node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
GNBP1 | PGRP-LC | FBpp0074817 | FBpp0088492 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | 0.839 |
GNBP1 | PGRP-LE | FBpp0074817 | FBpp0300347 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Peptidoglycan-recognition protein LE; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to murein peptidoglycans (PGN) of Gram- negative bacteria and activating the imd/Relish pathway. Has no activity against on Gram-positive bacteria. Binds to diaminopimelic acid-type PGN (DAP-type PGN), an activator of the imd/Relish pathway. Functions synergistically with PGRP-LC in producing resistance to E.coli and B.megaterium infections, which have the DAP-type peptidoglycan. Acts both upstream and in parallel with PGRP-LC in the imd/Relish pathway, and is req [...] | 0.835 |
GNBP1 | PGRP-SA | FBpp0074817 | FBpp0073358 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Peptidoglycan-recognition protein SA; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway upstream of spz activating enzyme SPE. Has no activity against Gram-negative bacteria and fungi. Shows some partial redundancy with PRPGP-SD in Gram-positive bacteria recognition. May act by forming a complex with GNBP1 that activates the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway. Binds to diaminopimelic acid-type tetrapeptide PGN (DAP-type PGN) an [...] | 0.999 |
GNBP1 | PGRP-SC1a | FBpp0074817 | FBpp0087786 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Peptidoglycan-recognition protein SC1a; N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity; Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. | 0.941 |
GNBP1 | PGRP-SC2 | FBpp0074817 | FBpp0087788 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Peptidoglycan recognition protein SC2 (PGRP-SC2) encodes a secreted peptidoglycan recognition protein (PGRP) with an amidase activity against peptidoglycans. It contributes to the down-regulation of the immune deficiency pathway, notably in the fat body during systemic bacterial infection. | 0.951 |
GNBP1 | PGRP-SD | FBpp0074817 | FBpp0076519 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Peptidoglycan-recognition protein SD; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway. Has no activity against on Gram-negative bacteria and fungi. Shows some partial redundancy with PRPGP-SA in Gram-positive bacteria recognition. May act by activating the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway. Recognizes S.aureus PGN; Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. | 0.959 |
GNBP1 | SPE | FBpp0074817 | FBpp0083832 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Spaetzle-processing enzyme heavy chain; Endopeptidase which plays a key role in innate immunity by cleaving Tl ligand spz and thereby activating the Toll pathway in response to fungal and Gram-positive bacterial infections. Acts downstream of pathogen recognition receptors PGRP-SA and GNBP1 and protease grass in response to Gram-positive bacterial infection. Acts downstream of protease psh in response to fungal infection. Belongs to the peptidase S1 family. CLIP subfamily. | 0.850 |
GNBP1 | imd | FBpp0074817 | FBpp0311815 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Protein immune deficiency; Essential for the imd/NF-kappa-B (Imd) humoral and epithelial immune response to Gram-negative bacteria. Functions as an adapter protein that transduces immunity signals from the activation of pathogen recognition receptors (PRRs) by bacterial infection to the Imd signaling pathway. Binding of diaminopimelic acid-type (DAP-type) bacterial peptidoglycans (PGN) causes multimerization or clustering of PGRP receptors which activate the Imd cascade probably by recruiting imd, Fadd and Dredd to the receptor complex. Once in proximity, Dredd cleaves imd in a Fadd-de [...] | 0.836 |
GNBP1 | modSP | FBpp0074817 | FBpp0082798 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Modular serine protease non-catalytic chain; Serine protease that plays a key role in innate immunity by activating the Toll pathway in response to infection with Gram-positive bacteria and fungi. During Gram- positive infection, acts downstream of PGRP-SA and upstream of Grass and Spz, and therefore appears to function in a pathway that links detection of Gram-positive lysine-type peptidoglycans to Toll activation. Functions in a separate pathway to the psh-mediated activation of the Toll pathway. Belongs to the peptidase S1 family. | 0.984 |
GNBP1 | psh | FBpp0074817 | FBpp0074400 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | Serine protease persephone; Serine protease that plays a key role in innate immunity in response to Gram-positive bacterial and fungal proteases. Acts as a component of the Toll pathway upstream of protease spz processing enzyme SPE and Tl ligand spz. Nec regulates the cascade by inhibiting psh ; Belongs to the peptidase S1 family. CLIP subfamily. | 0.852 |
PGRP-LC | GNBP1 | FBpp0088492 | FBpp0074817 | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | 0.839 |
PGRP-LC | PGRP-LE | FBpp0088492 | FBpp0300347 | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | Peptidoglycan-recognition protein LE; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to murein peptidoglycans (PGN) of Gram- negative bacteria and activating the imd/Relish pathway. Has no activity against on Gram-positive bacteria. Binds to diaminopimelic acid-type PGN (DAP-type PGN), an activator of the imd/Relish pathway. Functions synergistically with PGRP-LC in producing resistance to E.coli and B.megaterium infections, which have the DAP-type peptidoglycan. Acts both upstream and in parallel with PGRP-LC in the imd/Relish pathway, and is req [...] | 0.969 |
PGRP-LC | PGRP-SA | FBpp0088492 | FBpp0073358 | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | Peptidoglycan-recognition protein SA; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway upstream of spz activating enzyme SPE. Has no activity against Gram-negative bacteria and fungi. Shows some partial redundancy with PRPGP-SD in Gram-positive bacteria recognition. May act by forming a complex with GNBP1 that activates the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway. Binds to diaminopimelic acid-type tetrapeptide PGN (DAP-type PGN) an [...] | 0.407 |
PGRP-LC | PGRP-SD | FBpp0088492 | FBpp0076519 | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | Peptidoglycan-recognition protein SD; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway. Has no activity against on Gram-negative bacteria and fungi. Shows some partial redundancy with PRPGP-SA in Gram-positive bacteria recognition. May act by activating the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway. Recognizes S.aureus PGN; Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. | 0.509 |
PGRP-LC | SPE | FBpp0088492 | FBpp0083832 | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | Spaetzle-processing enzyme heavy chain; Endopeptidase which plays a key role in innate immunity by cleaving Tl ligand spz and thereby activating the Toll pathway in response to fungal and Gram-positive bacterial infections. Acts downstream of pathogen recognition receptors PGRP-SA and GNBP1 and protease grass in response to Gram-positive bacterial infection. Acts downstream of protease psh in response to fungal infection. Belongs to the peptidase S1 family. CLIP subfamily. | 0.524 |
PGRP-LC | imd | FBpp0088492 | FBpp0311815 | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | Protein immune deficiency; Essential for the imd/NF-kappa-B (Imd) humoral and epithelial immune response to Gram-negative bacteria. Functions as an adapter protein that transduces immunity signals from the activation of pathogen recognition receptors (PRRs) by bacterial infection to the Imd signaling pathway. Binding of diaminopimelic acid-type (DAP-type) bacterial peptidoglycans (PGN) causes multimerization or clustering of PGRP receptors which activate the Imd cascade probably by recruiting imd, Fadd and Dredd to the receptor complex. Once in proximity, Dredd cleaves imd in a Fadd-de [...] | 0.998 |
PGRP-LC | modSP | FBpp0088492 | FBpp0082798 | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | Modular serine protease non-catalytic chain; Serine protease that plays a key role in innate immunity by activating the Toll pathway in response to infection with Gram-positive bacteria and fungi. During Gram- positive infection, acts downstream of PGRP-SA and upstream of Grass and Spz, and therefore appears to function in a pathway that links detection of Gram-positive lysine-type peptidoglycans to Toll activation. Functions in a separate pathway to the psh-mediated activation of the Toll pathway. Belongs to the peptidase S1 family. | 0.665 |
PGRP-LC | psh | FBpp0088492 | FBpp0074400 | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | Serine protease persephone; Serine protease that plays a key role in innate immunity in response to Gram-positive bacterial and fungal proteases. Acts as a component of the Toll pathway upstream of protease spz processing enzyme SPE and Tl ligand spz. Nec regulates the cascade by inhibiting psh ; Belongs to the peptidase S1 family. CLIP subfamily. | 0.601 |
PGRP-LE | GNBP1 | FBpp0300347 | FBpp0074817 | Peptidoglycan-recognition protein LE; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to murein peptidoglycans (PGN) of Gram- negative bacteria and activating the imd/Relish pathway. Has no activity against on Gram-positive bacteria. Binds to diaminopimelic acid-type PGN (DAP-type PGN), an activator of the imd/Relish pathway. Functions synergistically with PGRP-LC in producing resistance to E.coli and B.megaterium infections, which have the DAP-type peptidoglycan. Acts both upstream and in parallel with PGRP-LC in the imd/Relish pathway, and is req [...] | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. | 0.835 |
PGRP-LE | PGRP-LC | FBpp0300347 | FBpp0088492 | Peptidoglycan-recognition protein LE; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to murein peptidoglycans (PGN) of Gram- negative bacteria and activating the imd/Relish pathway. Has no activity against on Gram-positive bacteria. Binds to diaminopimelic acid-type PGN (DAP-type PGN), an activator of the imd/Relish pathway. Functions synergistically with PGRP-LC in producing resistance to E.coli and B.megaterium infections, which have the DAP-type peptidoglycan. Acts both upstream and in parallel with PGRP-LC in the imd/Relish pathway, and is req [...] | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] | 0.969 |