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
mmab-1Corrinoid adenosyltransferase; Belongs to the Cob(I)alamin adenosyltransferase family. (214 aa)    
Predicted Functional Partners:
mmaa-1
Methylmalonic aciduria type A homolog, mitochondrial; May have GTPase activity. May also bind and hydrolyze ATP. May function as chaperone (By similarity). Likely to have a role in propionyl-CoA metabolism and adenosylcobalamin synthesis.
   
  
 0.986
cblc-1
MMACHC-like protein; Catalyzes the reductive dealkylation of cyanocobalamin to cob(II)alamin, using FAD or FMN as cofactor and NADPH as cosubstrate. Can also catalyze the glutathione-dependent reductive demethylation of methylcobalamin, and, with much lower efficiency, the glutathione- dependent reductive demethylation of adenosylcobalamin. Under anaerobic conditions cob(I)alamin is the first product; it is highly reactive and is converted to aquocob(II)alamin in the presence of oxygen. Binds cyanocobalamin, adenosylcobalamin, methylcobalamin and other, related vitamin B12 derivatives; [...]
  
  
 0.977
mmcm-1
Probable methylmalonyl-CoA mutase, mitochondrial; Involved, in man, in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species (By similarity).
   
  
 0.950
mce-1
Mitochondrial methylmalonyl-CoA epimerase.
  
  
 0.886
sup-18
Iodotyrosine dehalogenase 1 homolog; May contribute to coordination of muscle contraction as regulatory subunit of the nonessential sup-9 potassium channel complex. May act downstream of sup-10.
    
 0.857
mtrr-1
Methionine synthase reductase; Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state.
      
 0.856
pccb-1
Propionyl Coenzyme A Carboxylase Beta subunit.
      
 0.834
pcca-1
Propionyl-CoA carboxylase alpha chain, mitochondrial; This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl- CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By similarity). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl car [...]
   
  
 0.727
Y76A2B.5
Uncharacterized protein.
   
  
 0.671
hphd-1
Hydroxyacid-oxoacid transhydrogenase, mitochondrial; Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2- KG as hydrogen acceptor, resulting in the formation of D-2-HG. Belongs to the iron-containing alcohol dehydrogenase family. Hydroxyacid-oxoacid transhydrogenase subfamily.
  
 
 0.635
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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