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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
IRC15Increased recombination centers protein 15; Microtubule associated protein; regulates microtubule dynamics; required for accurate meiotic chromosome segregation; null mutant displays large budded cells due to delayed mitotic progression, increased levels of spontaneous Rad52 foci; IRC15 has a paralog, LPD1, that arose from the whole genome duplication; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (499 aa)    
Predicted Functional Partners:
LAT1
Dihydrolipoamide acetyltransferase component (E2) of the PDC; the pyruvate dehydrogenase complex (PDC) catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA.
 
 0.995
KGD2
2-oxoglutarate dehydrogenase E2 component (dihydrolipoamide succinyltransferase); Dihydrolipoyl transsuccinylase; component of the mitochondrial alpha-ketoglutarate dehydrogenase complex, which catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA in the TCA cycle; phosphorylated.
 0.988
PDB1
E1 beta subunit of the pyruvate dehydrogenase (PDH) complex; PDH is an evolutionarily conserved multi-protein complex found in mitochondria.
 
 0.970
LSC2
Beta subunit of succinyl-CoA ligase; succinyl-CoA ligase is a mitochondrial enzyme of the TCA cycle that catalyzes the nucleotide-dependent conversion of succinyl-CoA to succinate.
  
 0.956
KGD1
2-oxoglutarate dehydrogenase, mitochondrial; Subunit of the mitochondrial alpha-ketoglutarate dehydrogenase complex; catalyzes a key step in the tricarboxylic acid (TCA) cycle, the oxidative decarboxylation of alpha-ketoglutarate to form succinyl-CoA.
  
 0.955
PDA1
E1 alpha subunit of the pyruvate dehydrogenase (PDH) complex; catalyzes the direct oxidative decarboxylation of pyruvate to acetyl-CoA; phosphorylated; regulated by glucose; PDH complex is concentrated in spots within the mitochondrial matrix, often near the ERMES complex and near peroxisomes.
 
 
 0.951
PDX1
E3-binding protein of the mitochondrial pyruvate dehydrogenase complex; plays a structural role in the complex by binding and positioning dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide acetyltransferase (E2) core.
  
 0.927
LSC1
Alpha subunit of succinyl-CoA ligase; succinyl-CoA ligase is a mitochondrial enzyme of the TCA cycle that catalyzes the nucleotide-dependent conversion of succinyl-CoA to succinate; phosphorylated.
  
 0.899
IDH1
Subunit of mitochondrial NAD(+)-dependent isocitrate dehydrogenase; complex catalyzes the oxidation of isocitrate to alpha-ketoglutarate in the TCA cycle; Belongs to the isocitrate and isopropylmalate dehydrogenases family.
  
 0.868
IDH2
Subunit of mitochondrial NAD(+)-dependent isocitrate dehydrogenase; complex catalyzes the oxidation of isocitrate to alpha-ketoglutarate in the TCA cycle; phosphorylated; Belongs to the isocitrate and isopropylmalate dehydrogenases family.
  
 0.855
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
Server load: low (14%) [HD]