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YGL217C protein (Saccharomyces cerevisiae) - STRING interaction network
"YGL217C" - Dubious open reading frame unlikely to encode a protein, based on available experimental and comparative sequence data in Saccharomyces cerevisiae
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
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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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Gene Fusion
Cooccurence
Coexpression
Experiments
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[Homology]
Score
YGL217CDubious open reading frame unlikely to encode a protein, based on available experimental and comparative sequence data; partially overlaps the verified ORF KIP3/YGL216W (113 aa)    
Predicted Functional Partners:
BUD28
Dubious open reading frame, unlikely to encode a protein; not conserved in closely related Saccharomyces species; 98% of ORF overlaps the verified gene RPL22A; diploid mutant displays a weak budding pattern phenotype in a systematic assay; Diploid deletion displays a weak budding pattern phenotype in a systematic assay (125 aa)
           
  0.513
YNL043C
Dubious open reading frame unlikely to encode a protein, based on available experimental and comparative sequence data; partially overlaps the verified gene YIP3/YNL044W (106 aa)
           
  0.489
YLR125W
Putative protein of unknown function; mutant has decreased Ty3 transposition; YLR125W is not an essential gene (136 aa)
           
  0.485
CPR8
Peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; similarity to Cpr4p suggests a potential role in the secretory pathway; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (308 aa)
           
  0.418
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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