STRINGSTRING
STRING protein interaction network
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.
Node Color
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:
a 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 to 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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
PGRP-LDPeptidoglycan-recognition protein LD; Peptidoglycan-recognition protein probably involved in innate immunity by binding to peptidoglycans (PGN) of bacteria and activating the immune response; Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. (327 aa)    
Predicted Functional Partners:
PGRP-LA
Peptidoglycan-recognition protein LA; Peptidoglycan-recognition protein probably involved in innate immunity by binding to peptidoglycans (PGN) of bacteria and activating the immune response.
     
 0.982
PGRP-LC
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 [...]
     
0.925
PGRP-LB
Peptidoglycan recognition protein LB (PGRP-LB) encodes a secreted protein with an amidase activity that scavenges DAP-type peptidoglycan, a cell wall component found on Gram-negative bacteria and certain Gram positive bacteria. It negatively regulates the immune deficiency pathway; Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
      
 0.794
PGRP-LE
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 [...]
      
 0.626
Tep1
Thioester-containing protein 1; Endopeptidase inhibitor activity. It is involved in the biological process described with: innate immune response.
      
 0.625
PGRP-SB2
Peptidoglycan recognition protein SB2 (PGRP-SB2) encodes a secreted peptidoglycan recognition protein (PGRP) with amidase activity against DAP-type peptidoglycan, a cell wall component found on Gram-negative bacteria and certain Gram positive bacteria. It is strongly induced upon bacterial infection by the immune deficiency pathway, suggesting a role as an immune effector.
      
 0.609
Sc2
Sc2; Oxidoreductase activity; oxidoreductase activity, acting on the CH-CH group of donors. It is involved in the biological process described with: very long-chain fatty acid biosynthetic process.
      
 0.603
imd
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 [...]
      
 0.512
GNBP1
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.
      
 0.438
GNBP3
Gram-negative bacteria binding protein 3 (GNBP3) encodes a hemolymphatic protein involved in the sensing of glucan (a fungal cell wall component) upstream of the Toll pathway.
      
 0.430
Your Current Organism:
Drosophila melanogaster
NCBI taxonomy Id: 7227
Other names: D. melanogaster, Diptera sp. DNAS-2A9-224646, Sophophora melanogaster, fruit fly
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