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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[Homology]
Score
YLF2Obg-like ATPase homolog; Protein of unknown function; has weak similarity to E. coli GTP-binding protein gtp1; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies. (405 aa)    
Predicted Functional Partners:
PUF3
mRNA-binding protein PUF3; Protein of the mitochondrial outer surface; links the Arp2/3 complex with the mitochore during anterograde mitochondrial movement; also binds to and promotes degradation of mRNAs for select nuclear-encoded mitochondrial proteins.
    
   0.976
TMA20
Translation machinery-associated protein 20; Protein of unknown function that associates with ribosomes; has a putative RNA binding domain; interacts with Tma22p; null mutant exhibits translation defects; has homology to human oncogene MCT-1; protein abundance increases in response to DNA replication stress; Belongs to the TMA20 family.
 
 
    0.901
TKL1
Transketolase; catalyzes conversion of xylulose-5-phosphate and ribose-5-phosphate to sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate in the pentose phosphate pathway; needed for synthesis of aromatic amino acids; TKL1 has a paralog, TKL2, that arose from the whole genome duplication.
  
   0.834
CBR1
NADH-cytochrome b5 reductase 1; Cytochrome b reductase; not essential for viability; also detected in mitochondria; mutation in conserved NADH binding domain of the human ortholog results in type I methemoglobinemia.
    
   0.771
SAM2
S-adenosylmethionine synthase 2; S-adenosylmethionine synthetase; catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon.
  
 
 0.730
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.
  
   0.694
TRP5
Tryptophan synthase; catalyzes the last step of tryptophan biosynthesis; regulated by the general control system of amino acid biosynthesis; In the N-terminal section; belongs to the TrpA family.
  
  
 0.655
EFT2
Elongation factor 2 (EF-2), also encoded by EFT1; catalyzes ribosomal translocation during protein synthesis; contains diphthamide, the unique posttranslationally modified histidine residue specifically ADP-ribosylated by diphtheria toxin; EFT2 has a paralog, EFT1, that arose from the whole genome duplication.
  
 
 0.594
HSP82
ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.
    
   0.586
TIF2
Translation initiation factor eIF4A; DEA(D/H)-box RNA helicase that couples ATPase activity to RNA binding and unwinding; forms a dumbbell structure of two compact domains connected by a linker; interacts with eIF4G; protein abundance increases in response to DNA replication stress; TIF2 has a paralog, TIF1, that arose from the whole genome duplication.
   
 
 0.577
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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