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
SFL08986.1Serine protease, S1-C subfamily, contains C-terminal PDZ domain. (355 aa)    
Predicted Functional Partners:
glpK
Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate.
   
 0.814
pan
Proteasome regulatory subunit; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S p [...]
    
 0.788
pan-2
Proteasome regulatory subunit; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S p [...]
    
 0.788
SFL28843.1
Tetratricopeptide repeat-containing protein.
 
 
 0.657
lysA
Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine.
  
  
  0.648
dnaK
Molecular chaperone DnaK; Acts as a chaperone.
 
 
 0.613
SFK80342.1
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif.
   
  0.572
SFL08686.1
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif.
   
  0.572
SFL08966.1
Hypothetical protein.
       0.568
SFL60564.1
Serine protease, S1-C subfamily, contains C-terminal PDZ domain.
  
  
 
0.567
Your Current Organism:
Halogranum rubrum
NCBI taxonomy Id: 553466
Other names: CGMCC 1.7738, H. rubrum, Halobacteriaceae archaeon RO2-11, Halogranum rubrum Cui et al. 2010, JCM 15772, strain RO2-11
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