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
smd-1S-adenosylmethionine decarboxylase alpha chain; Essential for biosynthesis of the polyamines spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. (368 aa)    
Predicted Functional Partners:
spds-1
PABS domain-containing protein; Belongs to the spermidine/spermine synthase family.
  
 
 0.999
odc-1
Ornithine decarboxylase; Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
 
 
 
 0.982
sams-1
Probable S-adenosylmethionine synthase 1; Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate; Belongs to the AdoMet synthase family.
   
 
 0.947
sams-4
Probable S-adenosylmethionine synthase 4; Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate; Belongs to the AdoMet synthase family.
   
 
 0.941
sams-3
Probable S-adenosylmethionine synthase 3; Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate; Belongs to the AdoMet synthase family.
   
 
 0.940
sams-5
Probable S-adenosylmethionine synthase 5; Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
   
 
 0.940
T21F4.1
Uncharacterized protein; Belongs to the arginase family.
   
  
 0.900
F38B6.4
Trifunctional purine biosynthetic protein adenosine-3; In the C-terminal section; belongs to the GART family. In the central section; belongs to the AIR synthase family.
   
  
 0.830
vpat-1
MFS domain-containing protein.
   
  
 0.821
dhod-1
Dihydroorotate dehydrogenase (quinone), mitochondrial; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
   
  
 0.759
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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