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Si011422m Si011422m Si007605m Si007605m Si001723m Si001723m
"Si001723m" - Protein-lysine N-methyltransferase Si001723m.g in Setaria italica
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query proteins and first shell of interactors
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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
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Si001723mProtein-lysine N-methyltransferase Si001723m.g ; S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha (400 aa)    
Predicted Functional Partners:
Si011422m
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)
     
   
  0.405
Si007605m
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)
     
   
  0.405
Your Current Organism:
Setaria italica
NCBI taxonomy Id: 4555
Other names: Paniceae, S. italica, Setaria, Setaria P.Beauv., Setaria italica, Setaria italica (L.) P.Beauv., foxtail millet
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