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
rplMLSU ribosomal protein L13P; 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. (147 aa)    
Predicted Functional Partners:
rplC
LSU ribosomal protein L3P; 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.
 
 0.999
rpsI
COGs: COG0103 Ribosomal protein S9; InterPro IPR020574:IPR000754; KEGG: apv:Apar_1249 ribosomal protein S9; PFAM: ribosomal protein S9; SPTR: 30S ribosomal protein S9; IMG reference gene:2503576245; PFAM: Ribosomal protein S9/S16; Belongs to the universal ribosomal protein uS9 family.
 
 
 0.999
rplO
LSU ribosomal protein L15P; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
 
 0.998
rpmD
COGs: COG1841 Ribosomal protein L30/L7E; InterPro IPR005996:IPR000517; KEGG: ele:Elen_2160 ribosomal protein L30; PFAM: ribosomal protein L30; SPTR: 50S ribosomal protein L30; TIGRFAM: ribosomal protein L30; IMG reference gene:2503576123; PFAM: Ribosomal protein L30p/L7e; TIGRFAM: ribosomal protein L30, bacterial/organelle.
  
 0.998
rplR
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.
  
 0.998
rplF
LSU ribosomal protein L6P; 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
rplP
LSU ribosomal protein L16P; 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.
 
 0.998
rplV
LSU ribosomal protein L22P; 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
rplW
LSU ribosomal protein L23P; 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
rplT
LSU ribosomal protein L20P; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
 
 
 0.997
Your Current Organism:
Coriobacterium glomerans
NCBI taxonomy Id: 700015
Other names: C. glomerans PW2, Coriobacterium glomerans DSM 20642, Coriobacterium glomerans PW2, Coriobacterium glomerans str. PW2, Coriobacterium glomerans strain PW2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.