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GLYMA05G27690.1 protein (Glycine max) - STRING interaction network
"GLYMA05G27690.1" - Signal recognition particle subunit SRP72 in Glycine max
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Gene Fusion
Cooccurence
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Textmining
[Homology]
Score
GLYMA05G27690.1Signal recognition particle subunit SRP72; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane (662 aa)    
Predicted Functional Partners:
GLYMA08G01070.1
Signal recognition particle subunit SRP68; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane (603 aa)
     
 
  0.998
GLYMA05G38560.1
Signal recognition particle subunit SRP68; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane (603 aa)
     
 
  0.998
GLYMA16G26150.1
Uncharacterized protein (137 aa)
     
 
  0.988
GLYMA02G07200.1
Uncharacterized protein (137 aa)
     
 
  0.988
GLYMA12G00660.1
Uncharacterized protein (120 aa)
     
 
  0.979
GLYMA09G36700.1
Uncharacterized protein (120 aa)
     
 
  0.979
GLYMA18G31665.2
Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (103 aa)
     
 
  0.945
GLYMA10G03810.1
Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (103 aa)
     
 
  0.945
GLYMA08G46000.4
Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (103 aa)
     
 
  0.945
GLYMA02G15940.2
Uncharacterized protein (71 aa)
     
 
  0.945
Your Current Organism:
Glycine max
NCBI taxonomy Id: 3847
Other names: G. max, Glycine max, Glycine max (L.) Merr., soybean, soybeans
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