STRINGSTRING
SSE1 SSE1 Q6FNN5_CANGA Q6FNN5_CANGA YDJ1 YDJ1 CPR6 CPR6 Q6FRI9_CANGA Q6FRI9_CANGA Q6FS39_CANGA Q6FS39_CANGA SSA1 SSA1 SSA3 SSA3 Q6FTE2_CANGA Q6FTE2_CANGA SSB1 SSB1
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:
SSE1Heat shock protein homolog SSE1. (694 aa)
Q6FNN5_CANGAUncharacterized protein. (479 aa)
YDJ1Uncharacterized protein. (407 aa)
CPR6Peptidyl-prolyl cis-trans isomerase D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). (371 aa)
Q6FRI9_CANGAUncharacterized protein. (583 aa)
Q6FS39_CANGAJ domain-containing protein. (349 aa)
SSA1Uncharacterized protein; Belongs to the heat shock protein 70 family. (640 aa)
SSA3Uncharacterized protein; Belongs to the heat shock protein 70 family. (647 aa)
Q6FTE2_CANGAFlavin_Reduct domain-containing protein. (215 aa)
SSB1Ribosome-associated molecular chaperone SSB; Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation- prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-b [...] (613 aa)
Your Current Organism:
Candida glabrata
NCBI taxonomy Id: 284593
Other names: Candida glabrata ATCC 2001, Candida glabrata ATCC2001, Candida glabrata CBS 138, Candida glabrata CBS138, [. glabrata CBS 138, [Candida] glabrata CBS 138
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