Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Tyrosine is monoiodinated
Two DITs combine to form thyroxine
DIT and MIT combine to form triiodothyronine
Huntingtin interacting proteins are genetic modifiers of neurodegeneration.
Hepatitis C virus infection protein network.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Identification of a novel partner of duox: EFP1, a thioredoxin-related protein.
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TXNDC11/EFP1 interacts with the cytoplasmic regions of DUOX1 and DUOX2 and with thyroid peroxidase, implicating it as a redox regulator in the thyroid H2O2-generating system, though it is not sufficient for DUOX-mediated H2O2 generation.
EDEM2 stably disulfide-bonded to TXNDC11 catalyzes the first mannose trimming step in mammalian glycoprotein ERAD.
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EDEM2 is stably disulfide-bonded to TXNDC11 (C558 of EDEM2 to C692 in the Trx5 domain, the only CXXC-containing Trx domain of TXNDC11); this covalent bond is essential for mannose trimming and subsequent glycoprotein ERAD.
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The Trx5 domain of TXNDC11 exhibits reductase activity in vitro; TXNDC11 functions as a reductase rather than an oxidase in this complex.
Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates.
High Thioredoxin Domain-Containing Protein 11 Expression Is Associated with Tumour Progression in Glioma.
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High TXNDC11 protein expression is associated with WHO high-grade tumour classification and poor prognosis in glioma and is an independent prognostic factor; TXNDC11 silencing inhibits proliferation, migration and invasion and induces apoptosis in GBM cells, while overexpression has the opposite effect.
Mechanisms of substrate processing during ER-associated protein degradation.
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Authoritative 2023 review placing TXNDC11 among mammalian ERAD factors that coordinate recognition, processing, ubiquitylation, extraction and proteasomal targeting of ER substrates.
Regulation of the ER-Resident Mannosidase EDEM2 in HEK293 Cells.
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TXNDC11 deficiency markedly decreases EDEM2 protein without a corresponding decrease in EDEM2 mRNA, indicating that TXNDC11 post-transcriptionally stabilizes EDEM2; reductive stress (DTT) destabilizes both EDEM2 and TXNDC11 protein, and the destabilized EDEM2 can become an SEL1L-dependent ERAD substrate.
UniProt entry Q6PKC3 (TXD11_HUMAN), Thioredoxin domain-containing protein 11