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 UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue.
-
Recombinant Cne1p shows chaperone activity and lectin-site dependence in citrate synthase denaturation/refolding assays.
"Cne1p effectively suppressed the thermal denaturation of CS and enhanced the refolding of thermally or chemically denatured CS in a concentration-dependent manner... the chaperone function of Cne1p was greatly affected in the presence of monoglucosylated oligosaccharides (G1M9) that specifically bind to the lectin site."
Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities.
-
Cne1p interacts functionally with ER oxidoreductase Mpd1p, supporting a role in the ER folding/chaperone network but not a generic protein-binding annotation.
"Mpd1p alone does not have chaperone activity but that it interacts with and inhibits the chaperone activity of Cne1p"
Unstable mutant lysozymes are degraded through the interaction with calnexin homolog Cne1p in Saccharomyces cerevisiae.
-
Cne1p interacts with unstable misfolded lysozymes and promotes their ER retention and subsequent elimination via ER-associated degradation.
"These results suggest that in yeasts, Cne1p interacts with misfolded lysozyme proteins possibly causing their retention in the ER and subsequent elimination via ER-associated degradation."
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.
Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus.
-
Cne1p is an ER membrane glycoprotein and ER quality-control factor; the same study reported no detectable Ca2+ binding for Cne1p.
"Localization of the Cne1p protein by differential and analytical subcellular fractionation as well as by confocal immunofluorescence microscopy showed that it was exclusively located in the endoplasmic reticulum (ER)... Ca2+ binding activity has not been detected for Cne1p... Hence, Cne1p appears to function as a constituent of the S. cerevisiae ER protein quality control apparatus."
Falcon deep research report for CNE1
-
The Falcon report was reviewed and synthesized into the CNE1 curation, including core-function framing, family/PANTHER context, and evidence limitations.