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Bag2 protein (mouse) - STRING interaction network
"Bag2" - BCL2-associated athanogene 2 in Mus musculus
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
Bag2BCL2-associated athanogene 2; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (210 aa)    
Predicted Functional Partners:
Hspa8
Heat shock protein 8; Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (By similarity). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion. Participates in the ER-associated degra [...] (646 aa)
       
 
  0.934
Bag1
BCL2-associated athanogene 1; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli (355 aa)
         
  0.927
Hspa1a
Heat shock protein 1A; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. Essential for STUB1-mediated ubiquitination and degradation of FO [...] (641 aa)
       
  0.917
Hspbp1
HSPA (heat shock 70kDa) binding protein, cytoplasmic cochaperone 1; Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of target proteins (By similarity) (357 aa)
         
  0.872
Hspa4l
Heat shock protein 4 like; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (838 aa)
     
  0.859
Hsph1
Heat shock 105kDa/110kDa protein 1; Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (858 aa)
     
  0.854
Dnajc6
DnaJ (Hsp40) homolog, subfamily C, member 6; Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin-mediated endocytosis in neurons (968 aa)
       
      0.764
Gak
Cyclin G associated kinase; Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin- coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1 (By similarity) (1305 aa)
       
      0.764
Hspa1b
Heat shock protein 1B; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. Essential for STUB1-mediated ubiquitination and degradation of FO [...] (642 aa)
       
 
  0.589
Insm2
Insulinoma-associated 2; May function as a growth suppressor or tumor suppressor in liver cells and in certain neurons (493 aa)
     
   
  0.559
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus, Mus muscaris, Mus musculus, Mus sp. 129SV, house mouse, mice, mouse, nude mice, transgenic mice
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