ATG13 is a non-catalytic regulatory subunit of the ULK1/ULK2 (Atg1) protein kinase complex, which also contains FIP200 (RB1CC1) and ATG101 and is the most upstream initiator of macroautophagy in mammals. ATG13 has an N-terminal HORMA domain that heterodimerizes with ATG101, and a long intrinsically disordered C-terminal region that binds FIP200 and, through a C-terminal MIT-interacting motif, the ULK1/2 MIT domain; it also carries an LC3-interacting region that binds Atg8-family proteins. ATG13 bridges ULK1/2 to FIP200, stabilizes ULK and stimulates its kinase activity. The complex forms constitutively in the cytosol and is recruited to ER-associated phagophore assembly sites, where it coassembles with the class III PI3K complex I. mTORC1 phosphorylates ATG13 and ULK1 to keep the complex inactive under nutrient-rich conditions. ATG13 is required for autophagosome formation, ATG9 trafficking and mitophagy, during which it is recruited to damaged mitochondria.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000045 autophagosome assembly | IDA PMID:19225151 ULK-Atg13-FIP200 complexes mediate mTOR signaling to the aut... | ACCEPT | Summary: ATG13 is an essential, non-catalytic subunit of the ULK1/2 complex and is required for autophagosome formation. Reason: Knockdown of ATG13 blocks autophagosome formation, and ATG13 resides on the isolation membrane as part of the ULK1-ATG13-FIP200-ATG101 initiation complex. This is direct participation in autophagosome assembly at its initiating step. Supporting Evidence: PMID:19225151 The binding of Atg13 stabilizes and activates ULK and facilitates the phosphorylation of FIP200 by ULK, whereas knockdown of Atg13 inhibits autophagosome formation. PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0000045 autophagosome assembly | IEA GO_REF:0000120 | ACCEPT | Summary: ATG13 is an essential, non-catalytic subunit of the ULK1/2 complex and is required for autophagosome formation. Reason: Knockdown of ATG13 blocks autophagosome formation, and ATG13 resides on the isolation membrane as part of the ULK1-ATG13-FIP200-ATG101 initiation complex. This is direct participation in autophagosome assembly at its initiating step. Supporting Evidence: PMID:19225151 The binding of Atg13 stabilizes and activates ULK and facilitates the phosphorylation of FIP200 by ULK, whereas knockdown of Atg13 inhibits autophagosome formation. PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0000045 autophagosome assembly | IMP PMID:19211835 Nutrient-dependent mTORC1 association with the ULK1-Atg13-FI... | ACCEPT | Summary: ATG13 is an essential, non-catalytic subunit of the ULK1/2 complex and is required for autophagosome formation. Reason: Knockdown of ATG13 blocks autophagosome formation, and ATG13 resides on the isolation membrane as part of the ULK1-ATG13-FIP200-ATG101 initiation complex. This is direct participation in autophagosome assembly at its initiating step. Supporting Evidence: PMID:19225151 The binding of Atg13 stabilizes and activates ULK and facilitates the phosphorylation of FIP200 by ULK, whereas knockdown of Atg13 inhibits autophagosome formation. PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0000045 autophagosome assembly | IMP PMID:19211835 Nutrient-dependent mTORC1 association with the ULK1-Atg13-FI... | ACCEPT | Summary: ATG13 is an essential, non-catalytic subunit of the ULK1/2 complex and is required for autophagosome formation. Reason: Knockdown of ATG13 blocks autophagosome formation, and ATG13 resides on the isolation membrane as part of the ULK1-ATG13-FIP200-ATG101 initiation complex. This is direct participation in autophagosome assembly at its initiating step. Supporting Evidence: PMID:19225151 The binding of Atg13 stabilizes and activates ULK and facilitates the phosphorylation of FIP200 by ULK, whereas knockdown of Atg13 inhibits autophagosome formation. PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0000407 phagophore assembly site | EXP PMID:19211835 Nutrient-dependent mTORC1 association with the ULK1-Atg13-FI... | ACCEPT | Summary: ATG13 localizes with ULK1 and FIP200 to the autophagosome formation site/isolation membrane. Reason: Experimentally shown for human ATG13 and conserved from yeast Atg13, which is a PAS component; consistent with the IBA. Supporting Evidence: PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0000407 phagophore assembly site | IBA GO_REF:0000033 | ACCEPT | Summary: ATG13 localizes with ULK1 and FIP200 to the autophagosome formation site/isolation membrane. Reason: Experimentally shown for human ATG13 and conserved from yeast Atg13, which is a PAS component; consistent with the IBA. Supporting Evidence: PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0000407 phagophore assembly site | IDA PMID:19597335 Atg101, a novel mammalian autophagy protein interacting with... | ACCEPT | Summary: ATG13 localizes with ULK1 and FIP200 to the autophagosome formation site/isolation membrane. Reason: Experimentally shown for human ATG13 and conserved from yeast Atg13, which is a PAS component; consistent with the IBA. Supporting Evidence: PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0000407 phagophore assembly site | IEA GO_REF:0000120 | ACCEPT | Summary: ATG13 localizes with ULK1 and FIP200 to the autophagosome formation site/isolation membrane. Reason: Experimentally shown for human ATG13 and conserved from yeast Atg13, which is a PAS component; consistent with the IBA. Supporting Evidence: PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0000407 phagophore assembly site | ISS GO_REF:0000024 | ACCEPT | Summary: ATG13 localizes with ULK1 and FIP200 to the autophagosome formation site/isolation membrane. Reason: Experimentally shown for human ATG13 and conserved from yeast Atg13, which is a PAS component; consistent with the IBA. Supporting Evidence: PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0000423 mitophagy | IBA GO_REF:0000033 | ACCEPT | Summary: ATG13 is phosphorylated by ULK1, released and recruited to damaged mitochondria, and is required for efficient mitophagy. Reason: Direct experimental support that ATG13 phosphorylation and recruitment to damaged mitochondria are required for mitochondrial clearance; ULK1-complex dependent mitophagy is also the conserved PAINT assertion. Supporting Evidence: PMID:21855797 required for the phosphorylation and release of Atg13 from Ulk1, and for the recruitment of Atg13 to damaged mitochondria PMID:21855797 Hsp90-Cdc37, Ulk1, and Atg13 phosphorylation are all required for efficient mitochondrial clearance. |
| GO:0000423 mitophagy | IEA GO_REF:0000107 | ACCEPT | Summary: ATG13 is phosphorylated by ULK1, released and recruited to damaged mitochondria, and is required for efficient mitophagy. Reason: Direct experimental support that ATG13 phosphorylation and recruitment to damaged mitochondria are required for mitochondrial clearance; ULK1-complex dependent mitophagy is also the conserved PAINT assertion. Supporting Evidence: PMID:21855797 required for the phosphorylation and release of Atg13 from Ulk1, and for the recruitment of Atg13 to damaged mitochondria PMID:21855797 Hsp90-Cdc37, Ulk1, and Atg13 phosphorylation are all required for efficient mitochondrial clearance. |
| GO:0005515 protein binding | IPI PMID:19211835 Nutrient-dependent mTORC1 association with the ULK1-Atg13-FI... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:19211835 Nutrient-dependent mTORC1 association with the ULK1-Atg13-FI... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:19597335 Atg101, a novel mammalian autophagy protein interacting with... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:19597335 Atg101, a novel mammalian autophagy protein interacting with... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:19597335 Atg101, a novel mammalian autophagy protein interacting with... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20200478 Nix, a receptor protein for mitophagy in mammals. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20200478 Nix, a receptor protein for mitophagy in mammals. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:21900206 A directed protein interaction network for investigating int... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:23392225 FIP200 regulates targeting of Atg16L1 to the isolation membr... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:23392225 FIP200 regulates targeting of Atg16L1 to the isolation membr... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:23392225 FIP200 regulates targeting of Atg16L1 to the isolation membr... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:23524951 mTOR inhibits autophagy by controlling ULK1 ubiquitylation, ... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:24290141 Structural basis of the autophagy-related LC3/Atg13 LIR comp... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:24290141 Structural basis of the autophagy-related LC3/Atg13 LIR comp... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:24290141 Structural basis of the autophagy-related LC3/Atg13 LIR comp... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:24290141 Structural basis of the autophagy-related LC3/Atg13 LIR comp... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:24290141 Structural basis of the autophagy-related LC3/Atg13 LIR comp... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25686248 Huntingtin functions as a scaffold for selective macroautoph... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:26299944 Structure of the Human Atg13-Atg101 HORMA Heterodimer: an In... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:27334615 The C9orf72 protein interacts with Rab1a and the ULK1 comple... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:27334615 The C9orf72 protein interacts with Rab1a and the ULK1 comple... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:28195531 Multiplex image-based autophagy RNAi screening identifies SM... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:29950492 The C9orf72-interacting protein Smcr8 is a negative regulato... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:31806350 The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulat... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:31806350 The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulat... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33368531 Regulation of autophagosome biogenesis by OFD1-mediated sele... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33368531 Regulation of autophagosome biogenesis by OFD1-mediated sele... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33422265 ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-m... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33450483 The papain-like protease of coronaviruses cleaves ULK1 to di... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:34524948 Global Proximity Interactome of the Human Macroautophagy Pat... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:34524948 Global Proximity Interactome of the Human Macroautophagy Pat... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005737 cytoplasm | IC PMID:29487085 The deubiquitinating enzyme USP20 stabilizes ULK1 and promot... | ACCEPT | Summary: ATG13 is a cytoplasmic protein. Reason: Correct broad location, inferred by the curator from the ULK1-complex context. Supporting Evidence: PMID:29487085 ULK1 forms a stable complex with ATG13, ATG101, and FIP200 which is the mammalian ortholog of ATG17 |
| GO:0005739 mitochondrion | IDA PMID:21855797 Hsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-medi... | KEEP AS NON CORE | Summary: ATG13 is recruited to damaged mitochondria during mitophagy. Reason: Stimulus-dependent recruitment to the cytosolic face of damaged mitochondria; not a resident mitochondrial location. Supporting Evidence: PMID:21855797 required for the phosphorylation and release of Atg13 from Ulk1, and for the recruitment of Atg13 to damaged mitochondria |
| GO:0005776 autophagosome | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: ATG13 acts at the phagophore assembly site and isolation membrane, not on completed autophagosomes. Reason: The ULK1 complex is an initiation factor that is recruited to nascent autophagic membranes and released before or upon closure. Phagophore assembly site is the accurate location; the completed-autophagosome term overstates where ATG13 resides. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: COMPARTMENT OR COMPLEX MISMATCH Sources checked: PANTHER:PTN001268151 · PTN001268151 SUPPORTS SOURCE BUT NOT TARGET The ATG13-family node is sound for autophagy initiation; the completed-autophagosome location is broader than the phagophore assembly site where ATG13 acts. Supporting Evidence: PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-1632857 | KEEP AS NON CORE | Summary: Reactome places the ULK1 complex at ER membrane sites where omegasomes and phagophores originate. Reason: ATG13 has no transmembrane segment; it is recruited from the cytosol to ER-associated autophagosome formation sites. The term is acceptable as context but is less accurate than phagophore assembly site. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5679205 | KEEP AS NON CORE | Summary: Reactome places the ULK1 complex at ER membrane sites where omegasomes and phagophores originate. Reason: ATG13 has no transmembrane segment; it is recruited from the cytosol to ER-associated autophagosome formation sites. The term is acceptable as context but is less accurate than phagophore assembly site. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5679239 | KEEP AS NON CORE | Summary: Reactome places the ULK1 complex at ER membrane sites where omegasomes and phagophores originate. Reason: ATG13 has no transmembrane segment; it is recruited from the cytosol to ER-associated autophagosome formation sites. The term is acceptable as context but is less accurate than phagophore assembly site. |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | IEA GO_REF:0000120 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5665868 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672008 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672010 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672011 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672817 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5673768 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5675790 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5675868 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5679239 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5683925 | ACCEPT | Summary: ATG13 is cytosolic when not recruited to autophagosome formation sites. Reason: ULK1-ATG13-FIP200-ATG101 forms a stable cytosolic complex that is recruited to membranes on autophagy induction. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:0006914 autophagy | IEA GO_REF:0000002 | ACCEPT | Summary: ATG13 is required for autophagy. Reason: Correct general process term from the InterPro ATG13 family mapping. Supporting Evidence: PMID:18936157 Atg13 is required for autophagy and Atg9 trafficking during autophagy. |
| GO:0008285 negative regulation of cell population proliferation | IDA PMID:21795849 ULK1 inhibits the kinase activity of mTORC1 and cell prolife... | KEEP AS NON CORE | Summary: ATG13 knockdown phenocopies ULK1/2 loss, enhancing mTORC1 signalling and cell proliferation. Reason: This is an indirect consequence of ATG13 supporting ULK1 activity, which feeds back on mTORC1; ATG13 itself has no proliferation-specific activity. Supporting Evidence: PMID:21795849 Knockdown of Atg13, the binding partner of ULK1 and ULK2, mimicked the effects of ULK1 or ULK2 deficiency or knockdown. |
| GO:0008285 negative regulation of cell population proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ATG13 knockdown phenocopies ULK1/2 loss, enhancing mTORC1 signalling and cell proliferation. Reason: This is an indirect consequence of ATG13 supporting ULK1 activity, which feeds back on mTORC1; ATG13 itself has no proliferation-specific activity. Supporting Evidence: PMID:21795849 Knockdown of Atg13, the binding partner of ULK1 and ULK2, mimicked the effects of ULK1 or ULK2 deficiency or knockdown. |
| GO:0010508 positive regulation of autophagy | IDA PMID:29487085 The deubiquitinating enzyme USP20 stabilizes ULK1 and promot... | KEEP AS NON CORE | Summary: As an essential ULK1-complex subunit, ATG13 promotes autophagy initiation. Reason: ATG13 is a core component of the autophagy machinery rather than a modulator, so its process role is better captured by autophagosome assembly and macroautophagy; the regulation term is acceptable but not the most accurate description. Supporting Evidence: PMID:29487085 ULK1 forms a stable complex with ATG13, ATG101, and FIP200 which is the mammalian ortholog of ATG17 |
| GO:0010508 positive regulation of autophagy | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: As an essential ULK1-complex subunit, ATG13 promotes autophagy initiation. Reason: ATG13 is a core component of the autophagy machinery rather than a modulator, so its process role is better captured by autophagosome assembly and macroautophagy; the regulation term is acceptable but not the most accurate description. Supporting Evidence: PMID:19225151 The binding of Atg13 stabilizes and activates ULK and facilitates the phosphorylation of FIP200 by ULK, whereas knockdown of Atg13 inhibits autophagosome formation. |
| GO:0016236 macroautophagy | NAS PMID:40442316 Structure and activation of the human autophagy-initiating U... | ACCEPT | Summary: ATG13 is a subunit of the ULK1 complex, the most upstream initiation complex of mammalian macroautophagy. Reason: Correct and well supported; structural work defines ATG13 as a core subunit of ULK1C. Supporting Evidence: PMID:40442316 The Unc-51-like kinase protein kinase complex (ULK1C) is the most upstream and central player in the initiation of macroautophagy in mammals. PMID:40442316 The FIP200:ATG13:ULK1 core of ULK1C undergoes a rearrangement from 2:1:1 to 2:2:2 stoichiometry in the presence of PI3KC3-C1. |
| GO:0019209 kinase activator activity | IDA PMID:19225151 ULK-Atg13-FIP200 complexes mediate mTOR signaling to the aut... | ACCEPT | Summary: ATG13 binding stabilizes and activates ULK1/2 kinase. Reason: Direct evidence that ATG13 binding increases ULK activity toward FIP200; matches the conserved yeast Atg13 role as an Atg1 activator. Supporting Evidence: PMID:19225151 The binding of Atg13 stabilizes and activates ULK and facilitates the phosphorylation of FIP200 by ULK, whereas knockdown of Atg13 inhibits autophagosome formation. |
| GO:0019887 protein kinase regulator activity | IBA GO_REF:0000033 | ACCEPT | Summary: ATG13 is a non-catalytic regulatory subunit of the ULK1/2 kinase complex. Reason: Conserved activity of the ATG13 family (yeast Atg13 activates Atg1); human ATG13 stabilizes and activates ULK. Correct level of generality for an IBA. Supporting Evidence: PMID:19225151 The binding of Atg13 stabilizes and activates ULK and facilitates the phosphorylation of FIP200 by ULK, whereas knockdown of Atg13 inhibits autophagosome formation. |
| GO:0019901 protein kinase binding | IDA PMID:29487085 The deubiquitinating enzyme USP20 stabilizes ULK1 and promot... | ACCEPT | Summary: ATG13 binds the ULK1 and ULK2 kinases directly. Reason: Kinase binding is the basis of ATG13 function as a ULK regulatory subunit; the C-terminal MIM region of ATG13 binds the ULK1 MIT domain. Supporting Evidence: PMID:29487085 ULK1 forms a stable complex with ATG13, ATG101, and FIP200 which is the mammalian ortholog of ATG17 |
| GO:0019901 protein kinase binding | IPI PMID:18936157 Kinase-inactivated ULK proteins inhibit autophagy via their ... | ACCEPT | Summary: ATG13 binds the ULK1 and ULK2 kinases directly. Reason: Kinase binding is the basis of ATG13 function as a ULK regulatory subunit; the C-terminal MIM region of ATG13 binds the ULK1 MIT domain. Supporting Evidence: PMID:18936157 Additional mapping indicates that the CTD contains other distinct regions that direct membrane association and interaction with the putative human homologue of Atg13, which we have here characterized. |
| GO:0019901 protein kinase binding | IPI PMID:18936157 Kinase-inactivated ULK proteins inhibit autophagy via their ... | ACCEPT | Summary: ATG13 binds the ULK1 and ULK2 kinases directly. Reason: Kinase binding is the basis of ATG13 function as a ULK regulatory subunit; the C-terminal MIM region of ATG13 binds the ULK1 MIT domain. Supporting Evidence: PMID:18936157 Additional mapping indicates that the CTD contains other distinct regions that direct membrane association and interaction with the putative human homologue of Atg13, which we have here characterized. |
| GO:0034045 obsolete phagophore assembly site membrane | IDA PMID:19597335 Atg101, a novel mammalian autophagy protein interacting with... | MODIFY | Summary: ATG13 associates with the isolation membrane/phagophore assembly site. Reason: The localization is correct, but GOA reports this term as obsolete. The parent location phagophore assembly site, already annotated by several lines of evidence, captures the observation. Proposed replacements: phagophore assembly site Supporting Evidence: PMID:19211835 Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. |
| GO:0034497 protein localization to phagophore assembly site | IBA GO_REF:0000033 | ACCEPT | Summary: ATG13 helps recruit ULK1-complex partners to the phagophore assembly site. Reason: ATG13 bridges ULK1 to FIP200 and ATG101 and carries an LIR that binds Atg8-family proteins needed for proper autophagosome formation; recruitment of complex members to the PAS is a conserved Atg13 role. Supporting Evidence: PMID:19225151 The mammalian Atg13 binds both ULK1 and ULK2 and mediates the interaction of the ULK proteins with FIP200. PMID:24290141 Our results suggest that specific affinity of the LC3 isoforms to the Atg13 LIR is required for proper autophagosome formation. |
| GO:0034727 piecemeal microautophagy of the nucleus | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Piecemeal microautophagy of the nucleus is characterized in budding yeast; no ATG13-dependent equivalent route has been shown in human cells. Reason: The PAINT assertion derives from yeast Atg13. The general initiation role of ATG13 is captured by other terms; until a mammalian piecemeal nuclear microautophagy route is demonstrated, this transfer adds a route-specific claim without target support. The human ULK1 review leaves the equivalent row UNDECIDED for the same reason. Propagation Review Root cause: UNRESOLVED Failure modes: LINEAGE OR TAXON MISMATCH Sources checked: PANTHER:PTN001268151 · PTN001268151 UNRESOLVED The node assertion is grounded in yeast Atg13 experiments; no human or animal evidence for the specific piecemeal nuclear microautophagy route has been found. |
| GO:0035032 phosphatidylinositol 3-kinase complex, class III | IPI PMID:40442316 Structure and activation of the human autophagy-initiating U... | MARK AS OVER ANNOTATED | Summary: ULK1C (including ATG13) and PI3KC3-C1 coassemble into a supercomplex in vitro. Reason: ATG13 is not a subunit of the class III PI3K complex; the contacts in the supercomplex are made mainly by FIP200 with VPS15, ATG14 and BECN1. The finding is better described as ULK1 complex membership plus physical association with PI3KC3-C1. Supporting Evidence: PMID:40442316 We show that the two complexes coassemble through extensive contacts between the FIP200 scaffold subunit of ULK1C and the VPS15, ATG14 and BECN1 subunits of PI3KC3-C1. PMID:40442316 The FIP200:ATG13:ULK1 core of ULK1C undergoes a rearrangement from 2:1:1 to 2:2:2 stoichiometry in the presence of PI3KC3-C1. |
| GO:0042127 regulation of cell population proliferation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ATG13 knockdown phenocopies ULK1/2 loss, enhancing mTORC1 signalling and cell proliferation. Reason: This is an indirect consequence of ATG13 supporting ULK1 activity, which feeds back on mTORC1; ATG13 itself has no proliferation-specific activity. Supporting Evidence: PMID:21795849 Knockdown of Atg13, the binding partner of ULK1 and ULK2, mimicked the effects of ULK1 or ULK2 deficiency or knockdown. |
| GO:0098780 response to mitochondrial depolarization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ATG13 is recruited to damaged, depolarized mitochondria as part of mitophagy. Reason: Transferred from mouse; consistent with the human mitophagy data but describes a stimulus context rather than an activity. Supporting Evidence: PMID:21855797 required for the phosphorylation and release of Atg13 from Ulk1, and for the recruitment of Atg13 to damaged mitochondria |
| GO:1903059 regulation of protein lipidation | IDA PMID:19225151 ULK-Atg13-FIP200 complexes mediate mTOR signaling to the aut... | MARK AS OVER ANNOTATED | Summary: In the cited study ATG13 knockdown inhibited autophagosome formation but the authors conclude ATG13 may not be essential for LC3 lipidation. Reason: The paper itself argues against a strong role in LC3 lipidation; any effect on lipidation is indirect via autophagosome initiation. Supporting Evidence: PMID:19225151 Atg13, like ULK1 and ULK2, is important for autophagosome formation but may not be essential for the lipidation of LC3 |
| GO:1903749 obsolete positive regulation of protein localization to mitochondrion | HMP PMID:24270810 High-content genome-wide RNAi screens identify regulators of... | MARK AS OVER ANNOTATED | Summary: ATG13 emerged from a genome-wide siRNA screen for regulators of parkin translocation to damaged mitochondria. Reason: The term is reported as obsolete in GOA and the evidence is a high-throughput screen hit. ATG13 has no known role in localizing proteins to mitochondria; its mitophagy role is captured by the mitophagy annotations. |
| GO:1990316 Atg1/ULK1 kinase complex | IBA GO_REF:0000033 | ACCEPT | Summary: ATG13 is a core subunit of the ULK1/2 complex with ULK1/2, FIP200 (RB1CC1) and ATG101. Reason: Directly demonstrated biochemically and structurally; ATG13 bridges ULK1 to FIP200 and binds ATG101 through its HORMA domain. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:1990316 Atg1/ULK1 kinase complex | IEA GO_REF:0000120 | ACCEPT | Summary: ATG13 is a core subunit of the ULK1/2 complex with ULK1/2, FIP200 (RB1CC1) and ATG101. Reason: Directly demonstrated biochemically and structurally; ATG13 bridges ULK1 to FIP200 and binds ATG101 through its HORMA domain. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. |
| GO:1990316 Atg1/ULK1 kinase complex | IPI PMID:19211835 Nutrient-dependent mTORC1 association with the ULK1-Atg13-FI... | ACCEPT | Summary: ATG13 is a core subunit of the ULK1/2 complex with ULK1/2, FIP200 (RB1CC1) and ATG101. Reason: Directly demonstrated biochemically and structurally; ATG13 bridges ULK1 to FIP200 and binds ATG101 through its HORMA domain. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. PMID:19597335 Atg101 associates with the ULK-Atg13-FIP200 complex, most likely through direct interaction with Atg13. |
| GO:1990316 Atg1/ULK1 kinase complex | IPI PMID:19211835 Nutrient-dependent mTORC1 association with the ULK1-Atg13-FI... | ACCEPT | Summary: ATG13 is a core subunit of the ULK1/2 complex with ULK1/2, FIP200 (RB1CC1) and ATG101. Reason: Directly demonstrated biochemically and structurally; ATG13 bridges ULK1 to FIP200 and binds ATG101 through its HORMA domain. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. PMID:19597335 Atg101 associates with the ULK-Atg13-FIP200 complex, most likely through direct interaction with Atg13. |
| GO:1990316 Atg1/ULK1 kinase complex | IPI PMID:19597335 Atg101, a novel mammalian autophagy protein interacting with... | ACCEPT | Summary: ATG13 is a core subunit of the ULK1/2 complex with ULK1/2, FIP200 (RB1CC1) and ATG101. Reason: Directly demonstrated biochemically and structurally; ATG13 bridges ULK1 to FIP200 and binds ATG101 through its HORMA domain. Supporting Evidence: PMID:19211835 Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable approximately 3-MDa protein complex with ULK1 and FIP200. PMID:19597335 Atg101 associates with the ULK-Atg13-FIP200 complex, most likely through direct interaction with Atg13. |
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Download this section (compressed HTML)Q: How do mTORC1 and ULK1 phosphorylation sites on ATG13 change its binding to ULK1, FIP200 and Atg8-family proteins, and does ATG13 dissociate from ULK1 during mitophagy as reported?
Q: What partners occupy the animal-specific hydrophobic pockets of the ATG13-ATG101 HORMA heterodimer?
Experiment: Reconstitute ULK1 kinase activity with purified FIP200, ATG101 and wild-type versus MIM- or LIR-mutant ATG13 on liposomes to separate kinase activation from membrane recruitment.
Hypothesis: ATG13 MIM binding stimulates ULK1 activity, while the LIR and HORMA domains mainly control membrane recruitment.
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