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
rplJRibosomal protein L10 (rpl10); Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. (164 aa)    
Predicted Functional Partners:
rplM
Ribosomal protein L13 (rpl13); This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
   
 0.999
rplL
Ribosomal protein L7/L12 (rpl7/l12); Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
 
 
 0.999
rplA
Ribosomal protein L1 (rpl1); Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. Peptides originating from the N-terminal end of L1 have antibacterial activity against bacteria such as E.coli and B.megaterium and modest antifungal activities. Has no effect on H.pylori itself. Peptides are not hemolytic against mammalian cells. These peptides may be released in the stomach during altruistic lysis to kill other fast growing bacteria.
 
 0.999
rplO
Ribosomal protein L15 (rpl15); Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
 0.999
rplR
Ribosomal protein L18 (rpl18); 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
rplF
Ribosomal protein L6 (rpl6); 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.
  
 0.999
rplX
Ribosomal protein L24 (rpl24); One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
  
 0.999
rpmC
Ribosomal protein L29 (rpL29); Similar to SP:P38514 PID:437931 GB:AE000512 percent identity: 45.61; identified by sequence similarity; putative; Belongs to the universal ribosomal protein uL29 family.
  
 0.999
rplP
Ribosomal protein L16 (rpl16); Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
  
 0.999
rplV
Ribosomal protein L22 (rpl22); 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
Your Current Organism:
Helicobacter pylori
NCBI taxonomy Id: 85962
Other names: H. pylori 26695, Helicobacter pylori (strain 26695), Helicobacter pylori 26695, Helicobacter pylori ATCC 700392, Helicobacter pylori KE26695, Helicobacter pylori str. 26695, Helicobacter pylori strain 26695
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.