Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Peroxiredoxin-4 interacts with and regulates the thromboxane A(2) receptor.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum.
Proteomic characterization of the human sperm nucleus.
Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4.
Toward an understanding of the protein interaction network of the human liver.
Quantitative interaction proteomics of neurodegenerative disease proteins.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation.
Exocytosis of secretory granule lumen proteins
Exocytosis of ficolin-rich granule lumen proteins
Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells.
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Endogenous PRDX4 in human cells is cotranslationally translocated, protected from proteinase K inside calnexin-containing membranes, and retained in the ER without secretion, despite lacking a retention/retrieval motif.
"The data indicate that native Prx IV is ER-retained in human cells even when over-produced, despite lacking a recognised retention/retrieval motif."
Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation.
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PRDX4 metabolises H2O2 produced by the ER oxidase Ero1 within the ER.
"Here, we show that mammalian peroxiredoxin IV (PrxIV) metabolises hydrogen peroxide produced by Ero1."
UniProt record for human PRDX4
Falcon deep research on PRDX4 function
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Falcon report identifies PRDX4 as ER-localized typical 2-Cys peroxiredoxin.
"PRDX4 catalyzes peroxide reduction through the canonical typical 2-Cys cycle"
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Falcon report emphasizes ER luminal localization and secreted/extracellular context.
"PRDX4 is localized mainly to the endoplasmic reticulum"