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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
FliYFlagellum motor switch protein. (422 aa)    
Predicted Functional Partners:
FliM
Flagellar motor switch protein.
 0.999
FliG
Flagellar motor switch protein.
 
 0.999
FlgC
Flagellar basal body rod protein; Belongs to the flagella basal body rod proteins family.
 
 
 0.999
FlgK
Flagellar hook-associated protein.
 
 
 0.998
CheD
Chemotaxis protein; Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis; Belongs to the CheD family.
 
 
 0.997
FliI
Flagellar biosynthesis/type III secretory pathway ATPase.
 
 
 0.996
FliP
Flagellar biosynthesis pathway, component FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family.
 
 0.995
FliQ
Flagellar biosynthesis pathway, component FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family.
 
 
 0.994
FliS
Flagellin-specific chaperone FliS.
 
  
 0.992
FliD
Flagellar capping protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
 
  
 0.992
Your Current Organism:
Pelotomaculum thermopropionicum
NCBI taxonomy Id: 370438
Other names: P. thermopropionicum SI, Pelotomaculum thermopropionicum SI, Pelotomaculum thermopropionicum str. SI, Pelotomaculum thermopropionicum strain SI
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