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
MNEG_10289Uncharacterized protein. (81 aa)    
Predicted Functional Partners:
MNEG_13037
Uncharacterized protein.
    
 0.593
MNEG_3462
Uncharacterized protein.
    
 0.593
MNEG_1775
Serine/threonine-protein kinase plk-3.
   
 
 0.553
MNEG_0971
Protein kinase domain-containing protein.
    
 
 0.463
MNEG_1369
Protein phosphatase.
   
 
 0.457
MNEG_0999
TYR_PHOSPHATASE_2 domain-containing protein.
   
 
 0.457
MNEG_12607
TYR_PHOSPHATASE_2 domain-containing protein.
   
 
 0.457
MNEG_5100
Protein phosphatase.
   
 
 0.457
MNEG_4323
T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
   
  0.447
MNEG_1975
T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
   
  0.447
Your Current Organism:
Monoraphidium neglectum
NCBI taxonomy Id: 145388
Other names: M. neglectum, Monoraphidium neglectum Heynig & Krienitz, SAG 48.87
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