STRINGSTRING
Hspa12a protein (mouse) - STRING interaction network
"Hspa12a" - Heat shock protein 12A in Mus musculus
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
Hspa12aHeat shock protein 12A (675 aa)    
Predicted Functional Partners:
Hspa4l
Heat shock 70 kDa protein 4L; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (838 aa)
     
  0.982
Hspa4
Heat shock protein 4; Belongs to the heat shock protein 70 family (842 aa)
     
  0.982
Hspa9
Stress-70 protein, mitochondrial; Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (By similarity). Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging; Belongs to the heat shock protein 70 family (679 aa)
     
  0.979
Hspa13
Heat shock 70 kDa protein 13; Has peptide-independent ATPase activity; Belongs to the heat shock protein 70 family (471 aa)
         
  0.975
Hspa14
Heat shock 70 kDa protein 14; Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity (By similarity); Belongs to the heat shock protein 70 family (509 aa)
         
  0.972
Hsph1
Heat shock protein 105 kDa; Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (By similarity). 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)
     
  0.969
Dnajc2
DnaJ homolog subfamily C member 2; Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone- component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb- repressed genes to an active state- specifically recruited at hist [...] (621 aa)
     
  0.961
Hspa5
78 kDa glucose-regulated protein; Plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate; Belongs to the heat shock protein 70 family (655 aa)
     
  0.957
Dnajb1
DnaJ homolog subfamily B member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (340 aa)
   
  0.938
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 [...] (641 aa)
         
  0.937
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus muscaris, Mus musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
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