Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.
ERp16, an endoplasmic reticulum-resident thiol-disulfide oxidoreductase: biochemical properties and role in apoptosis induced by endoplasmic reticulum stress.
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ERp16 (the same protein as ERp18/ERp19/hTLP19/TXNDC12) is an ER-lumen thiol-disulfide oxidoreductase (redox potential about -165 mV) that catalyzes formation, reduction, and isomerization of disulfide bonds via its CGAC motif.
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Catalytically active TXNDC12 protects HeLa cells against ER-stress-induced apoptosis, whereas a catalytically dead mutant or knockdown potentiates it, indicating a catalysis-dependent role in defense against prolonged ER stress.
A proteome-scale map of the human interactome network.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
A novel role for protein disulfide isomerase ERp18 in venous thrombosis.
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ERp18 (TXNDC12) enhances venous thrombosis: ERp18-knockout mice develop significantly less thrombosis in an inferior vena cava stenosis model, and this pro-thrombotic role is dependent on its enzymatic activity (the inactive CGAC-to-SGAS mutant fails to support thrombosis). ERp18 is detected in endothelial cells, leukocytes and platelets and its deficiency lowers vWF at the thrombus site, implicating ERp18 in regulating vWF release.
UniProt entry O95881 (TXD12_HUMAN), Thioredoxin domain-containing protein 12