3.4.11.22	additional information	ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules, overview, loss of enzyme results in disruption of generation of naturally processed peptides in the endoplasmic reticulum, decreased stability of peptide-MHC class I complexes, and diminished CD8+ T cell responses	
3.4.11.22	additional information	ERAP1 trims MHC class I-presented peptides in vivo and plays an important role in immunodominance, overview	
3.4.11.22	additional information	the endoplasmic reticulum enzyme ERAP1 trims precursors to lengths of MHC class I peptides by a 'molecular ruler' mechanism, overview, the enzyme is important in antigen presentation, overview	
3.4.11.22	additional information	the glycosylated Ape2 aminopeptidase might be responsible for uptake of hydrophobic peptides, especially of leucine N-terminal peptides	
3.4.11.22	additional information	ERAP1 trims a large variety of long peptide sequences efficiently, and its activity drops dramatically for peptides shorter than eight or nine amino acids, the enzyme efficiently excises virtually any amino acid in the context of a larger peptide, ERAP1 has broad N-terminal specificity due to strong preferences for residues downstream in the peptide-substrate sequence