Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation.
Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes.
Unc-51-like kinase 1/2-mediated endocytic processes regulate filopodia extension and branching of sensory axons.
siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy.
Identification of new kinase clusters required for neurite outgrowth and retraction by a loss-of-function RNA interference screen.
Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism.
Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy.
ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery.
Atg101, a novel mammalian autophagy protein interacting with Atg13.
Network organization of the human autophagy system.
The dynamic interaction of AMBRA1 with the dynein motor complex regulates mammalian autophagy.
The association of AMPK with ULK1 regulates autophagy.
ULK1 inhibits the kinase activity of mTORC1 and cell proliferation.
Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC.
Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy.
TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes.
Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8 regulates autophagy.
FIP200 regulates targeting of Atg16L1 to the isolation membrane.
mTOR inhibits autophagy by controlling ULK1 ubiquitylation, self-association and function through AMBRA1 and TRAF6.
Structural basis of the autophagy-related LC3/Atg13 LIR complex: recognition and interaction mechanism.
TBC1D5 and the AP2 complex regulate ATG9 trafficking and initiation of autophagy.
FLCN, a novel autophagy component, interacts with GABARAP and is regulated by ULK1 phosphorylation.
TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition.
AMBRA1 links autophagy to cell proliferation and tumorigenesis by promoting c-Myc dephosphorylation and degradation.
Huntingtin functions as a scaffold for selective macroautophagy.
IRGM governs the core autophagy machinery to conduct antimicrobial defense.
TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity.
Targeting PDK1 with dichloroacetophenone to inhibit acute myeloid leukemia (AML) cell growth.
Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to induce motor neuron dysfunction and cell death.
The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy.
Multiplex image-based autophagy RNAi screening identifies SMCR8 as ULK1 kinase activity and gene expression regulator.
Hepatitis C virus triggers Golgi fragmentation and autophagy through the immunity-related GTPase M.
WIPI3 and WIPI4 β-propellers are scaffolds for LKB1-AMPK-TSC signalling circuits in the control of autophagy.
A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B.
The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity to Control ER-Isolation Membrane Contacts for Autophagosome Formation.
The deubiquitinating enzyme USP20 stabilizes ULK1 and promotes autophagy initiation.
The C9orf72-interacting protein Smcr8 is a negative regulator of autoimmunity and lysosomal exocytosis.
Autophagy induction in atrophic muscle cells requires ULK1 activation by TRIM32 through unanchored K63-linked polyubiquitin chains.
The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.
The Autophagy-Initiating Kinase ULK1 Controls RIPK1-Mediated Cell Death.
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated assembly of the SNARE complex required for autolysosome formation.
The papain-like protease of coronaviruses cleaves ULK1 to disrupt host autophagy.
Global Proximity Interactome of the Human Macroautophagy Pathway.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
TRIM27 cooperates with STK38L to inhibit ULK1-mediated autophagy and promote tumorigenesis.
Phosphorylation of phase-separated p62 bodies by ULK1 activates a redox-independent stress response.
Structure and activation of the human autophagy-initiating ULK1C:PI3KC3-C1 supercomplex.
Human ULK1, a novel serine/threonine kinase related to UNC-51 kinase of Caenorhabditis elegans: cDNA cloning, expression, and chromosomal assignment.
ULK1 phosphorylates AMBRA1:BECN1 complex
Regulation of TNFR1 signaling
AMPK (complex) phosphorylates ULK1 (complex)
Thr-180 of ULK1 is phosphorylated
Active MTORC1 phosphorylates ULK1
p-AMPK:AMP binds the ULK complex
Active MTORC1 binds the ULK1 complex
p-AMPK:AMP phosphorylates Raptor in the MTORC1 complex
MTORC1 dissociates from ULK complex
ULK1 phosphorylates ATG13 and RB1CC1
ULK1 phosphorylates Beclin-1
ULK complex translocates to the ER
TBC1D14 binds RAB11 and ULK1
p-ULK1 phosphorylates DENND3
Receptor Mediated Mitophagy
ULK1 Translocates to the mitochondria
FUNDC1 is phosphorylated by ULK1 at Ser17
ULK1 phosphorylates RIPK1 at S357
Palmitoylation of ULK1 by ZDHHC13 plays a crucial role in autophagy.