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IPP1 protein (Yarrowia lipolytica) - STRING interaction network
"IPP1" - YALI0F13541p in Yarrowia lipolytica
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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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
IPP1YALI0F13541p (287 aa)    
Predicted Functional Partners:
XP_505205.1
YALI0F09405p (196 aa)
     
  0.946
XP_504936.1
YALI0F03179p; Produces ATP from ADP in the presence of a proton gradient across the membrane (536 aa)
     
 
  0.942
XP_504924.2
YALI0F02893p (293 aa)
     
 
  0.926
XP_500475.2
YALI0B03982p; Produces ATP from ADP in the presence of a proton gradient across the membrane (509 aa)
     
  0.921
XP_502751.2
YALI0D12584p (214 aa)
     
  0.918
XP_505831.1
YALI0F24475p; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (164 aa)
     
  0.917
XP_504637.2
YALI0E31471p; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (161 aa)
     
  0.917
ATP9
ATP synthetase subunit 9; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subu [...] (76 aa)
     
  0.917
XP_504463.1
YALI0E27346p (512 aa)
     
 
  0.913
XP_503135.1
YALI0D22022p (137 aa)
     
 
  0.913
Your Current Organism:
Yarrowia lipolytica
NCBI taxonomy Id: 4952
Other names: Candida lipolytica, Dipodascaceae, Mycotorula lipolytica, Y. lipolytica, Yarrowia, Yarrowia lipolytica
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