Trimming of peptides in ER

Stable Identifier
Reaction [omitted]
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
17088086 ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum

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

Immunity 2006
12436110 The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues

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

Nat Immunol 2002
12436109 An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides

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

Nat Immunol 2002
Participant Of
Catalyst Activity
Catalyst Activity
endopeptidase activity of ERAP1/2 [endoplasmic reticulum lumen]
Physical Entity
Orthologous Events
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