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
cpdA3',5'-cyclic-AMP phosphodiesterase; Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. (279 aa)    
Predicted Functional Partners:
cyaA
Adenylate cyclase; Catalyzes transfer of adenylyl group of ATP from pyrophosphate to the 3'-hydroxyl group to form cyclic AMP; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the adenylyl cyclase class-1 family.
  
  
 0.964
yqiA
Displays esterase activity toward palmitoyl-CoA and pNP-butyrate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.956
mazG
Nucleoside triphosphate pyrophosphohydrolase; Functions in degradation of stringent response intracellular messenger ppGpp; in Escherichia coli this gene is co-transcribed with the toxin/antitoxin genes mazEF; activity of MazG is inhibited by MazEF in vitro; ppGpp inhibits mazEF expression; MazG thus works in limiting the toxic activity of the MazF toxin induced during starvation; MazG also interacts with the GTPase protein Era; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
  0.915
AND13294.1
Adenylate cyclase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.913
ushA
Bifunctional UDP-sugar hydrolase/5'-nucleotidase; Catalyzes the degradation of periplasmic UDP-glucose to uridine, glucose-1-phosphate and inorganic phosphate; specific for uridine nucleotides; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 5'-nucleotidase family.
   
 
 0.902
yhcR
Bifunctional metallophosphatase/5'-nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 5'-nucleotidase family.
   
 
 0.902
ygdH
LOG family protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.901
adk
Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.
     
 0.901
pcaB_3
Adenylosuccinate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.900
surE
5'/3'-nucleotidase SurE; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.
     
  0.900
Your Current Organism:
Proteus mirabilis
NCBI taxonomy Id: 584
Other names: ATCC 29906, CCUG 26767, CIP 103181, DSM 4479, LMG 3257, LMG:3257, NCTC 11938, P. mirabilis
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