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
CALRCalreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin family. (417 aa)    
Predicted Functional Partners:
PDIA3
Protein disulfide-isomerase.
   
 0.999
HSP90B1
Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Belongs to the heat shock protein 90 family.
   
 0.997
HSPA5
Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...]
   
 
 0.975
CANX
Calnexin.
   
 
0.968
PDIA4
Protein disulfide-isomerase.
   
 
 0.965
P4HB
Protein disulfide-isomerase.
   
 
 0.935
TAP2
Uncharacterized protein.
   
 0.933
PDIA6
Uncharacterized protein; Belongs to the protein disulfide isomerase family.
   
 
 0.931
TAP1
Transporter 1, ATP binding cassette subfamily B member.
   
 0.926
B2M
Beta-2-microglobulin; Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity).
   
 0.926
Your Current Organism:
Sus scrofa
NCBI taxonomy Id: 9823
Other names: S. scrofa, pig, pigs, swine, wild boar
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