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  • 11.0 [archived version]
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IRAK2 IRAK2 IL1RL1 IL1RL1 IL1RAP IL1RAP IL1R1 IL1R1 TNFAIP3 TNFAIP3 GPANK1 GPANK1 TBK1 TBK1 FADD FADD CCDC103 CCDC103 IL1R2 IL1R2 IL18R1 IL18R1 CASP8 CASP8 IL18BP IL18BP CASP3 CASP3 SMAD3 SMAD3 IL37 IL37 IL1RL2 IL1RL2 CASP1 CASP1 IL18RAP IL18RAP CASP4 CASP4 ZSCAN12 ZSCAN12 CASP5 CASP5 CARD16 CARD16 GSG1 GSG1 CARD18 CARD18 CARD17 CARD17
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
IL1RL1Interleukin-1 receptor-like 1; Receptor for interleukin-33 (IL-33); signaling requires association of the coreceptor IL1RAP. Its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function; I-set domain containing (556 aa)
IRAK2Interleukin-1 receptor-associated kinase-like 2; Binds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization (625 aa)
IL37Interleukin-37; Suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. This function requires SMAD3. Suppresses, or reduces, proinflammatory cytokine production, including IL1A and IL6, as well as CCL12, CSF1, CSF2, CXCL13, IL1B, IL23A and IL1RN, but spares anti-inflammatory cytokines. Inhibits dendritic cell activation; Interleukins (218 aa)
IL1RL2Interleukin-1 receptor-like 2; Receptor for interleukin-36 (IL36A, IL36B and IL36G). After binding to interleukin-36 associates with the coreceptor IL1RAP to form the interleukin-36 receptor complex which mediates interleukin-36-dependent activation of NF-kappa-B, MAPK and other pathways (By similarity). The IL-36 signaling system is thought to be present in epithelial barriers and to take part in local inflammatory response; it is similar to the IL-1 system. Seems to be involved in skin inflammatory response by induction of the IL- 23/IL-17/IL-22 pathway; Immunoglobulin like domain co [...] (575 aa)
IL18RAPInterleukin-18 receptor accessory protein; Within the IL18 receptor complex, does not mediate IL18- binding, but involved in IL18-dependent signal transduction, leading to NF-kappa-B and JNK activation (599 aa)
FADDFAS-associated death domain protein; Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling; Death effector domain containing (208 aa)
CASP3Caspase-3; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage (277 aa)
IL1RAPInterleukin 1 receptor accessory protein; Immunoglobulin like domain containing (687 aa)
TBK1Serine/threonine-protein kinase TBK1; Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents. Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB. In order to establish such an antiviral state, TBK1 form s [...] (729 aa)
IL1R2Interleukin-1 receptor type 2; Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors; CD molecules (398 aa)
SMAD3Mothers against decapentaplegic homolog 3; Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and mi [...] (425 aa)
CASP8Caspase-8; Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death- inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, [...] (538 aa)
ZSCAN12Zinc finger and SCAN domain-containing protein 12; May be involved in transcriptional regulation; SCAN domain containing (604 aa)
CARD16Caspase recruitment domain-containing protein 16; Caspase inhibitor. Acts as a regulator of procaspase- 1/CASP1 activation implicated in the regulation of the proteolytic maturation of pro-interleukin-1 beta (IL1B) and its release during inflammation. Inhibits the release of IL1B in response to LPS in monocytes. Also induces NF-kappa-B activation during the pro- inflammatory cytokine response. Also able to inhibit CASP1- mediated neuronal cell death, TNF-alpha, hypoxia-, UV-, and staurosporine-mediated cell death but not ER stress-mediated cell death. Acts by preventing activation of c [...] (197 aa)
CARD17Caspase recruitment domain-containing protein 17; Regulator of procaspase-1/CASP1 activation implicated in the regulation of the proteolytic maturation of pro-IL-1beta/IL1B and its release during inflammation. Inhibits the release of IL1B in response to LPS in monocytes. However, unlike CASP1, do not induce NF-kappa-B activation; Caspase recruitment domain containing (110 aa)
GPANK1G-patch domain and ankyrin repeats 1 (356 aa)
CASP5Caspase-5; Mediator of programmed cell death (apoptosis). During non-canonical inflammasome activation, cuts MB21D1 and may play a role in the regulation of antiviral innate immune activation; Caspase recruitment domain containing (447 aa)
IL18BPInterleukin-18-binding protein; Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response; Immunoglobulin like domain containing (194 aa)
IL1R1Interleukin-1 receptor type 1; Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex (569 aa)
IL18R1Interleukin-18 receptor 1; Within the IL18 receptor complex, responsible for the binding of the proinflammatory cytokine IL18, but not IL1A nor IL1B (Probable). Contributes to IL18-induced cytokine production, either independently of SLC12A3, or as a complex with SLC12A3 (By similarity); CD molecules (541 aa)
CASP4Caspase-4; Inflammatory caspase. Essential effector of NLRP3 inflammasome- dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation, cholera enterotoxin subunit B and cytosolic LPS. Independently of NLRP3 inflammasome and CASP1, promotes pyroptosis, through GSDMD cleavage and activation, and IL1A, IL18 and HMGB1 release in response to non-canonical inflammasome activators. Plays a crucial role in the restriction of Salmonella typhimurium replication in colonic epithelial cells during infection. In later stages of the infectio [...] (377 aa)
CCDC103Coiled-coil domain containing 103; Dynein-attachment factor required for cilia motility; Belongs to the CCDC103/PR46b family (242 aa)
GSG1Germ cell-specific gene 1 protein; May cause the redistribution of PAPOLB from the cytosol to the endoplasmic reticulum (339 aa)
CASP1Caspase-1; Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of MB21D1/cGAS, rendering it inactive; Belongs to the peptidase C14A family (404 aa)
CARD18Caspase recruitment domain-containing protein 18; Inhibits generation of IL-1-beta by interacting with caspase-1 and preventing its association with RIP2. Down-regulates the release of IL1B; Caspase recruitment domain containing (90 aa)
TNFAIP3Tumor necrosis factor alpha-induced protein 3; Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in [...] (790 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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