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GLYMA08G22820.1 protein (Glycine max) - STRING interaction network
"GLYMA08G22820.1" - Signal recognition particle 54 kDa protein in Glycine max
Nodes:
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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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:
some 3D structure is known or predicted
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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 each other.
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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[Homology]
Score
GLYMA08G22820.1Signal recognition particle 54 kDa protein; Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein); Belongs to the GTP-binding SRP family. SRP54 subfamily (495 aa)    
Predicted Functional Partners:
GLYMA16G26150.1
Uncharacterized protein (137 aa)
     
 
  0.947
GLYMA02G07200.1
Uncharacterized protein (137 aa)
     
 
  0.947
GLYMA12G00660.1
Uncharacterized protein (120 aa)
     
 
  0.940
GLYMA09G36700.1
Uncharacterized protein (120 aa)
     
 
  0.940
GLYMA08G10671.1
Signal recognition particle subunit SRP72; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane (662 aa)
     
 
  0.940
GLYMA05G27690.1
Signal recognition particle subunit SRP72; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane (662 aa)
     
 
  0.940
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)
     
 
  0.926
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)
     
 
  0.926
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)
     
 
  0.925
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)
     
 
  0.925
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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