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
rplA50S ribosomal protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. (231 aa)    
Predicted Functional Partners:
rplK
50S ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
 
 0.999
rplJ
50S ribosomal 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.
 
 0.999
rplL
50S ribosomal protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family.
 
 
 0.999
rplW
50S ribosomal 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.
  
 0.999
rplV
50S ribosomal protein L22; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).
  
 0.999
rpmC
Similar to RL29_VIBCH (Q9KNZ2) 50S ribosomal protein L29 from Vibrio cholerae (63 aa). FASTA: opt: 190 Z-score: 279.3 E(): 1.2e-07 Smith-Waterman score: 190; 45.614 identity in 57 aa overlap; Belongs to the universal ribosomal protein uL29 family.
  
 0.999
rplR
50S ribosomal 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.
  
 0.999
rpmD
Similar to Q9JQT4 (Q9JQT4) 50S ribosomal protein L30 from Neisseria meningitidis (61 aa). FASTA: opt: 259 Z-score: 408.8 E(): 7e-15 Smith-Waterman score: 259; 68.333 identity in 60 aa overlap.
  
 0.999
rpsB
Similar to RS2_SPIPL (P34831) 30S ribosomal protein S2 from Spirulina platensis (251 aa). FASTA: opt: 953 Z-score: 1141.6 E(): 1.1e-55 Smith-Waterman score: 953; 61.364 identity in 220 aa overlap; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.998
rplC
50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
  
 0.998
Your Current Organism:
Francisella tularensis SCHUS4
NCBI taxonomy Id: 177416
Other names: F. tularensis subsp. tularensis SCHU S4, Francisella tularensis Biovar A str. SCHU S4, Francisella tularensis Biovar A str. Schu 4, Francisella tularensis subsp. tularensis SCHU S4, Francisella tularensis subsp. tularensis Schu 4, Francisella tularensis subsp. tularensis str. SCHU S4, Francisella tularensis subsp. tularensis strain SCHU S4
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.