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  • 11.0 [archived version]
STRINGSTRING
ERICH4 ERICH4 MAGEB2 MAGEB2 TXNRD1 TXNRD1 PDILT PDILT DNAJC10 DNAJC10 CALR3 CALR3 CANX CANX TPST2 TPST2 ERO1L ERO1L CLGN CLGN ADAM2 ADAM2
"PDILT" - Protein disulfide-isomerase-like protein of the testis in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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PDILTProtein disulfide-isomerase-like protein of the testis; Probable redox-inactive chaperone involved in spermatogenesis; Belongs to the protein disulfide isomerase family (584 aa)    
Predicted Functional Partners:
CALR3
Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family (384 aa)
     
 
  0.814
CLGN
Calmegin; Functions during spermatogenesis as a chaperone for a range of client proteins that are important for sperm adhesion onto the egg zona pellucida and for subsequent penetration of the zona pellucida. Required for normal sperm migration from the uterus into the oviduct. Required for normal male fertility. Binds calcium ions (By similarity) (610 aa)
     
 
  0.760
ERO1L
ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby pla [...] (468 aa)
     
 
  0.667
TXNRD1
Thioredoxin reductase 1, cytoplasmic; Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid; Glutaredoxin domain containing (649 aa)
   
 
  0.644
TPST2
Protein-tyrosine sulfotransferase 2; Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3’-phosphoadenylyl sulfate (PAPS) as cosubstrate; Sulfotransferases, membrane bound (377 aa)
     
 
  0.643
ADAM2
Disintegrin and metalloproteinase domain-containing protein 2; Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein; ADAM metallopeptidase domain containing (735 aa)
     
 
  0.593
MAGEB2
Melanoma-associated antigen B2; May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3-substrate complex; MAGE family (319 aa)
           
  0.583
DNAJC10
DnaJ 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 activity, [...] (793 aa)
     
 
  0.565
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)
     
 
  0.537
ERICH4
Glutamate-rich protein 4; Glutamate rich 4 (130 aa)
           
  0.497
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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