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
PHO12One of three repressible acid phosphatases; glycoprotein that is transported to the cell surface by the secretory pathway; pregulated by phosphate starvation; PHO12 has a paralog, PHO11, that arose from a segmental duplication. (467 aa)    
Predicted Functional Partners:
PHO84
High-affinity inorganic phosphate (Pi) transporter; also low-affinity manganese transporter; regulated by Pho4p and Spt7p; mutation confers resistance to arsenate; exit from the ER during maturation requires Pho86p; cells overexpressing Pho84p accumulate heavy metals but do not develop symptoms of metal toxicity.
   
  
 0.981
PHO11
One of three repressible acid phosphatases; glycoprotein that is transported to the cell surface by the secretory pathway; induced by phosphate starvation and coordinately regulated by PHO4 and PHO2; PHO11 has a paralog, PHO12, that arose from a segmental duplication.
  
0.978
PHO8
Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN.
   
 
 0.965
PHO5
Repressible acid phosphatase; 1 of 3 repressible acid phosphatases that also mediates extracellular nucleotide-derived phosphate hydrolysis; secretory pathway derived cell surface glycoprotein; induced by phosphate starvation and coordinately regulated by PHO4 and PHO2; Belongs to the histidine acid phosphatase family.
  
0.953
PHO3
Constitutively expressed acid phosphatase similar to Pho5p; brought to the cell surface by transport vesicles; hydrolyzes thiamin phosphates in the periplasmic space, increasing cellular thiamin uptake; expression is repressed by thiamin.
  
0.932
LTP1
Protein phosphotyrosine phosphatase of unknown cellular role; activated by adenine.
     
 0.921
THI80
Thiamine pyrophosphokinase; phosphorylates thiamine to produce the coenzyme thiamine pyrophosphate (thiamine diphosphate).
     
 0.919
PHO81
Phosphate system positive regulatory protein PHO81; Cyclin-dependent kinase (CDK) inhibitor; regulates Pho80p-Pho85p and Pcl7p-Pho85p cyclin-CDK complexes in response to phosphate levels; inhibitory activity for Pho80p-Pho85p requires myo-D-inositol heptakisphosphate (IP7) generated by Vip1p; relative distribution to the nucleus increases upon DNA replication stress.
   
  
 0.913
THI6
Thiamine biosynthetic bifunctional enzyme; Thiamine-phosphate diphosphorylase and hydroxyethylthiazole kinase; required for thiamine biosynthesis; GFP-fusion protein localizes to the cytoplasm in a punctate pattern.
     
 0.905
DIA3
Probable acid phosphatase DIA3; Protein of unknown function; involved in invasive and pseudohyphal growth.
  
  
0.902
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.