Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT).
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First comprehensive characterization of GILT enzymatic function.
"We describe here a lysosomal thiol reductase optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro."
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Demonstrated thiol reductase activity optimal at acidic pH.
"We describe here a lysosomal thiol reductase optimally active at low pH"
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Identified CXXC active site through mutagenesis.
"The active site, determined by mutagenesis, consists of a pair of cysteine residues separated by two amino acids, similar to other enzymes of the thioredoxin family."
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Showed mannose-6-phosphate receptor-mediated lysosomal targeting.
"After delivery into the endosomal/lysosomal system by the mannose 6-phosphate receptor, N- and C-terminal prosequences are removed."
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Demonstrated processing from 35 kDa precursor to mature form.
"The enzyme is a soluble glycoprotein that is synthesized as a precursor."
Functional requirements for the lysosomal thiol reductase GILT in MHC class II-restricted antigen processing.
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Demonstrated that GILT thiol reductase activity is essential for MHC class II antigen processing.
"These studies demonstrate that the thiol reductase activity of GILT is its essential function in MHC class II-restricted Ag processing."
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Showed that active site cysteine mutations abolish antigen processing function.
"Mutation of either Cys(46) or Cys(49) abrogated MHC class II processing of a GILT-dependent HEL epitope."
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Established functional link between enzymatic activity and immune function.
"These studies demonstrate that the thiol reductase activity of GILT is its essential function in MHC class II-restricted Ag processing."
A proteome-scale map of the human interactome network.
Molecular and biochemical characterization of a novel gamma-interferon-inducible protein.
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Original characterization of IP-30 (GILT) as IFN-gamma-inducible protein.
"A cDNA clone has been isolated from mRNA derived from the monocytic cell line U937, which detects an mRNA that is present and inducible by gamma-interferon"
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Demonstrated secretion and intracellular processing.
"a 30-kDa polypeptide (referred to as IP-30) is either secreted or converted intracellularly into a 25-kDa protein"
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Showed vesicular localization consistent with lysosomes.
"Indirect immunofluorescence microscopy reveals a punctate fluorescence pattern in monocytes consistent with a vesicular subcellular location."
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Identified disulfide-linked dimeric forms.
"the extracellular form is involved in both intrachain and interchain disulfide bonding."
A reference map of the human binary protein interactome.
Expression of IFNG-stimulated genes
MHC class II antigen presentation
Reduction of disulphide bonds in MHC II antigens
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GILT specifically catalyzes disulfide bond reduction in MHC II antigens.
"The lysosomal thiol reductase gamma-IFN-inducible lysosomal thiol reductase (GILT) has been shown to facilitate MHC class II-restricted antigen (Ag) processing by breaking disulphide bonds."
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Optimal activity at acidic pH in lysosomes.
"The reduction of disulphide bonds by mature GILT is optimal at acidic pH"