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.
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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
XDJ1DnaJ protein homolog XDJ1; Chaperone with a role in facilitating mitochondrial protein import; ascomycete-specific member of the DnaJ-like family, closely related to Ydj1p; predicted to be C-terminally prenylated; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies. (459 aa)    
Predicted Functional Partners:
VMA10
Subunit G of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; involved in vacuolar acidification; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits.
   
 
 0.959
VMA13
Subunit H of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; serves as an activator or a structural stabilizer of the V-ATPase; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits.
   
   0.956
VMA1
Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family.
    
   0.955
VMA7
Subunit F of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; required for the V1 domain to assemble onto the vacuolar membrane; the V1 peripheral membrane domain of vacuolar H+-ATPase (V-ATPase) has eight subunits.
    
   0.955
TOM40
Mitochondrial import receptor subunit TOM40; Component of the TOM (translocase of outer membrane) complex; responsible for recognition and initial import steps for all mitochondrially directed proteins; constitutes the core element of the protein conducting pore; pre-Tom40p is phosphorylated by PKA, which impairs its import into mitochondria under non-respiratory conditions.
   
 
 0.859
CWC23
Pre-mRNA-splicing factor CWC23; Component of a complex containing Cef1p; putatively involved in pre-mRNA splicing; has similarity to E. coli DnaJ and other DnaJ-like proteins and to S. pombe Cwf23p.
    
 
 0.844
SSE1
ATPase component of heat shock protein Hsp90 chaperone complex; serves as nucleotide exchange factor to load ATP onto the SSA class of cytosolic Hsp70s; plays a role in prion propagation and determining prion variants; binds unfolded proteins; member of Hsp110 subclass of HSP70 proteins; deletion results in spindle elongation in S phase; SSE1 has a paralog, SSE2, that arose from the whole genome duplication.
  
 0.816
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.
   
   0.808
JJJ2
J protein JJJ2; Protein of unknown function; contains a J-domain, which is a region with homology to the E. coli DnaJ protein.
   
  
 0.786
RPL32
Ribosomal 60S subunit protein L32; overexpression disrupts telomeric silencing; homologous to mammalian ribosomal protein L32, no bacterial homolog.
 
 
  
 0.784
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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