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YGL193C protein (Saccharomyces cerevisiae) - STRING interaction network
"YGL193C" - Haploid-specific gene repressed by a1-alpha2, turned off in sir3 null strains, absence enhances the sensitivity of rad52-327 cells to campothecin almost 100-fold in Saccharomyces cerevisiae
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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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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
YGL193CHaploid-specific gene repressed by a1-alpha2, turned off in sir3 null strains, absence enhances the sensitivity of rad52-327 cells to campothecin almost 100-fold (103 aa)    
Predicted Functional Partners:
RFS1
Protein of unknown function; member of a flavodoxin-like fold protein family that includes Pst2p and Ycp4p; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm in a punctate pattern (210 aa)
           
  0.642
PST2
Protein with similarity to members of a family of flavodoxin-like proteins; induced by oxidative stress in a Yap1p dependent manner; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies (198 aa)
           
  0.485
FPR3
Nucleolar peptidyl-prolyl cis-trans isomerase (PPIase); FK506 binding protein; phosphorylated by casein kinase II (Cka1p-Cka2p-Ckb1p-Ckb2p) and dephosphorylated by Ptp1p; PPIases accelerate the folding of proteins. FK506- and rapamycin-binding protein. Specifically binds nuclear localization sequences. May be involved in the assembly or folding of ribosomal proteins (411 aa)
           
  0.443
LIF1
Component of the DNA ligase IV complex that mediates nonhomologous end joining in DNA double-strand break repair; physically interacts with Dnl4p and Nej1p; homologous to mammalian XRCC4 protein; Stabilizes DNL4. Involved in non-homologous repair of DNA double-strand breaks (421 aa)
           
  0.430
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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