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ProteomicsMouse TAPBPR functions as an MHC-I peptide exchange catalyst
Human TAPBPR is known to function as a Major Histocompatibility Complex class I (MHC-I) peptide exchange catalyst which shapes the peptide repertoire presented to immune cells. Never14theless, investigations characterizing TAPBPR from other species are limited. Here, we characterize mouse TAPBPR, ex...
ORGANISM(S): Mus musculus (Mouse) 
2026-03-23 | PXD069965 | Pride
Mouse Tapbpr Immunopeptidomics Mhc-i Lc-ms/ms 
ProteomicsMouse TAPBPR functions as an MHC-I peptide exchange catalyst
Human TAPBPR is known to function as a Major Histocompatibility Complex class I (MHC-I) peptide exchange catalyst which shapes the peptide repertoire presented to immune cells. Never14theless, investigations characterizing TAPBPR from other species are limited. Here, we characterize mouse TAPBPR, ex...
ORGANISM(S): Mus musculus (Mouse) 
2026-03-23 | PXD068540 | Pride
H-2kb Mouse tapbpr Peptide exchange H-2db Mhc-i Calnexin 
ProteomicsTAPBPR promotes editing of the HLA-B*44 peptide repertoire, increasing the presentation of peptides containing a C-terminal tryptophan
Major histocompatibility complex class I (MHC-I) molecules play a key part in the adaptive immune response through the presentation of antigens to CD8+ T cells. The high degree of polymorphism in MHC-I leads to significant variation in their dependence on components of the antigen processing and pre...
ORGANISM(S): Homo sapiens (Human) 
2025-10-24 | PXD063219 | Pride
GenomicsSites on TAPBPR that scaffold assembly of a MHC-I H chain with beta2m are important for TAPBPR chaperone activity
Sites on TAPBPR that scaffold assembly of a MHC-I H chain with beta2m are important for TAPBPR chaperone activity
PRJNA613093 | ENA
ProteomicsIdentification of novel HLA class I-restricted hepatitis B virus peptides and their modulation by peptide editor TAPBPR
Hepatitis B virus (HBV) is the leading cause of hepatocellular carcinoma and infections remain a substantial global health problem for which no curative therapy exists. As cytotoxic CD8+ T lymphocytes are the principal effectors of natural HBV resolution, there is considerable interest in discoverin...
ORGANISM(S): Homo sapiens (Human) 
2026-07-15 | PXD078020 | Pride
Immunopeptidomics Hla Tapbpr Mhc 
OtherSites on TAPBPR that scaffold assembly of a MHC-I H chain with beta2m are important for TAPBPR chaperone activity
TAP-binding protein-related (TAPBPR) facilitates the processing of nascent class I MHC (MHC-I) by (1, chaperone function) acting as a chaperone for misfolded or partially folded MHC-I substrates in the cell and (2, editing function) by catalyzing exchange of low affinity for high affinity antigenic ...
ORGANISM(S): Homo sapiens 
2020-03-18 | GSE147137 | GEO
UnknownTAPBPR isoforms exhibit altered association with MHC class I.
Not available
S-EPMC4008236 | biostudies-literature
GenomicsA deep mutational scan of the MHC class I-specific chaperone TAPBPR for sites important for peptide editing
A deep mutational scan of the MHC class I-specific chaperone TAPBPR for sites important for peptide editing
PRJNA905819 | ENA
OtherA deep mutational scan of the MHC class I-specific chaperone TAPBPR for sites important for peptide editing
TAP-binding protein-related (TAPBPR) is an endoplasmic reticulum-resident chaperone that facilitates class I MHC (MHC-I) processing and peptide loading. TAPBPR has (1) chaperone function to stabilize misfolded or partially folded nascent MHC-I substrates, and (2) editing function, in which it cataly...
ORGANISM(S): Homo sapiens 
2023-03-09 | GSE218828 | GEO
UnknownTAPBPR mediates peptide dissociation from MHC class I using a leucine lever.
Not available
S-EPMC6307860 | biostudies-literature
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