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
AMAG_20155Cyclic nucleotide-binding domain-containing protein. (1007 aa)    
Predicted Functional Partners:
AMAG_00196
Aldo_ket_red domain-containing protein.
    
 0.525
AMAG_17633
Aldo_ket_red domain-containing protein.
    
 0.525
AMAG_17634
Aldo_ket_red domain-containing protein.
    
 0.525
AMAG_01403
Voltage-dependent potassium channel beta subunit.
    
 0.525
AMAG_05605
Voltage-dependent potassium channel beta subunit.
    
 0.525
AMAG_10755
Aldo_ket_red domain-containing protein.
    
 0.525
AMAG_11032
Peptidase A1 domain-containing protein; Belongs to the peptidase A1 family.
   
 
  0.522
AMAG_11644
Peptidase A1 domain-containing protein; Belongs to the peptidase A1 family.
   
 
  0.522
AMAG_12403
Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
     
 0.460
AMAG_14055
Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
     
 0.460
Your Current Organism:
Allomyces macrogynus
NCBI taxonomy Id: 578462
Other names: A. macrogynus ATCC 38327, Allomyces macrogynus ATCC 38327
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