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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
YPR099CPutative uncharacterized protein YPR099C; Dubious open reading frame; unlikely to encode a functional protein, based on available experimental and comparative sequence data; partially overlaps the verified gene MRPL51/YPR100W (118 aa)    
Predicted Functional Partners:
MRPL51
Mitochondrial 54s ribosomal protein mrpl51; Mitochondrial ribosomal protein of the large subunit
   
  
 0.924
YOL019W
Uncharacterized membrane protein YOL019W; Protein of unknown function; green fluorescent protein (GFP)-fusion protein localizes to the cell periphery and vacuole; YOL019W has a paralog, DCV1, that arose from the whole genome duplication
      
 0.816
ECM14
Putative metallocarboxypeptidase ECM14; Putative metalloprotease with similarity to zinc carboxypeptidases; required for normal cell wall assembly; Belongs to the peptidase M14 family
      
 0.766
MHR1
Mitochondrial ribosomal protein of the large subunit; also involved in homologous recombination in mitochondria; required for recombination-dependent mtDNA partitioning; involved in stimulation of mitochondrial DNA replication in response to oxidative stress
      
 0.697
MRPL27
Mitochondrial 54s ribosomal protein yml27; Mitochondrial ribosomal protein of the large subunit; homolog of human Bcl-2 interacting protein BMRP
      
 0.574
VMA11
Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen
      
 0.574
VTC4
Vacuolar transporter chaperone 4; Vacuolar membrane polyphosphate polymerase; subunit of the vacuolar transporter chaperone (VTC) complex involved in synthesis and transfer of polyP to the vacuole; regulates membrane trafficking; role in non-autophagic vacuolar fusion; protein abundance increases in response to DNA replication stress
      
 0.573
PYK2
Pyruvate kinase; appears to be modulated by phosphorylation; transcription repressed by glucose, and Pyk2p may be active under low glycolytic flux; PYK2 has a paralog, CDC19, that arose from the whole genome duplication
      
 0.563
VTC1
Regulatory subunit of the vacuolar transporter chaperone (VTC) complex; VTC complex is involved in membrane trafficking, vacuolar polyphosphate accumulation, microautophagy and non-autophagic vacuolar fusion; also has mRNA binding activity; protein abundance increases in response to DNA replication stress
      
 0.556
VMA3
V-type proton ATPase subunit c; Proteolipid subunit c of the V0 domain of vacuolar H(+)-ATPase; dicyclohexylcarbodiimide binding subunit; required for vacuolar acidification and important for copper and iron metal ion homeostasis; Belongs to the V-ATPase proteolipid subunit family
      
 0.526
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.