+ |
oligopeptide | up-regulates quantity
precursor of
|
peptide antigen |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267863 |
|
|
Homo sapiens |
|
pmid |
sentence |
31810556 |
Within the phagosome, the internalized antigens are partially degraded by Cathepsin S and the GILT complex, a necessary step for further export to cytosol. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267770 |
|
|
Homo sapiens |
|
pmid |
sentence |
31810556 |
While peptides loaded onto MHC class I molecules are 8–11 amino acid residues long (a restriction based on the size and conformation of the peptide-binding groove of MHC class I molecules), peptides translocated by TAP can be significantly longer. These peptides will be trimmed to the correct length by ERAP-1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267866 |
|
|
Homo sapiens |
|
pmid |
sentence |
31810556 |
Within the phagosome, the internalized antigens are partially degraded by Cathepsin S and the GILT complex, a necessary step for further export to cytosol. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
26S Proteasome | up-regulates quantity
cleavage
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267768 |
|
|
Homo sapiens |
|
pmid |
sentence |
15571818 |
The proteasome system is the central proteolytic system of the eukaryotic cell [1] and plays an important role in the generation of MHC-class I peptides. The enzyme complex responsible for the selectivity of intracellular protein degradation is the 26S proteasome that degrades poly-ubiquitinated substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ERAP1 | down-regulates quantity
chemical modification
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267771 |
|
|
Homo sapiens |
|
pmid |
sentence |
31810556 |
While peptides loaded onto MHC class I molecules are 8–11 amino acid residues long (a restriction based on the size and conformation of the peptide-binding groove of MHC class I molecules), peptides translocated by TAP can be significantly longer. These peptides will be trimmed to the correct length by ERAP-1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NPEPPS | down-regulates quantity
chemical modification
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272467 |
|
|
Homo sapiens |
|
pmid |
sentence |
11062501 |
The proteasome generates exact major histocompatibility complex (MHC) class I ligands as well as NH2-terminal-extended precursor peptides| We performed in vitro peptide digests using recombinant PSA | PSA behaved exclusively as an aminopeptidase |BH and PSA act as complementary and redundant systems responsible for the final trimming of the correct NH2 terminus. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ERAP2 | down-regulates quantity
chemical modification
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272495 |
|
|
Homo sapiens |
|
pmid |
sentence |
15908954 |
The generation of many HLA class I peptides entails a final trimming step in the endoplasmic reticulum that, in humans, is accomplished by two 'candidate' aminopeptidases | We show here that one of these, ERAP1, was unable to remove several N-terminal amino acids that were trimmed efficiently by the second enzyme, ERAP2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IFI30 | down-regulates quantity
chemical modification
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267865 |
|
|
Homo sapiens |
|
pmid |
sentence |
31810556 |
Within the phagosome, the internalized antigens are partially degraded by Cathepsin S and the GILT complex, a necessary step for further export to cytosol. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TAP1 | down-regulates quantity
relocalization
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267778 |
|
|
Homo sapiens |
|
pmid |
sentence |
31810556 |
Following cytosolic proteolysis, antigenic peptides are recruited to the ER and translocated to its lumen by the Transporter associated with Antigen Processing (TAP). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AP-2/clathrin vescicle | up-regulates quantity
relocalization
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267861 |
|
|
Homo sapiens |
|
pmid |
sentence |
25720354 |
APCs cell surface receptors facilitate antigen entry into antigen-processing compartments through clathrin-mediated endocytosis. It is in these compartments that internalized antigen proteolysis and peptide–MHC class II complex formation takes place. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AP-3/clathrin vescicle | up-regulates quantity
relocalization
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267862 |
|
|
Homo sapiens |
|
pmid |
sentence |
25720354 |
APCs cell surface receptors facilitate antigen entry into antigen-processing compartments through clathrin-mediated endocytosis. It is in these compartments that internalized antigen proteolysis and peptide–MHC class II complex formation takes place. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTSS | down-regulates quantity
chemical modification
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267868 |
|
|
Homo sapiens |
|
pmid |
sentence |
31810556 |
Within the phagosome, the internalized antigens are partially degraded by Cathepsin S and the GILT complex, a necessary step for further export to cytosol. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AP-1/clathrin vescicle | up-regulates quantity
relocalization
|
oligopeptide |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267860 |
|
|
Homo sapiens |
|
pmid |
sentence |
25720354 |
APCs cell surface receptors facilitate antigen entry into antigen-processing compartments through clathrin-mediated endocytosis. It is in these compartments that internalized antigen proteolysis and peptide–MHC class II complex formation takes place. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |