BAIT
ATG9A
APG9L1, MGD3208, mATG9
autophagy related 9A
GO Process (5)
GO Function (1)
GO Component (9)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
TNK2
ACK, ACK-1, ACK1, p21cdc42Hs
tyrosine kinase, non-receptor, 2
GO Process (12)
GO Function (8)
GO Component (9)
Gene Ontology Biological Process
- cell differentiation [IBA]
- cell migration [IBA]
- cell surface receptor signaling pathway [TAS]
- innate immune response [IBA]
- negative regulation of catalytic activity [TAS]
- peptidyl-tyrosine autophosphorylation [IBA]
- phosphorylation [IDA]
- positive regulation of peptidyl-tyrosine phosphorylation [IDA]
- regulation of cell proliferation [IBA]
- regulation of clathrin-mediated endocytosis [IDA]
- small GTPase mediated signal transduction [TAS]
- transmembrane receptor protein tyrosine kinase signaling pathway [IBA]
Gene Ontology Molecular Function- GTPase inhibitor activity [TAS]
- WW domain binding [ISS]
- epidermal growth factor receptor binding [IDA]
- hormone receptor binding [IBA]
- non-membrane spanning protein tyrosine kinase activity [IBA]
- protein binding [IPI]
- protein serine/threonine/tyrosine kinase activity [IDA]
- protein tyrosine kinase activity [IDA]
- GTPase inhibitor activity [TAS]
- WW domain binding [ISS]
- epidermal growth factor receptor binding [IDA]
- hormone receptor binding [IBA]
- non-membrane spanning protein tyrosine kinase activity [IBA]
- protein binding [IPI]
- protein serine/threonine/tyrosine kinase activity [IDA]
- protein tyrosine kinase activity [IDA]
Gene Ontology Cellular Component
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.
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