An IFN-γ–induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I–presented peptides

By T. Šarić, Shi-Chung Chang, A. Hattori, I. York, S. Markant, K. Rock, M. Tsujimoto, A. Goldberg. Nature Immunology, 2002

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Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. (2006, background): “Within the ER is a newly discovered aminopeptidase, endoplasmic reticulum aminopeptidase 1 (ERAP1), which has the unusual capacity to trim extra amino acids off the longer precursors and then stops at eight to nine residues, the precise length for binding to MHC molecules (53,57,58).”
Molecular Mechanisms of IFN-γ to Up-Regulate MHC Class I Antigen Processing and Presentation (2009, neutral): “Other amino-peptidases cannot do that [145].”
Pathways of Antigen Processing (2013, background): “One other ER luminal component that is critically important for the proper generation of MHC-I-peptide complexes is an aminopeptidase, in the mouse called ER Aminopeptidase associated with Antigen Processing (ERAAP) and in humans called ER Aminopeptidase-1 (ERAP1) (Figure 3) (38, 39).”