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ProteomicsDysregulation of N-glycosylation by RPN1 knockout in spermatocytes induces male infertility via impaired mitochondrial function in mice
N-glycosylation protein modifications play a crucial regulatory role in numerous biological processes, although their contribution to male reproduction in mammals remains largely undefined. Here, we found that Ribophorin I (RPN1), a subunit of oligosaccharyltransferase complex, is indispensable for ...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-06 | PXD051379 | Pride
Rpn1  n-glycosylation  meiosis  spermatogenesis  fertility 
ProteomicsDysregulation of N-glycosylation by Rpn1 knockout in spermatocytes induces male infertility via endoplasmic reticulum stress in mice
N-glycosylation protein modification plays a crucial regulatory role in numerous biological processes, although their contribution to male reproduction in mammals remains largely undefined. Here, we found that Ribophorin I (RPN1), a subunit of oligosaccharyltransferase complex, is indispensable for ...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-07 | PXD056290 | Pride
Rpn1  n-glycosylation  meiosis  endoplasmic reticulum stress  fertility 
ProteomicsNovel recognition site for polyUb and UBL signals in Rpn1
Rpn1 is the largest proteasomal receptor for polyubiquitin and shuttle proteins contains one known binding site for polyubiquitin and shuttle proteins. We used a combination of NMR spectroscopy, photo-crosslinking, mass spectrometry, and mutagenesis,to confirm the presence of additional ubiquitin re...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2021-08-09 | PXD027128 | Pride
Uv-crosslinking Rpn1 Bpa Ubiquitin 
ProteomicsReversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function
The fundamental importance of the 26S proteasome in health and disease suggests that its function must be finely controlled, and yet our knowledge about proteasome regulation remains limited. Posttranslational modifications, especially phosphorylation, of proteasome subunits have been shown to impac...
ORGANISM(S): Homo Sapiens 
2019-12-08 | PXD016643 |
GenomicsHomo sapiens
RIP-seq for Rpn1
PRJDB17275 | ENA
UnknownRpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome.
Not available
S-EPMC3340268 | biostudies-literature
UnknownReversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function.
Not available
S-EPMC6955308 | biostudies-literature
UnknownCirc-SNX27 sponging miR-375/RPN1 axis contributes to hepatocellular carcinoma progression.
Not available
S-EPMC10316188 | biostudies-literature
UnknownPolyubiquitin and ubiquitin-like signals share common recognition sites on proteasomal subunit Rpn1.
Not available
S-EPMC8008175 | biostudies-literature
UnknownRpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome.
Not available
S-EPMC4980823 | biostudies-literature
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