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
NCP1NADP-cytochrome P450 reductase; involved in ergosterol biosynthesis; associated and coordinately regulated with Erg11p; In the N-terminal section; belongs to the flavodoxin family. (691 aa)    
Predicted Functional Partners:
MET5
Sulfite reductase beta subunit; involved in amino acid biosynthesis, transcription repressed by methionine; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
 
 0.936
CYB5
Cytochrome b5; involved in the sterol and lipid biosynthesis pathways; acts as an electron donor to support sterol C5-6 desaturation.
   
 
 0.926
ERG11
Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation.
   
 
 0.924
PMC1
Vacuolar Ca2+ ATPase involved in depleting cytosol of Ca2+ ions; prevents growth inhibition by activation of calcineurin in the presence of elevated concentrations of calcium; similar to mammalian PMCA1a.
    
 0.910
YAH1
Adrenodoxin homolog, mitochondrial; Ferredoxin of the mitochondrial matrix; required for formation of cellular iron-sulfur proteins; involved in heme A biosynthesis; human homolog FDX1L can complement yeast by allowing growth during down-regulation of yeast YAH1; Belongs to the adrenodoxin/putidaredoxin family.
   
 
 0.824
ERG24
C-14 sterol reductase; acts in ergosterol biosynthesis; mutants accumulate the abnormal sterol ignosterol (ergosta-8,14 dienol), and are viable under anaerobic growth conditions but inviable on rich medium under aerobic conditions; Belongs to the ERG4/ERG24 family.
   
  
 0.820
MET14
Adenylylsulfate kinase; required for sulfate assimilation and involved in methionine metabolism; human homolog PAPSS2 complements yeast null mutant.
  
 
 0.807
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.
    
 0.800
HMX1
Heme-binding protein HMX1; ER localized heme oxygenase; involved in heme degradation during iron starvation and in the oxidative stress response; expression is regulated by AFT1 and oxidative stress; relocates to the perinuclear region in the presence of oxidants.
    
 
 0.786
HSC82
ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.
    
 0.786
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: medium (46%) [HD]
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