Trimming of peptides in ER

Stable Identifier
R-HSA-983158
Type
Reaction [BlackBoxEvent]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
Participants
Participates
Catalyst Activity

endopeptidase activity of ERAP1/2 [endoplasmic reticulum lumen]

Orthologous Events
Authored
Reviewed
Created
Cite Us!