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SUGT1P3 SUGT1P3 TTC12 TTC12 CDC37 CDC37 HSP90AA1 HSP90AA1 SUGT1 SUGT1 PTGES3 PTGES3 HSP90AB1 HSP90AB1 UBC UBC AHSA1 AHSA1 PPID PPID STIP1 STIP1
"HSP90AB1" - heat shock protein 90kDa alpha 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.
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small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
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colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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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
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from curated databases
experiment edge
experimentally determined
Predicted Interactions
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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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HSP90AB1heat 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)    
Predicted Functional Partners:
SUGT1
SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae); May play a role in ubiquitination and subsequent proteasomal degradation of target proteins (365 aa)
      score_image score_image score_image score_image   0.999
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   0.999
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 score_image score_image 0.999
PTGES3
prostaglandin E synthase 3 (cytosolic); Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor- mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (160 aa)
      score_image score_image   score_image   0.999
UBC
ubiquitin C (685 aa)
      score_image score_image   score_image   0.999
AHSA1
AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast); Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking (338 aa)
      score_image score_image   score_image   0.999
CDC37
cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (378 aa)
      score_image score_image score_image score_image   0.999
PPID
peptidylprolyl isomerase D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be i [...] (370 aa)
      score_image score_image   score_image   0.999
SUGT1P3
suppressor of G2 allele of SKP1 (S. cerevisiae) pseudogene 3 (91 aa)
      score_image score_image   score_image   0.999
TTC12
tetratricopeptide repeat domain 12 (705 aa)
      score_image score_image   score_image   0.999
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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