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
Mnod_2958PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane protein. (566 aa)    
Predicted Functional Partners:
dnaJ
Chaperone protein 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, D [...]
 0.993
grpE
GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 i [...]
 
 0.983
Mnod_1070
PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: met:M446_2102 heat shock protein DnaJ domain-containing protein.
 0.973
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.927
groL-2
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.927
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.922
Mnod_7171
KEGG: met:M446_6321 NifU domain-containing protein.
  
 0.902
Mnod_0778
PFAM: ATPase AAA-2 domain protein; KEGG: oan:Oant_4466 ATPase AAA-2 domain protein.
 
 
 0.893
Mnod_4909
PFAM: heat shock protein DnaJ domain protein; protein of unknown function DUF1332; KEGG: met:M446_4375 heat shock protein DnaJ domain-containing protein.
  
 0.885
clpB
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
 
 
 0.880
Your Current Organism:
Methylobacterium nodulans
NCBI taxonomy Id: 460265
Other names: M. nodulans ORS 2060, Methylobacterium nodulans ORS 2060, Methylobacterium nodulans str. ORS 2060, Methylobacterium nodulans strain ORS 2060
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