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.
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
mntHManganese transport protein; H(+)-stimulated, divalent metal cation uptake system. Belongs to the NRAMP family. (443 aa)    
Predicted Functional Partners:
AGA_1058
UreA carboxylase.
  
  
 0.732
AGA_984
Putative cation ABC transporter, permease protein; ABC-3.
   
  
 0.474
AGA_1070
LamB/YcsF family protein; Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
  
  
 0.472
def-2
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family.
       0.430
Your Current Organism:
Acetobacter ghanensis
NCBI taxonomy Id: 431306
Other names: A. ghanensis, Acetobacter ghanensis Cleenwerck et al. 2007, Acetobacter sp. 384, Acetobacter sp. 444B, DSM 18895, LMG 23848, LMG:23848, strain 430A, strain R-29337
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