Type |
Details |
Score |
Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
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•
•
•
•
•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
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|
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•
•
•
•
•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform |
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•
•
•
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•
|
Allele |
Name: |
protein disulfide isomerase associated 6; endonuclease-mediated mutation 2, Shanghai Model Organisms Center |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Null/knockout |
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•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, endonuclease-mediated mutation, mutant strain |
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•
•
•
•
•
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Allele |
Name: |
protein disulfide isomerase associated 6; endonuclease-mediated mutation 1, Shanghai Model Organisms Center |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Conditional ready, No functional change |
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•
•
•
•
•
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Strain |
Attribute String: |
coisogenic, endonuclease-mediated mutation, mutant strain |
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•
•
•
•
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Publication |
First Author: |
Kimura T |
Year: |
2005 |
Journal: |
J Biol Chem |
Title: |
Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities. |
Volume: |
280 |
Issue: |
36 |
Pages: |
31438-41 |
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•
•
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•
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Protein Domain |
Type: |
Family |
Description: |
This entry represents a group disulfide-isomerases, including PDIA6 from animals, Mpd1 from yeasts and PDI22/PDI23 from Arabidopsis. Protein-disulfide isomerase (PDI) is a resident of the endoplasmic reticulum (ER) that catalyses the formation, reduction, and isomerization of disulfide bonds. PDIA6 is an active oxidoreductase with similar enzymatic properties to other PDIs; however, it doesn't seem to be involved directly in protein folding. Instead, it regulates the unfolded protein response (UPR) through controlling the decay of IRE1alpha signaling via disulfide-dependent association []. Mpd1 have oxidative refolding activity and interacts with Cne1, an integral membrane ER chaperone involved in folding and quality control of glycoproteins []. |
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Publication |
First Author: |
Eletto D |
Year: |
2012 |
Journal: |
J Cell Sci |
Title: |
Limitation of individual folding resources in the ER leads to outcomes distinct from the unfolded protein response. |
Volume: |
125 |
Issue: |
Pt 20 |
Pages: |
4865-75 |
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•
•
•
•
•
|
Publication |
First Author: |
Wen W |
Year: |
2024 |
Journal: |
Front Pharmacol |
Title: |
Sex-specific effects of alcohol on neurobehavioral performance and endoplasmic reticulum stress: an analysis using neuron-specific MANF deficient mice. |
Volume: |
15 |
|
Pages: |
1407576 |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
440
 |
Fragment?: |
false |
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•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
440
 |
Fragment?: |
false |
|
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•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
445
 |
Fragment?: |
false |
|
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•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
391
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
445
 |
Fragment?: |
false |
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•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
445
 |
Fragment?: |
false |
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•
•
•
•
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