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ERO1L ERO1L PPIB PPIB UBC UBC GANAB GANAB HSPA5 HSPA5 CANX CANX PDIA3 PDIA3 CALR CALR ERP27 ERP27 HLA-A HLA-A ERAP1 ERAP1
"PDIA3" - protein disulfide isomerase family A, member 3 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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small nodes:
protein of unknown 3D structure
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some 3D structure is known or predicted
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query proteins and first shell of interactors
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white nodes:
second shell of interactors
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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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Score
PDIA3protein disulfide isomerase family A, member 3 (505 aa)    
Predicted Functional Partners:
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 score_image   0.999
CANX
calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] (592 aa)
      score_image score_image score_image score_image   0.999
ERP27
endoplasmic reticulum protein 27 (273 aa)
      score_image score_image   score_image   0.994
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   0.978
HLA-A
major histocompatibility complex, class I, A; Involved in the presentation of foreign antigens to the immune system (By similarity) (365 aa)
        score_image score_image score_image   0.968
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   0.955
UBC
ubiquitin C (685 aa)
      score_image score_image   score_image   0.948
ERAP1
endoplasmic reticulum aminopeptidase 1; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play [...] (948 aa)
        score_image score_image score_image   0.945
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   0.944
GANAB
glucosidase, alpha; neutral AB; Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (966 aa)
      score_image score_image score_image score_image   0.940
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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