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
AAEL005552Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial; GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (421 aa)    
Predicted Functional Partners:
AAEL006833
Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits.
 0.999
AAEL008871
Mitochondrial succinate dehydrogenase cytochrome b subunit.
  
 
 0.986
AAEL010330
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial; Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
 
 0.981
AAEL010608
Succinate dehydrogenase (quinone); Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 
 0.974
AAEL002764
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase.
 
 0.973
AAEL004294
AAEL004294-PA.
 
 0.946
AAEL003090
AAEL003090-PA.
   
 
 0.925
AAEL011746
Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial; ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
  
 
 
0.925
AAEL002383
Succinate dehydrogenase [ubiquinone] cytochrome b small subunit; Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q); Belongs to the CybS family.
   
 
 0.923
AAEL014505
Succinate dehydrogenase [ubiquinone] cytochrome b small subunit; Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q); Belongs to the CybS family.
   
 
 0.923
Your Current Organism:
Aedes aegypti
NCBI taxonomy Id: 7159
Other names: A. aegypti, Stegomyia aegypti, yellow fever mosquito
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.