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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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
HSPB8Heat shock protein family B (small) member 8; Belongs to the small heat shock protein (HSP20) family. (210 aa)    
Predicted Functional Partners:
BAG3
BCL2 associated athanogene 3.
   
 0.982
A0A287BQU9_PIG
Uncharacterized protein.
   
 0.807
HSPA8
Uncharacterized protein; Belongs to the heat shock protein 70 family.
   
 0.794
DNAJB2
DnaJ heat shock protein family (Hsp40) member B2.
   
 
 0.790
HSP90AB1
Heat shock protein 90 alpha family class B member 1.
   
 0.785
HSP90AA1
Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...]
   
 0.741
DNAJB1
J domain-containing protein.
   
 0.702
HSPA4
Heat shock protein family A (Hsp70) member 4.
    
 
 0.667
STUB1
STIP1 homology and U-box containing protein 1.
     
 0.656
HSPB1
Heat shock protein beta-1; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.
   
 
0.619
Your Current Organism:
Sus scrofa
NCBI taxonomy Id: 9823
Other names: S. scrofa, pig, pigs, swine, wild boar
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