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
rlpA50S 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. (230 aa)    
Predicted Functional Partners:
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
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
rplK
50S ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
 
 0.999
rpsB
30S ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.998
rplF
50S ribosomal 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
rplN
50S ribosomal protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
  
 0.998
rplV
50S ribosomal 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
rpsS
30S ribosomal protein S19; Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
  
 
 0.998
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.
  
 0.998
rplC_1
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; Belongs to the universal ribosomal protein uL3 family.
  
 0.998
Your Current Organism:
Bifidobacterium bifidum
NCBI taxonomy Id: 1681
Other names: AS 1.2212, ATCC 29521, Actinobacterium bifidum, Actinomyces bifidus, Actinomyces parabifidus, B. bifidum, BCRC 14615, Bacillus bifidus, Bacillus bifidus communis, Bacterium bifidum, Bacteroides bifidus, Bifidibacterium bifidum, CCRC 14615, CCRC:14615, CCUG 18364, CCUG 45217, CIP 56.7, Cohnistreptothrix bifidus, DSM 20456, IFO 14252, KCTC 3202, LMG 11041, LMG 8810, LMG:11041, LMG:8810, Lactobacillus bifidus type II, Lactobacillus parabifidus, NBRC 100015, NBRC 14252, NCFB 2715, NCIMB 702715, NCTC 13001, Nocardia bifida, Tissieria bifida, strain Ti
Server load: low (38%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.