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STRINGSTRING
PPIL6 PPIL6 ENSG00000108825 ENSG00000108825 HSP90B1 HSP90B1 PTGES3L PTGES3L HSP90AA1 HSP90AA1 HSP90AB1 HSP90AB1 TTC28 TTC28 PTGES3 PTGES3 TRAP1 TRAP1 PPID PPID PPIH PPIH
"TTC28" - tetratricopeptide repeat domain 28 in Homo sapiens
Nodes:
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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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query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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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
TTC28tetratricopeptide repeat domain 28 (2481 aa)    
Predicted Functional Partners:
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   0.999
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   0.999
TRAP1
TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity (704 aa)
      score_image score_image   score_image   0.960
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   0.951
PTGES3L
prostaglandin E synthase 3 (cytosolic)-like (166 aa)
      score_image score_image   score_image   0.918
ENSG00000108825
PTGES3L-AARSD1 readthrough; Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala) (By similarity) (586 aa)
      score_image score_image   score_image   0.918
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   0.918
PPIL6
peptidylprolyl isomerase (cyclophilin)-like 6; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (337 aa)
      score_image score_image   score_image   0.884
PPIH
peptidylprolyl isomerase H (cyclophilin H); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone (177 aa)
      score_image score_image   score_image   0.884
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   0.884
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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