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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
rplALSU ribosomal protein L1p (L10Ae); Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. (233 aa)    
Predicted Functional Partners:
rplL
LSU ribosomal protein L7/L12 (L23e); 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
rplJ
LSU ribosomal protein L10p (P0); 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
rplK
LSU ribosomal protein L11p (L12e); Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
 0.999
rplB
LSU ribosomal protein L2p (L8e); One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
 
 0.998
rplE
LSU ribosomal protein L5p (L11e); 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
LSU ribosomal protein L6p (L9e); 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
rplM
LSU ribosomal protein L13p (L13Ae); 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.
 
 0.998
rplC
LSU ribosomal protein L3p (L3e); 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.
  
 0.997
rplD
LSU ribosomal protein L4p (L1e); Forms part of the polypeptide exit tunnel.
  
 0.997
rpsC
SSU ribosomal protein S3p (S3e); Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation; Belongs to the universal ribosomal protein uS3 family.
  
 
 0.997
Your Current Organism:
Vibrio metschnikovii
NCBI taxonomy Id: 675813
Other names: V. metschnikovii CIP 69.14, Vibrio metschnikovii CIP 69.14, Vibrio metschnikovii str. CIP 69.14, Vibrio metschnikovii strain CIP 69.14
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.