Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
HSPA6 HSPA6 HSPA8 HSPA8 HSPA5 HSPA5 HYOU1 HYOU1 HSPA4 HSPA4 HSPA1B HSPA1B HSPA1A HSPA1A HSP90B1 HSP90B1 DNAJB9 DNAJB9 HSPA2 HSPA2 HSPA13 HSPA13
"DNAJB9" - 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
DNAJB9DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) (223 aa)    
Predicted Functional Partners:
HSPA5
heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER (654 aa)
score_image   score_image score_image score_image   score_image   0.979
HSPA13
heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity (471 aa)
score_image   score_image score_image score_image   score_image   0.925
HYOU1
hypoxia up-regulated 1; Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding (999 aa)
score_image     score_image score_image   score_image   0.922
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   0.907
HSPA1A
heat shock 70kDa protein 1A (641 aa)
score_image   score_image score_image score_image   score_image   0.902
HSP90B1
heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (803 aa)
      score_image score_image   score_image   0.902
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   0.902
HSPA1B
heat shock 70kDa protein 1B (641 aa)
score_image   score_image score_image score_image   score_image   0.901
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   0.896
HSPA4
heat shock 70kDa protein 4 (840 aa)
score_image   score_image score_image score_image   score_image   0.894
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Server load: low (20%)