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
DNAJC5GDnaJ heat shock protein family (Hsp40) member C5 gamma. (184 aa)    
Predicted Functional Partners:
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 [...]
  
 0.710
HSPA9
Heat shock protein family A (Hsp70) member 9; Belongs to the heat shock protein 70 family.
  
 0.696
HSPA6
Heat shock 70 kDa protein 6; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP [...]
  
 0.683
HSPA1L
Heat shock 70 kDa protein 1-like; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis an [...]
  
 0.678
A0A287BQU9_PIG
Uncharacterized protein.
  
 0.676
HSPA8
Uncharacterized protein; Belongs to the heat shock protein 70 family.
  
 0.675
HSPH1
Heat shock protein family H (Hsp110) member 1.
  
 0.672
HSPA13
Heat shock protein family A (Hsp70) member 13.
  
 0.670
HSPA14
Heat shock protein family A (Hsp70) member 14; Belongs to the heat shock protein 70 family.
  
 0.670
HSPA4
Heat shock protein family A (Hsp70) member 4.
  
 0.667
Your Current Organism:
Sus scrofa
NCBI taxonomy Id: 9823
Other names: S. scrofa, pig, pigs, swine, wild boar
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.