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
ghrA2-ketoacid reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (301 aa)    
Predicted Functional Partners:
serC
3-phosphoserine/phosphohydroxythreonine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
  
 
 0.859
AMG30802.1
IclR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.800
metL
Bifunctional aspartokinase II/homoserine dehydrogenase II; Multifunctional homodimeric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.714
thrA
Bifunctional aspartokinase I/homoserine dehydrogenase I; Multifunctional homotetrameric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.714
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.
    
   0.634
rplP
50S ribosomal protein L16; 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.
   
   0.622
AMG30804.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.607
udk
Uridine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  0.607
rplM
50S ribosomal protein L13; 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.
   
   0.605
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.
    
 
 0.605
Your Current Organism:
Grimontia hollisae
NCBI taxonomy Id: 673
Other names: ATCC 33564, CAIM 625, CCUG 13625, CDC 0075-80, CIP 101886, DSM 15132, G. hollisae, IMET 12291, LMG 17719, LMG:17719, NCTC 11640, Special Bacteriology group EF-13, Vibrio hollisae
Server load: medium (46%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.