Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB Subcellular Location vocabulary mapping
ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57.
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ERp27 is a two-domain ER-located protein homologous to the non-catalytic b and b' domains of PDI; it binds the PDI test peptide Delta-somatostatin via its second domain, undergoes a conformational change on substrate binding, and interacts with ERp57/PDIA3 (PDIA3-binding site residues 230-233).
The varicellovirus UL49.5 protein blocks the transporter associated with antigen processing (TAP) by inhibiting essential conformational transitions in the 6+6 transmembrane TAP core complex.
The crystal structure of the protein-disulfide isomerase family member ERp27 provides insights into its substrate binding capabilities.
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The crystal structure of redox-inactive ERp27 reveals a PDI-homologous substrate-binding cleft that adapts in size and hydrophobicity; ITC shows ERp27 distinguishes folded from unfolded substrates, only binding the latter, and is up-regulated during ER stress, presumably binding misfolded substrates and presenting them to ERp57 for catalysis.
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.
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.
UniProt entry Q96DN0 (ERP27_HUMAN), Endoplasmic reticulum resident protein 27