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ERO1LB ERO1LB ERO1L ERO1L UBC UBC PDIA4 PDIA4 HYOU1 HYOU1 HSPA5 HSPA5 APOB APOB TG TG HSP90B1 HSP90B1 PPIB PPIB CALR CALR
"PDIA4" - protein disulfide isomerase family A, member 4 in Homo sapiens
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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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protein of unknown 3D structure
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some 3D structure is known or predicted
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white nodes:
second shell of interactors
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from curated databases
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experimentally determined
Predicted Interactions
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fusion edge
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gene co-occurrence
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textmining
coexpression edge
co-expression
homology edge
protein homology
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[Homology]
Score
PDIA4protein disulfide isomerase family A, member 4 (645 aa)    
Predicted Functional Partners:
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   0.993
ERO1L
ERO1-like (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of g [...] (468 aa)
        score_image score_image score_image   0.985
ERO1LB
ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] (467 aa)
        score_image score_image score_image   0.982
APOB
apolipoprotein B (including Ag(x) antigen) (4563 aa)
        score_image   score_image   0.972
CALR
calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity) (417 aa)
      score_image score_image   score_image   0.953
PPIB
peptidylprolyl isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (216 aa)
      score_image score_image   score_image   0.951
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   0.949
TG
thyroglobulin (2768 aa)
        score_image   score_image   0.936
UBC
ubiquitin C (685 aa)
      score_image score_image   score_image   0.931
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   0.927
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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