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
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
htpGMolecular chaperone HtpG; Molecular chaperone. Has ATPase activity. (628 aa)    
Predicted Functional Partners:
dnaJ
Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]
 
 0.971
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.966
dnaK-2
Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.965
OAH46563.1
Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.960
OAH43151.1
Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.948
groEL
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.921
groEL-2
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.921
OAH37877.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
   
 
 0.921
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.920
OAH42599.1
ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.
   
  
 0.915
Your Current Organism:
Sphingobium yanoikuyae
NCBI taxonomy Id: 13690
Other names: ATCC 51230, Beijerinckia sp. B1, CCUG 28380, CCUG 31205, CIP 106726, DSM 7462, GIFU 9882, GIFU:9882, IFO 15102, JCM 7371, LMG 11252, LMG:11252, NBRC 15102, S. yanoikuyae, Sphingobium sp. TJ, Sphingomonas yanoikuyae
Server load: low (20%) [HD]