STRINGSTRING
GRMZM2G429057_P01 protein (Zea mays) - STRING interaction network
"GRMZM2G429057_P01" - Uncharacterized protein in Zea mays
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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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
GRMZM2G429057_P01Uncharacterized protein (717 aa)    
Predicted Functional Partners:
100191967
Amino acid permease; Uncharacterized protein (487 aa)
           
  0.713
pco090513
Uncharacterized protein; Signal peptidase complex subunit 2; Uncharacterized protein (192 aa)
           
  0.709
pco124429
DNA replication complex GINS protein PSF1; Uncharacterized protein (204 aa)
           
  0.538
IDP388
Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 Methylthioribulose-1-phosphate dehydratase Enolase-phosphatase E1; In the C-terminal section; belongs to the HAD-like hydrolase superfamily. MasA/MtnC family (517 aa)
   
   
  0.526
GRMZM2G080907_P01
Putative FAD-binding Berberine family protein ; Belongs to the oxygen-dependent FAD-linked oxidoreductase family (546 aa)
         
  0.506
100273608
D-2-hydroxyglutarate dehydrogenase mitochondrial (562 aa)
         
  0.503
103635100
Sec23/Sec24 protein transport family protein (866 aa)
           
  0.503
GRMZM2G429540_P01
FAD-binding Berberine family protein; Belongs to the oxygen-dependent FAD-linked oxidoreductase family (561 aa)
         
  0.502
csy1
Preprotein translocase subunit SECY, chloroplastic; The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity) (553 aa)
     
   
  0.500
107521951
annotation not available (462 aa)
           
  0.499
Your Current Organism:
Zea mays
NCBI taxonomy Id: 4577
Other names: Z. mays, Zea mays, Zea mays L., Zea mays var. japonica, maize
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