BAIT

ATG9A

APG9L1, MGD3208, mATG9

autophagy related 9A

Autophagy Project

GO Process (5)

GO Function (1)

GO Component (9)

Gene Ontology Biological Process

autophagic vacuole assembly [IMP]

late nucleophagy [IBA]

mitochondrion degradation [IBA]

piecemeal microautophagy of nucleus [IBA]

protein localization to pre-autophagosomal structure [IBA]

Gene Ontology Molecular Function

protein binding [IPI]

Gene Ontology Cellular Component

autophagic vacuole [IBA]

autophagic vacuole membrane [IDA]

integral component of membrane [IBA]

late endosome [IDA]

pre-autophagosomal structure [IBA, IDA]

recycling endosome [IDA]

trans-Golgi network [IDA]

CRISPR Database HGNC Alliance of Genome Resources OMIM Entrez Gene RefSeq UniprotKB Ensembl

Homo sapiens

PREY

DST

BP240, BPA, BPAG1, CATX-15, CATX15, D6S1101, DMH, DT, EBSB2, HSAN6, MACF2, RP3-361I14.2

dystonin

Glioblastoma Project

GO Process (9)

GO Function (5)

GO Component (16)

Gene Ontology Molecular Function

integrin binding [IPI]
microtubule plus-end binding [IDA]
protein C-terminus binding [IPI]
protein binding [IPI]
protein homodimerization activity [IDA]

Gene Ontology Cellular Component

actin cytoskeleton [IDA]

basal plasma membrane [NAS]

basement membrane [TAS]

cell leading edge [IDA]

cytoplasm [IDA, ISS]

cytoplasmic membrane-bounded vesicle [IDA]

extracellular vesicular exosome [IDA]

focal adhesion [IDA]

hemidesmosome [IDA, TAS]

intermediate filament cytoskeleton [IDA]

microtubule cytoskeleton [IDA]

microtubule plus-end [IDA]

CRISPR Database OMIM HGNC Alliance of Genome Resources Entrez Gene RefSeq UniprotKB Ensembl

Homo sapiens

Proximity Label-MS

An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

Publication

BioID reveals an ATG9A interaction with ATG13-ATG101 in the degradation of p62/SQSTM1-ubiquitin clusters.

Kannangara AR, Poole DM, McEwan CM, Youngs JC, Weerasekara VK, Thornock AM, Lazaro MT, Balasooriya ER, Oh LM, Soderblom EJ, Lee JJ, Simmons DL, Andersen JL

ATG9A, the only multi-pass transmembrane protein among core ATG proteins, is an essential regulator of autophagy, yet its regulatory mechanisms and network of interactions are poorly understood. Through quantitative BioID proteomics, we identify a network of ATG9A interactions that includes members of the ULK1 complex and regulators of membrane fusion and vesicle trafficking, including the TRAPP, EARP, GARP, exocyst, AP-1, ... [more]

EMBO Rep Dec. 05, 2020; 22(10);e51136 [Pubmed: 34369648]

Throughput

High Throughput

Curated By

BioGRID