STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
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:
a 3D structure is known or predicted
Edges:
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 to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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FPR2Membrane-bound peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; expression pattern suggests possible involvement in ER protein trafficking; relocalizes from nucleus to vacuole upon DNA replication stress; mutation is functionally complemented by human FKBP2. (135 aa)    
Predicted Functional Partners:
CPR5
Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication.
 
 
 0.972
CPR2
Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema.
 
 
 0.968
CPR6
Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.
 
 
 0.947
CPR1
Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A; N-terminally propionylated in vivo; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.
 
 
 0.942
CPR3
Mitochondrial peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; involved in protein refolding after import into mitochondria.
 
 
 0.941
YPL162C
Vacuolar membrane protein YPL162C; Putative protein of unknown function; green fluorescent protein (GFP)-fusion protein localizes to the membrane of vacuole with cell cycle-correlated morphology.
 
 
 
 0.931
CMD1
Calmodulin; Ca2+ binding protein that regulates Ca2+ independent processes (mitosis, bud growth, actin organization, endocytosis, etc.) and Ca2+ dependent processes (stress-activated pathways), targets include Nuf1p, Myo2p and calcineurin; binds to the Hog1p MAPK in response to hyperosmotic stress; potentiates membrane tubulation and constriction mediated by the Rvs161p-Rvs167p complex; human CALM1 or CALM2 functionally complement repression induced inviability.
   
 
 0.896
EUG1
Protein disulfide-isomerase EUG1; Protein disulfide isomerase of the endoplasmic reticulum lumen; EUG1 has a paralog, PDI1, that arose from the whole genome duplication; function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER.
   
 
 0.879
MLC1
Essential light chain for Myo1p; light chain for Myo2p; stabilizes Myo2p by binding to the neck region; interacts with Myo1p, Iqg1p, and Myo2p to coordinate formation and contraction of the actomyosin ring with targeted membrane deposition.
   
 
 0.877
LHS1
Heat shock protein 70 homolog LHS1; Molecular chaperone of the endoplasmic reticulum lumen; involved in polypeptide translocation and folding; nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; regulated by the unfolded protein response pathway.
   
 
 0.860
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.