(Q27547546)

Protein disulphide isomerase

1 reference

Thioredoxin domain, protein family

1 reference

based on heuristic

inferred from protein domain or family

Thioredoxin, conserved site, protein family

1 reference

based on heuristic

inferred from protein domain or family

found in taxon

Saccharomyces cerevisiae S288c

1 reference

25 May 2022

1 reference

25 May 2022

protein-disulfide reductase activity

1 reference

9 May 2019

Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

protein disulfide isomerase activity

Functional differences in yeast protein disulfide isomerases

5 references

21 June 2018

http://www.ebi.ac.uk/QuickGO/annotations?protein=P17967&geneProductId=UniProtKB:P17967

http://www.ebi.ac.uk/QuickGO/annotations?protein=P17967&geneProductId=UniProtKB:P17967

21 June 2018

http://www.ebi.ac.uk/QuickGO/annotations?protein=P17967&geneProductId=UniProtKB:P17967

21 June 2018

21 June 2018

Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities

http://www.ebi.ac.uk/QuickGO/annotations?protein=P17967&geneProductId=UniProtKB:P17967

21 June 2018

The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites

http://www.ebi.ac.uk/QuickGO/annotations?protein=P17967&geneProductId=UniProtKB:P17967

isomerase activity

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

1 reference

9 May 2019

protein binding

4 references

9 May 2019

Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

9 May 2019

Proteome survey reveals modularity of the yeast cell machinery

IntAct protein interaction database

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

9 May 2019

Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.

IntAct protein interaction database

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

9 May 2019

Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum

IntAct protein interaction database

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

unfolded protein binding

1 reference

9 May 2019

Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

protein disulfide isomerase activity

Functional differences in yeast protein disulfide isomerases

6 references

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

9 May 2019

9 May 2019

The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

9 May 2019

Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

9 May 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

IBA

cell component

endoplasmic reticulum

http://www.ebi.ac.uk/QuickGO/annotations?protein=P17967&geneProductId=UniProtKB:P17967

1 reference

21 June 2018

endoplasmic reticulum

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

3 references

9 May 2019

9 May 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

IBA

9 May 2019

One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

protein alpha-1,2-demannosylation

HDA

biological process

1 reference

9 May 2019

A Complex of Pdi1p and the Mannosidase Htm1p Initiates Clearance of Unfolded Glycoproteins from the Endoplasmic Reticulum

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

cell redox homeostasis

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

1 reference

9 May 2019

protein folding

IMP

1 reference

21 June 2018

Functional differences in yeast protein disulfide isomerases

http://www.ebi.ac.uk/QuickGO/annotations?protein=P17967&geneProductId=UniProtKB:P17967

mannose trimming involved in glycoprotein ERAD pathway

IMP

A Complex of Pdi1p and the Mannosidase Htm1p Initiates Clearance of Unfolded Glycoproteins from the Endoplasmic Reticulum

4 references

9 May 2019

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

IMP

9 May 2019

A Complex of Pdi1p and the Mannosidase Htm1p Initiates Clearance of Unfolded Glycoproteins from the Endoplasmic Reticulum

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

IGI

9 May 2019

A Complex of Pdi1p and the Mannosidase Htm1p Initiates Clearance of Unfolded Glycoproteins from the Endoplasmic Reticulum

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

9 May 2019

A Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

response to endoplasmic reticulum stress

IBA

1 reference

9 May 2019

Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium

http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P17967

1 reference

Thioredoxin, conserved site

1 reference

Identifiers

1 reference

20 March 2022

1 reference

25 May 2022

1 reference