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
rpmIHAMAP: Ribosomal protein L35, non-mitochondrial; InterPro IPR001706:IPR021137; KEGG: fba:FIC_00851 LSU ribosomal protein L35p; PFAM: Ribosomal protein L35; SPTR: 50S ribosomal protein L35; TIGRFAM: Ribosomal protein L35, non-mitochondrial; PFAM: Ribosomal protein L35; TIGRFAM: ribosomal protein L35; Belongs to the bacterial ribosomal protein bL35 family. (65 aa)    
Predicted Functional Partners:
rplS
50S ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
  
 
 0.999
rpmE2
COGs: COG0254 Ribosomal protein L31; HAMAP: Ribosomal protein L31; InterPro IPR002150; KEGG: fjo:Fjoh_0109 50S ribosomal protein L31 type B; PFAM: Ribosomal protein L31; SPTR: 50S ribosomal protein L31; TIGRFAM: Ribosomal protein L31; PFAM: Ribosomal protein L31; TIGRFAM: ribosomal protein L31.
  
 
 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
rplA
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.
   
 
 0.999
rplK
Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
   
 
 0.999
rpsU
HAMAP: Ribosomal protein S21; InterPro IPR001911; KEGG: fba:FIC_00265 SSU ribosomal protein S21p; PFAM: Ribosomal protein S21; SPTR: 30S ribosomal protein S21; TIGRFAM: Ribosomal protein S21; PFAM: Ribosomal protein S21; TIGRFAM: ribosomal protein S21; Belongs to the bacterial ribosomal protein bS21 family.
  
 
 0.999
rpsT
30S ribosomal protein S20; Binds directly to 16S ribosomal RNA.
   
 
 0.999
rpsP
COGs: COG0228 Ribosomal protein S16; HAMAP: Ribosomal protein S16; InterPro IPR000307; KEGG: fba:FIC_01831 SSU ribosomal protein S16p; PFAM: Ribosomal protein S16; SPTR: 30S ribosomal protein S16; TIGRFAM: Ribosomal protein S16; PFAM: Ribosomal protein S16; TIGRFAM: ribosomal protein S16; Belongs to the bacterial ribosomal protein bS16 family.
  
 
 0.999
rplY
50S ribosomal protein L25; This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily.
  
 
 0.999
rpmA
COGs: COG0211 Ribosomal protein L27; HAMAP: Ribosomal protein L27; InterPro IPR001684; KEGG: fba:FIC_02444 50S ribosomal protein L27; PFAM: Ribosomal protein L27; SPTR: 50S ribosomal protein L27; TIGRFAM: Ribosomal protein L27; PFAM: Ribosomal L27 protein; TIGRFAM: ribosomal protein L27; Belongs to the bacterial ribosomal protein bL27 family.
   
 
 0.999
Your Current Organism:
Weeksella virosa
NCBI taxonomy Id: 865938
Other names: W. virosa DSM 16922, Weeksella virosa ATCC 43766, Weeksella virosa CIP 103040, Weeksella virosa DSM 16922, Weeksella virosa str. DSM 16922, Weeksella virosa strain DSM 16922
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.