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YKL118W protein (Saccharomyces cerevisiae) - STRING interaction network
"YKL118W" - Dubious open reading frame, unlikely to encode a protein in Saccharomyces cerevisiae
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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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[Homology]
Score
YKL118WDubious open reading frame, unlikely to encode a protein; partially overlaps the verified gene VPH2 (103 aa)    
Predicted Functional Partners:
YLR235C
Dubious open reading frame unlikely to encode a protein, based on available experimental and comparative sequence data; partially overlaps the verified gene TOP3 (132 aa)
           
  0.578
HUR1
Protein of unknown function; reported null mutant phenotype of hydroxyurea sensitivity may be due to effects on overlapping PMR1 gene (110 aa)
           
  0.520
YOR331C
Dubious open reading frame unlikely to encode a protein, based on available experimental and comparative sequence data; open reading frame overlaps the verified gene VMA4/YOR332W (185 aa)
           
  0.483
YJL175W
Dubious open reading frame unlikely to encode a functional protein; deletion confers resistance to cisplatin, hypersensitivity to 5-fluorouracil, and growth defect at high pH with high calcium; overlaps gene for SWI3 transcription factor (170 aa)
           
  0.455
VPS65
Dubious open reading frame, unlikely to encode a protein; not conserved in closely related Saccharomyces species; 75% of ORF overlaps the verified gene SFH1; deletion causes a vacuolar protein sorting defect and blocks anaerobic growth; Deletion causes a vacuolar protein sorting defect (104 aa)
           
  0.414
VMA6
Subunit d of the five-subunit V0 integral membrane domain of vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found in the endomembrane system; stabilizes VO subunits; required for V1 domain assembly on the vacuolar membrane; Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. The active enzyme consists of a catalytic V1 domain attached to an integral membrane V0 proton pore complex. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be [...] (345 aa)
           
  0.412
VMA8
Subunit D of the eight-subunit V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found throughout the endomembrane system; plays a role in the coupling of proton transport and ATP hydrolysis; Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (256 aa)
           
  0.412
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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