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
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
AMQ42004.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (164 aa)    
Predicted Functional Partners:
rpsC
30S ribosomal protein S3; 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.
  
   0.959
rpmC
50S ribosomal protein L29; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uL29 family.
  
   0.957
rplC
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.
   
   0.951
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.
  
   0.950
rpsQ
30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
  
   0.945
rpsO
30S ribosomal protein S15; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
   
   0.941
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.
  
   0.926
rplX
50S ribosomal protein L24; One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
  
   0.894
rpsN
30S ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
   
   0.893
rpsG
30S ribosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
   
   0.893
Your Current Organism:
Aeromonas veronii
NCBI taxonomy Id: 654
Other names: A. veronii, ATCC 35624, ATCC 49904 [[Aeromonas ichthiosmia]], Aeromonas culicicola, Aeromonas culicicola Pidiyar et al. 2002, Aeromonas hybridization group 10 (HG10), Aeromonas ichthiosmia, Aeromonas sp. G18, Aeromonas sp. R1, Aeromonas sp. R9, Aeromonas sp. TH074, Aeromonas sp. TH076, CCUG 27821, CECT 4257, CECT 4486 [[Aeromonas ichthiosmia]], CIP 103438, CIP 104613 [[Aeromonas ichthiosmia]], CIP 107763 [[Aeromonas culicicola]], DSM 6393 [[Aeromonas ichthiosmia]], DSM 7386, Enteric Group 77, JCM 7375, JCM 8354 [[Aeromonas ichthiosmia]], LMG 12645 [[Aeromonas ichthiosmia]], LMG:12645 [[Aeromonas ichthiosmia]], MTCC 3249 [[Aeromonas culicicola]], NCIMB 13205 [[Aeromonas ichthiosmia]], NICM 5147 [[Aeromonas culicicola]], strain 115/II [[Aeromonas ichthiosmia]]
Server load: medium (52%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.