Trimming of peptides in ER

Stable Identifier
Reaction [BlackBoxEvent]
Homo sapiens
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Transporter associated with antigen processing (TAP) prefers peptides 8-16 residues long, slightly longer than the canonical 8-10 residue peptides that fit into class I MHC binding sites. These longer peptides are further trimmed at their N-termini by the ER-associated aminopeptidase (ERAP). ERAP trims peptides to a length of 8-10 residues, suitable for loading into the MHC class I binding groove.

Literature References
PubMed ID Title Journal Year
12436110 The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues

Rock, KL, Favreau, JM, Chang, SC, Keys, JA, Saric, T, Goldberg, AL, York, IA

Nat Immunol 2002
17088086 ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum

Blanchard, N, Gonzalez, F, Shastri, N, Hammer, GE, Kanaseki, T

Immunity 2006
12436109 An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides

Tsujimoto, M, Rock, KL, Hattori, A, Markant, S, Chang, SC, Saric, T, Goldberg, AL, York, IA

Nat Immunol 2002
Catalyst Activity

endopeptidase activity of ERAP1/2 [endoplasmic reticulum lumen]

Orthologous Events
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