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Dnajb1 Dnajb1 Dnajc10 Dnajc10 Hyou1 Hyou1 Hsp90ab1 Hsp90ab1 Hspa5 Hspa5 Pdia4 Pdia4 Cad Cad Hsp90b1 Hsp90b1 Hsp90aa1 Hsp90aa1 Dnajb11 Dnajb11 Dnajb9 Dnajb9
"Hspa5" - Heat shock protein 5 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.
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
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Score
Hspa5Heat shock protein 5; Probably 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 (By similarity) (655 aa)    
Predicted Functional Partners:
Hsp90b1
Heat shock protein 90, 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. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity) (802 aa)
      score_image score_image score_image score_image   0.999
Hsp90aa1
Heat shock protein 90, 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 (By similarity). Binds bacterial lipo [...] (733 aa)
      score_image score_image   score_image   0.994
Hsp90ab1
Heat shock protein 90 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 (By similarity) (724 aa)
      score_image score_image score_image score_image   0.994
Dnajc10
DnaJ (Hsp40) homolog, subfamily C, member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase [...] (793 aa)
score_image     score_image score_image score_image score_image   0.991
Dnajb11
DnaJ (Hsp40) homolog, subfamily B, member 11; Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (By similarity) (358 aa)
score_image   score_image score_image score_image score_image score_image   0.990
Pdia4
Protein disulfide isomerase associated 4 (641 aa)
score_image     score_image score_image score_image score_image   0.982
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 (By similarity) (999 aa)
    score_image score_image score_image score_image score_image score_image 0.982
Dnajb9
DnaJ (Hsp40) homolog, subfamily B, member 9; Involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Acts as a co-chaperone with an Hsp70 protein (222 aa)
score_image   score_image score_image score_image score_image score_image   0.972
Dnajb1
DnaJ (Hsp40) homolog, subfamily B, member 1; Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP (By similarity) (340 aa)
score_image   score_image score_image score_image score_image score_image   0.970
Cad
Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase; This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase) (2225 aa)
score_image     score_image score_image   score_image   0.961
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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