BioGRID
-
ATG16L1 ATG16L1
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
2521278

Curated By

  • BioGRID