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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
rplXLSU ribosomal protein L24p (L26e); One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. (104 aa)    
Predicted Functional Partners:
rplN
50S ribosomal subunit protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
 
 0.999
rplW
50S ribosomal subunit protein L23; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family.
 
 0.998
rplV
50S ribosomal subunit protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
 
 0.998
rpmC
50S ribosomal subunit protein L29; Protein involved in structural constituent of ribosome and translation; Belongs to the universal ribosomal protein uL29 family.
  
 0.998
rplE
50S ribosomal subunit protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
 
 0.998
rplF
50S ribosomal subunit protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
 
 0.998
rplR
50S ribosomal subunit protein L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
 
 0.998
rpmD
50S ribosomal subunit protein L30; Protein involved in structural constituent of ribosome and translation.
 
 0.998
rplJ
50S ribosomal subunit protein L10; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family.
 
 0.997
rpsH
30S ribosomal subunit protein S8; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit; Belongs to the universal ribosomal protein uS8 family.
 
 0.996
Your Current Organism:
Dickeya dadantii
NCBI taxonomy Id: 198628
Other names: D. dadantii 3937, Dickeya dadantii 3937, Dickeya dadantii str. 3937, Dickeya dadantii strain 3937, Erwinia chrysanthemi str. 3937, Pectobacterium chrysanthemi str. 3937
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.