node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACVR1 | RNF149 | ENSP00000263640 | ENSP00000295317 | Activin receptor type-1; On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity) | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | 0.643 |
FAM151B | RNF149 | ENSP00000282226 | ENSP00000295317 | Protein FAM151B; Family with sequence similarity 151 member B | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | 0.541 |
GNG10 | RNF149 | ENSP00000363411 | ENSP00000295317 | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Interacts with beta-1 and beta-2, but not with beta-3 | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | 0.567 |
IL1R2 | LONRF3 | ENSP00000330959 | ENSP00000360690 | Interleukin-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 | LON peptidase N-terminal domain and ring finger 3 | 0.496 |
IL1R2 | RNF149 | ENSP00000330959 | ENSP00000295317 | Interleukin-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 | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | 0.586 |
IL1R2 | TBC1D8 | ENSP00000330959 | ENSP00000366036 | Interleukin-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 | TBC1 domain family member 8; May act as a GTPase-activating protein for Rab family protein(s); GRAM domain containing | 0.567 |
IL1RAPL1 | LONRF3 | ENSP00000368278 | ENSP00000360690 | Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family | LON peptidase N-terminal domain and ring finger 3 | 0.553 |
IL1RAPL1 | RNF149 | ENSP00000368278 | ENSP00000295317 | Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | 0.627 |
IL1RAPL1 | TBC1D8 | ENSP00000368278 | ENSP00000366036 | Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family | TBC1 domain family member 8; May act as a GTPase-activating protein for Rab family protein(s); GRAM domain containing | 0.627 |
IL1RAPL2 | LONRF3 | ENSP00000361663 | ENSP00000360690 | Interleukin 1 receptor accessory protein like 2; Belongs to the interleukin-1 receptor family | LON peptidase N-terminal domain and ring finger 3 | 0.400 |
IL1RAPL2 | RNF149 | ENSP00000361663 | ENSP00000295317 | Interleukin 1 receptor accessory protein like 2; Belongs to the interleukin-1 receptor family | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | 0.539 |
IL1RAPL2 | TBC1D8 | ENSP00000361663 | ENSP00000366036 | Interleukin 1 receptor accessory protein like 2; Belongs to the interleukin-1 receptor family | TBC1 domain family member 8; May act as a GTPase-activating protein for Rab family protein(s); GRAM domain containing | 0.544 |
LONRF3 | IL1R2 | ENSP00000360690 | ENSP00000330959 | LON peptidase N-terminal domain and ring finger 3 | Interleukin-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 | 0.496 |
LONRF3 | IL1RAPL1 | ENSP00000360690 | ENSP00000368278 | LON peptidase N-terminal domain and ring finger 3 | Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family | 0.553 |
LONRF3 | IL1RAPL2 | ENSP00000360690 | ENSP00000361663 | LON peptidase N-terminal domain and ring finger 3 | Interleukin 1 receptor accessory protein like 2; Belongs to the interleukin-1 receptor family | 0.400 |
LONRF3 | RNF149 | ENSP00000360690 | ENSP00000295317 | LON peptidase N-terminal domain and ring finger 3 | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | 0.681 |
LONRF3 | TBC1D8 | ENSP00000360690 | ENSP00000366036 | LON peptidase N-terminal domain and ring finger 3 | TBC1 domain family member 8; May act as a GTPase-activating protein for Rab family protein(s); GRAM domain containing | 0.694 |
RNF149 | ACVR1 | ENSP00000295317 | ENSP00000263640 | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | Activin receptor type-1; On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity) | 0.643 |
RNF149 | FAM151B | ENSP00000295317 | ENSP00000282226 | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | Protein FAM151B; Family with sequence similarity 151 member B | 0.541 |
RNF149 | GNG10 | ENSP00000295317 | ENSP00000363411 | E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Interacts with beta-1 and beta-2, but not with beta-3 | 0.567 |