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 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
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation.
Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis.
Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule.
Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways.
Caspase-8 and caspase-10 activate NF-kappaB through RIP, NIK and IKKalpha kinases.
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes.
The inhibitor ABIN-2 disrupts the interaction of receptor-interacting protein with the kinase subunit IKKgamma to block activation of the transcription factor NF-kappaB and potentiate apoptosis.
TRAF7 potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis.
IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction.
Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis.
Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1.
Caspase-8 prevents sustained activation of NF-kappaB in monocytes undergoing macrophagic differentiation.
RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation.
RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation.
From death receptor to reactive oxygen species and c-Jun N-terminal protein kinase: the receptor-interacting protein 1 odyssey.
IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis.
Involvement of Ymer in suppression of NF-kappaB activation by regulated interaction with lysine-63-linked polyubiquitin chain.
Casein kinase 1alpha interacts with RIP1 and regulates NF-kappaB activation.
CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation.
TNF-alpha induces two distinct caspase-8 activation pathways.
ABIN-1 is a ubiquitin sensor that restricts cell death and sustains embryonic development.
Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha.
Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation.
Proteinase-activated receptor-2 mediated inhibition of TNFalpha-stimulated JNK activation - A novel paradigm for G(q/11) linked GPCRs.
MicroRNA-155 prevents necrotic cell death in human cardiomyocyte progenitor cells via targeting RIP1.
Annexin-1 interacts with NEMO and RIP1 to constitutively activate IKK complex and NF-κB: implication in breast cancer metastasis.
NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-α feedforward signaling.
TWEAK induces apoptosis through a death-signaling complex comprising receptor-interacting protein 1 (RIP1), Fas-associated death domain (FADD), and caspase-8.
cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms.
AWP1 binds to tumor necrosis factor receptor-associated factor 2 (TRAF2) and is involved in TRAF2-mediated nuclear factor-kappaB signaling.
Control of NOD2 and Rip2-dependent innate immune activation by GEF-H1.
cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).
Smac mimetic bypasses apoptosis resistance in FADD- or caspase-8-deficient cells by priming for tumor necrosis factor α-induced necroptosis.
RIP1 is required for IAP inhibitor-mediated sensitization of childhood acute leukemia cells to chemotherapy-induced apoptosis.
Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase.
The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways.
Pick your poison: the Ripoptosome, a cell death platform regulating apoptosis and necroptosis.
The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis.
Vesicles released by activated T cells induce both Fas-mediated RIP-dependent apoptotic and Fas-independent nonapoptotic cell deaths.
Immunodeficiency, autoinflammation and amylopectinosis in humans with inherited HOIL-1 and LUBAC deficiency.
Ubiquitin-specific protease 4 promotes TNF-α-induced apoptosis by deubiquitination of RIP1 in head and neck squamous cell carcinoma.
Structural basis of RIP1 inhibition by necrostatins.
Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains.
A type III effector antagonizes death receptor signalling during bacterial gut infection.
SH3RF2 functions as an oncogene by mediating PAK4 protein stability.
In silico prediction of physical protein interactions and characterization of interactome orphans.
A proteome-scale map of the human interactome network.
WDFY1 mediates TLR3/4 signaling by recruiting TRIF.
The seventh zinc finger motif of A20 is required for the suppression of TNF-α-induced apoptosis.
MicroRNA analysis suggests an additional level of feedback regulation in the NF-κB signaling cascade.
Herpes Simplex Virus 1 (HSV-1) and HSV-2 Mediate Species-Specific Modulations of Programmed Necrosis through the Viral Ribonucleotide Reductase Large Subunit R1.
Death-domain dimerization-mediated activation of RIPK1 controls necroptosis and RIPK1-dependent apoptosis.
PELI1 Selectively Targets Kinase-Active RIP3 for Ubiquitylation-Dependent Proteasomal Degradation.
A protein-protein interaction map of the TNF-induced NF-κB signal transduction pathway.
Serine 25 phosphorylation inhibits RIPK1 kinase-dependent cell death in models of infection and inflammation.
A dominant autoinflammatory disease caused by non-cleavable variants of RIPK1.
A reference map of the human binary protein interactome.
A SARS-CoV-2 protein interaction map reveals targets for drug repurposing.
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.
Structural insights into the disruption of TNF-TNFR1 signalling by small molecules stabilising a distorted TNF.
A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF.
The Role of Tumor Necrosis Factor Alpha (TNF-α) in Autoimmune Disease and Current TNF-α Inhibitors in Therapeutics.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
SARS-CoV-2 promotes RIPK1 activation to facilitate viral propagation.
Novel biochemical, structural, and systems insights into inflammatory signaling revealed by contextual interaction proteomics.
A comprehensive SARS-CoV-2-human protein-protein interactome reveals COVID-19 pathobiology and potential host therapeutic targets.
Death by TNF: a road to inflammation.
Curcumin alleviates experimental colitis in mice by suppressing necroptosis of intestinal epithelial cells.
RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death.
TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex.
CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP.
Caspase-8 processing in the DISC
TRADD:TRAF2:RIP1 binds FADD
TNF-mediated dimerization of procaspase-8
K63-linked ubiquitination of RIP1 bound to the activated TLR complex
TRIF:activated TLR3/TLR4 complex recruits RIP1
Viral dsRNA:TLR3:TRIF complex recruits RIP1
MAVS interacts with RIPK1 and FADD
ZBP1(DAI) recruits RIP1 and RIP3
TLR4-induced ripoptosome assembly
Caspase-8 processing within TLR4 complex
FLIP(L) and procaspase-8 form heterodimer in TNF signaling
FLIP(S) and procaspase-8 form heterodimer
Caspase-8 and FLIP(L) processing at DISC
RIPK1-mediated regulated necrosis
RIPK1:RIPK3 oligomer binds MLKL
RIPK1:RIPK3 oligomerizes to form amyloid-like fibrils
RIPK3 phosphorylates MLKL
BIRC(cIAP1/2) ubiquitinates RIPK1
TNF:TNFR1:TRADD:TRAF2:K63polyUb-RIPK1:BIRC2,3:LUBAC recruits IKKA:IKBKB:IKBKG
TNF:TNFR1:TRADD:TRAF2:RIPK1 recruits BIRC2/3 (cIAP1/2)
RIPK1 is cleaved by CASP8
K63polyUb-RIPK1 is deubiquitinated
TNF:TNFR1:TRADD:TRAF2:K63polyUb-RIPK1:BIRC2/3:LUBAC recruits TAK1 complex
TNF:TNFR1:TRADD:TRAF2:RIPK1 binds LUBAC
CLIP3 and CYLD bind TNF signaling complex
TRAF1 binds TRAF2 within TNFR1 signaling complex
FLIP(L) and procaspase-8 form heterodimer
USP21 deubiquitinates RIPK1,DDX58
TNFAIP3 (A20) ubiquitinates RIPK1
TNFAIP3 (A20) deubiquitinates K63polyUb-RIPK1
TAX1BP1:TNFAIP3(A20) binds RIPK1-containing complexes
TNFAIP3 (A20) ubiquitinates RIPK1 with K48-linked Ub chains
CYLD deubiquitinates K63polyUb-TRAF2,K63polyUb-TRAF6,K63polyUb-RIPK1,K63polyUb-IKBKG
TRADD:TRAF2:RIP1:FADD binds pro-caspase 8
TRADD:TRAF2:RIP1 dissociates from TNF-α:TNFR1
TNF:TNFR1 binds TRADD, TRAF2 and RIPK1
TLR3-induced ripoptosome assembly
Caspase-8 processing within TLR3 complex
K63-linked ubiquitination of RIP1 bound to the activated TLR complex
IKBKG subunit of IKK complex binds K63pUb- RIP1 within the TLR3 complex
Dimerzation of procaspase-8, procaspase-10
Recruitment of caspase-8 and -10 to FADD complex
Recruitment of IKK complex
IKBKG subunit of IKK complex binds polyubiquinated RIP1
SARS-CoV-1 3a oligomerizes
SARS-CoV-1 3a binds the lysosomal membrane
SARS-CoV-1 3a binds RIPK1:RIPK3 oligomer
PELI1 ubiquitinates RIPK3 at K363
PELI1 binds activated RIPK1:RIPK3
MLKL binds IP4, IP5 and IP6
MLKL binds PDCD6IP and SDCBP
RIPK1 variant is not cleaved by CASP8
Small molecule inhibitor binds RIPK1, RIPK3
Caspase-8 and FLIP(L) processing at TNFR signaling complex
RIPK1 is cleaved by CASP8:FLIP(L)
ITCH polyubiquitinates MLKL at K50
LUBAC ubiquitinates RIPK1 at K627
OPTN binds polyUb-RIPK1 within the TNFR1 complex
MIB2 binds RIPK1 within TNF-α:TNFR1:TRADD:RIPK1:TRAF2
MIB2 ubiquitinates RIPK1 at K377, K604, K634
CYLD:SPATA2:LUBAC binds TNFR1 signaling complex
STUB1 ubiquitinates RIPK1 at K571, K604, K627
MAPKAPK2 phosphorylates RIPK1 at S320
SPATA2:CYLD-bound LUBAC ubiquitinates RIPK1 at K627 within the TNFR1 signaling complex
TBK1, IKBKE phosphorylate RIPK1 at T189
CYLD hydrolyses K63polyUb on RIPK1 within the TNFR1 complex
TBK1, IKBKE binds Met1-polyUb within the TNFR1 complex
CHUK, IKBKB phosphorylate RIPK1 at S25
CYLD hydrolyses M1polyUb on RIPK1 within the TNFR1 complex
ULK1 phosphorylates RIPK1 at S357
OPTN recruits CYLD to the TNFR1 complex