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STRINGSTRING
HSPA4 HSPA4 DNAJB5 DNAJB5 HSPA5 HSPA5 HSPA1L HSPA1L HSP90AA1 HSP90AA1 HSP90AB1 HSP90AB1 HSPA8 HSPA8 HSPH1 HSPH1 STIP1 STIP1 HSPA4L HSPA4L HSPA6 HSPA6
"DNAJB5" - 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
DNAJB5DnaJ (Hsp40) homolog, subfamily B, member 5 (462 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   0.951
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   0.937
STIP1
stress-induced-phosphoprotein 1; Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB) (543 aa)
      score_image score_image   score_image   0.931
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   0.929
HSPA4
heat shock 70kDa protein 4 (840 aa)
score_image   score_image score_image score_image   score_image   0.925
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   0.925
HSPA4L
heat shock 70kDa protein 4-like; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (By similarity) (839 aa)
score_image   score_image score_image score_image   score_image   0.921
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   0.905
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   0.900
HSPA1L
heat shock 70kDa protein 1-like (641 aa)
score_image   score_image score_image score_image   score_image   0.897
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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