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.
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
Isop_0076Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023: IPR018181: IPR013126; KEGG: cac:CA_C0472 HSP70/DnaK family protein; PFAM: Heat shock protein 70; SPTR: Chaperone protein dnaK; PFAM: Hsp70 protein. (560 aa)    
Predicted Functional Partners:
Isop_2051
Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623: IPR002939: IPR003095: IPR018253; KEGG: psl:Psta_4209 chaperone DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Chaperone DnaJ domain protein; PFAM: DnaJ C terminal region; DnaJ domain.
 
 0.926
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 [...]
 
 0.924
grpE-2
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 [...]
 
 
 0.896
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 [...]
 
 
 0.813
Isop_0219
ATP-binding region ATPase domain protein; COGs: COG0326 Molecular chaperone HSP90 family; InterPro IPR001404: IPR020575: IPR003594; KEGG: lic:LIC12469 HSP90 family protein; PFAM: ATP-binding region ATPase domain protein; SPTR: HtpG; PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.
   
 0.804
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.804
thiE
Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family.
  
 
 0.796
Isop_1969
Nitrogen-fixing NifU domain protein; COGs: COG0822 NifU homolog involved in Fe-S cluster formation; InterPro IPR002871; KEGG: plm:Plim_1321 nitrogen-fixing NifU domain protein; PFAM: nitrogen-fixing NifU domain protein; SPTR: Nitrogen-fixing NifU domain protein; PFAM: NifU-like N terminal domain; TIGRFAM: SUF system FeS assembly protein, NifU family.
 
 0.786
Isop_3138
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 [...]
  
 
 0.777
Isop_0075
KEGG: pan:PODANSg8032 hypothetical protein; SPTR: Chromosome 10 SCAF15123, whole genome shotgun sequence.
       0.773
Your Current Organism:
Isosphaera pallida
NCBI taxonomy Id: 575540
Other names: I. pallida ATCC 43644, Isosphaera pallida ATCC 43644, Isosphaera pallida DSM 9630, Isosphaera pallida IS1B, Isosphaera pallida str. ATCC 43644, Isosphaera pallida strain ATCC 43644
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