Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
UBC UBC HSP90AB1 HSP90AB1 DNAJB1 DNAJB1 HSPA2 HSPA2 HSPA8 HSPA8 HSP90AA1 HSP90AA1 HSPA1A HSPA1A HSPA6 HSPA6 HSPH1 HSPH1 DNAJB6 DNAJB6 GRPEL1 GRPEL1
"DNAJB6" - DnaJ in Homo sapiens
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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 each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
DNAJB6DnaJ (Hsp40) homolog, subfamily B, member 6 (326 aa)    
Predicted Functional Partners:
HSPA8
heat shock 70kDa 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 (646 aa)
score_image   score_image score_image score_image score_image score_image   0.999
HSP90AA1
heat shock protein 90kDa alpha (cytosolic), class A member 1; 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. 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 (854 aa)
      score_image score_image score_image score_image   0.990
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 (By similarity) (858 aa)
score_image   score_image score_image score_image score_image score_image   0.990
HSPA6
heat shock 70kDa protein 6 (HSP70B’); 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 (By similarity) (643 aa)
score_image   score_image score_image score_image score_image score_image   0.988
HSP90AB1
heat shock protein 90kDa alpha (cytosolic), class B member 1; 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. 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 (724 aa)
      score_image score_image score_image score_image   0.987
HSPA2
heat shock 70kDa protein 2; 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 (639 aa)
score_image   score_image score_image score_image   score_image   0.982
UBC
ubiquitin C (685 aa)
        score_image   score_image   0.963
GRPEL1
GrpE-like 1, mitochondrial (E. coli); Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (217 aa)
score_image     score_image score_image   score_image   0.950
DNAJB1
DnaJ (Hsp40) homolog, subfamily B, member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP (340 aa)
    score_image   score_image score_image score_image score_image 0.950
HSPA1A
heat shock 70kDa protein 1A (641 aa)
score_image   score_image score_image score_image   score_image   0.939
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Server load: low (22%)