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
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling.
The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation.
The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA.
ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response.
ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization.
STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity.
WDR5 is essential for assembly of the VISA-associated signaling complex and virus-triggered IRF3 and NF-kappaB activation.
Tom70 mediates activation of interferon regulatory factor 3 on mitochondria.
IFI16 is an innate immune sensor for intracellular DNA.
The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA.
IFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging MAVS and TBK1.
Mapping a dynamic innate immunity protein interaction network regulating type I interferon production.
STING is a direct innate immune sensor of cyclic di-GMP.
Activation of STAT6 by STING is critical for antiviral innate immunity.
Coronavirus papain-like proteases negatively regulate antiviral innate immune response through disruption of STING-mediated signaling.
STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway.
Cyclic di-GMP sensing via the innate immune signaling protein STING.
Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system.
The structural basis for the sensing and binding of cyclic di-GMP by STING.
Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP.
Tetraspanin 6 (TSPAN6) negatively regulates retinoic acid-inducible gene I-like receptor-mediated immune signaling in a ubiquitination-dependent manner.
Hepatitis C virus NS4B protein targets STING and abrogates RIG-I-mediated type I interferon-dependent innate immunity.
Hepatitis C virus NS4B blocks the interaction of STING and TBK1 to evade host innate immunity.
Cyclic GMP-AMP containing mixed phosphodiester linkages is an endogenous high-affinity ligand for STING.
Structure-function analysis of STING activation by c[G(2',5')pA(3',5')p] and targeting by antiviral DMXAA.
NLRC3, a member of the NLR family of proteins, is a negative regulator of innate immune signaling induced by the DNA sensor STING.
SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3-TBK1 complex.
RNF26 temporally regulates virus-triggered type I interferon induction by two distinct mechanisms.
The ER-associated protein ZDHHC1 is a positive regulator of DNA virus-triggered, MITA/STING-dependent innate immune signaling.
Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation.
DNA tumor virus oncogenes antagonize the cGAS-STING DNA-sensing pathway.
Rat and human STINGs profile similarly towards anticancer/antiviral compounds.
Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins.
Ubiquitination of STING at lysine 224 controls IRF3 activation.
Quantitative Proteomics Identified TTC4 as a TBK1 Interactor and a Positive Regulator of SeV-Induced Innate Immunity.
ZDHHC11 modulates innate immune response to DNA virus by mediating MITA-IRF3 association.
Pro-inflammation Associated with a Gain-of-Function Mutation (R284S) in the Innate Immune Sensor STING.
Targeting STING with covalent small-molecule inhibitors.
Inhibition of AIM2 inflammasome activation by a novel transcript isoform of IFI16.
The Kinase IKKβ Regulates a STING- and NF-κB-Dependent Antiviral Response Pathway in Drosophila.
Design of amidobenzimidazole STING receptor agonists with systemic activity.
TMED2 Potentiates Cellular IFN Responses to DNA Viruses by Reinforcing MITA Dimerization and Facilitating Its Trafficking.
STING directly activates autophagy to tune the innate immune response.
Structural basis of STING binding with and phosphorylation by TBK1.
Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP.
Autophagy induction via STING trafficking is a primordial function of the cGAS pathway.
STING Polymer Structure Reveals Mechanisms for Activation, Hyperactivation, and Inhibition.
HIV-2/SIV Vpx targets a novel functional domain of STING to selectively inhibit cGAS-STING-mediated NF-κB signalling.
TBK1 and IKKε Act Redundantly to Mediate STING-Induced NF-κB Responses in Myeloid Cells.
A reference map of the human binary protein interactome.
STEEP mediates STING ER exit and activation of signaling.
EGFR-mediated tyrosine phosphorylation of STING determines its trafficking route and cellular innate immunity functions.
The cGAS-STING pathway as a therapeutic target in inflammatory diseases.
Human Cytomegalovirus UL138 Protein Inhibits the STING Pathway and Reduces Interferon Beta mRNA Accumulation during Lytic and Latent Infections.
Gain-of-function genetic screening identifies the antiviral function of TMEM120A via STING activation.
Activation of STING by targeting a pocket in the transmembrane domain.
Varicella-Zoster Virus ORF39 Transmembrane Protein Suppresses Interferon-Beta Promoter Activation by Interacting with STING.
The mechanism of STING autoinhibition and activation.
MicroRNA-4691-3p inhibits the inflammatory response by targeting STING in human dental pulp cells: A laboratory investigation.
Human STING is a proton channel.
TAK1 is an essential kinase for STING trafficking.
HERC5-catalyzed ISGylation potentiates cGAS-mediated innate immunity.
PELI2 is a negative regulator of STING signaling that is dynamically repressed during viral infection.
IKKɛ induces STING non-IFN immune responses via a mechanism analogous to TBK1.
A TBK1-independent primordial function of STING in lysosomal biogenesis.
The cGAS-STING pathway activates transcription factor TFEB to stimulate lysosome biogenesis and pathogen clearance.
ArfGAP2 promotes STING proton channel activity, cytokine transit, and autoinflammation.
Beyond interferons: Non-canonical roles of MITA/STING.
STING signals to NF-κB from late endolysosomal compartments using IRF3 as an adaptor.
Regulation of STING activation by phosphoinositide and cholesterol.
PtdIns(3,5)P(2) is an endogenous ligand of STING in innate immune signalling.
STING-NF-κB signaling builds an influenza spillover barrier.
TRIM69 potentiates the cGAS-STING signalling pathway by promoting STING ubiquitination.
STING signaling modulation by COPII cargo recognition.
STING recruits TBK1 and IRF3
STING binds TRIM32 or TRIM56
TBK1 is phosphorylated within STING:TBK1:IRF3 complex
IRF3 is phosphorylated by TBK1
STING ubiquitination by TRIM32 or TRIM56
DENV protease NS2B3 binds STING
DENV protease NS2B3 cleaves STING
STING binds cyclic GMP-AMP
TBK1 phosphorylates STAT6 at Ser407
STING recruits TBK1 and STAT6
TBK1 is phosphorylated within STING:TBK1:STAT6 complex
NLRP4 and DTX4 associate with p-S172-TBK1 within STING:TBK1:IRF3
Exocytosis of secretory granule membrane proteins
DTX4 ubiquitinates p-S172-TBK1 within NLRP4:DTX4:STING:TBK1:IRF3
SARS-CoV-1 nsp3 deubiquinates K63-linked pUb-STING
SARS-CoV-2 3CLpro dimer binds to STING
SARS-CoV-2 3a binds to STING
Publisher Correction: PtdIns(3,5)P(2) is an endogenous ligand of STING in innate immune signalling.
Glues that can STING: Lipids in innate immunity.
Membrane lipids regulate the STING pathway and type I interferon responses.
STING mediates lysosomal quality control and recovery through its proton channel function and TFEB activation in lysosomal storage disorders.
C92, a proton channel-blocking allosteric STING agonist generates robust antitumor activity.