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Literature summary for 3.4.11.22 extracted from

  • Chen, L.; Fischer, R.; Peng, Y.; Reeves, E.; McHugh, K.; Ternette, N.; Hanke, T.; Dong, T.; Elliott, T.; Shastri, N.; Kollnberger, S.; James, E.; Kessler, B.; Bowness, P.
    Critical role of endoplasmic reticulum aminopeptidase 1 in determining the length and sequence of peptides bound and presented by HLA-B27 (2014), Arthritis Rheum., 66, 284-294.
    View publication on PubMed
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Application

Application Comment Organism
medicine in both HeLa-B27 and C1R-B27 cells, the proportion of 9-mer HLA-B27-bound peptides is decreased by isoform ERAP1 silencing, whereas the percentages of longer peptides, 11-13 mer, are increased. Following ERAP1 silencing, C-terminally extended peptides are readily identified. These are better able to bind to HLA–B27 than N-terminally extended peptides lacking an arginine at position 2. In both HeLa-B27 cells and mouse fibroblasts expressing HLA-B27, the absence of ERAP1 reduces peptide recognition by HLA-B27-restricted immunodominant viral HLA–B27 epitope KK10-specific cytotoxic T-lymphocytes. Presence of an ankylosing spondylitis-protective variant of ERAP1, K528R, as compared to wild-type ERAP1, reduces the peptide recognition by KK10 cytotoxic T lymphocytes following transfection with extended KK10 minigenes Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Homo sapiens 5783
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9NZ08
-
-

Source Tissue

Source Tissue Comment Organism Textmining
C1R-B27 cell
-
 Homo sapiens
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HeLa cell
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 Homo sapiens
-

Synonyms

Synonyms Comment Organism
endoplasmic reticulum aminopeptidase 1
-
 Homo sapiens
ERAP1
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function in both HeLa-B27 and C1R-B27 cells, the proportion of 9-mer HLA-B27-bound peptides is decreased by isoform ERAP1 silencing, whereas the percentages of longer peptides, 11-13 mer, are increased. Following ERAP1 silencing, C-terminally extended peptides are readily identified. These are better able to bind to HLA–B27 than N-terminally extended peptides lacking an arginine at position 2. In both HeLa-B27 cells and mouse fibroblasts expressing HLA-B27, the absence of ERAP1 reduces peptide recognition by HLA-B27-restricted immunodominant viral HLA–B27 epitope KK10-specific cytotoxic T-lymphocytes. Presence of an ankylosing spondylitis-protective variant of ERAP1, K528R, as compared to wild-type ERAP1, reduces the peptide recognition by KK10 cytotoxic T lymphocytes following transfection with extended KK10 minigenes Homo sapiens