close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
srp19Signal recognition particle, subunit SRP19 (srp19); Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP. (95 aa)    
Predicted Functional Partners:
srp54
Signal recognition particle subunit FFH/SRP54 (srp54); Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily.
   
 0.999
ftsY
Signal recognition particle-docking protein FtsY; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
   
 
 0.981
rps8e
TIGRFAM: ribosomal protein S8e; PFAM: ribosomal protein S8E; KEGG: neq:NEQ469 SSU ribosomal protein S8E.
  
    0.897
rpl19e
LSU ribosomal protein L19E; Binds to the 23S rRNA; Belongs to the eukaryotic ribosomal protein eL19 family.
  
 
 0.838
rpl30e
PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; KEGG: pho:PHS043 50S ribosomal protein L30e; Belongs to the eukaryotic ribosomal protein eL30 family.
  
   0.834
rpl18
LSU ribosomal protein L18P; 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.
  
   0.834
rpl15e
PFAM: Ribosomal protein L15e; KEGG: ape:APE1452 50S ribosomal protein L15e; Belongs to the eukaryotic ribosomal protein eL15 family.
  
 
   0.820
rpl24
LSU ribosomal protein L24P; 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.
  
   0.820
rpl37ae
LSU ribosomal protein L37AE; Binds to the 23S rRNA; Belongs to the eukaryotic ribosomal protein eL43 family. Putative zinc-binding subfamily.
 
 
   0.815
rpl10e
TIGRFAM: ribosomal protein L10.e; PFAM: Ribosomal protein L10E; KEGG: ape:APE0449 50S ribosomal protein L10e; Belongs to the universal ribosomal protein uL16 family.
  
 
 
 0.809
Your Current Organism:
Staphylothermus marinus
NCBI taxonomy Id: 399550
Other names: S. marinus F1, Staphylothermus marinus ATCC 43588, Staphylothermus marinus DSM 3639, Staphylothermus marinus F1, Staphylothermus marinus JCM 9404, Staphylothermus marinus str. F1, Staphylothermus marinus strain F1
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.