STRINGSTRING
AFW93725.1 AFW93725.1 groEL groEL AFW95083.1 AFW95083.1 dnaJ dnaJ dnaK dnaK grpE grpE AFW95936.1 AFW95936.1 groS groS groL groL dnaK-2 dnaK-2 dnaJ-2 dnaJ-2 dnaK-3 dnaK-3 AFW96959.1 AFW96959.1
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:
AFW93725.1DnaJ-class molecular chaperone. (325 aa)
groELChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (557 aa)
AFW95083.1Heat shock protein 90. (655 aa)
dnaJChaperone 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 [...] (379 aa)
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (621 aa)
grpEGrpE 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 [...] (224 aa)
AFW95936.1DnaJ domain-containing protein. (229 aa)
groSChaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (103 aa)
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (544 aa)
dnaK-2Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (686 aa)
dnaJ-2Chaperone protein DnaJ. (331 aa)
dnaK-3Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (635 aa)
AFW96959.1Heat shock protein 70. (532 aa)
Your Current Organism:
Anabaena sp. 90
NCBI taxonomy Id: 46234
Other names: A. sp. 90, Anabaena circinalis 90, Anabaena sp. strain 90
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