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ProteomicsSystematic discovery of UFM1 receptors reveals a regulatory module in DNA repair directing non-homologous end-joining
As the most recently identified UBL, UFM1 is garnering increasing attention for its roles beyond its canonical functions at the endoplasmic reticulum. To address the challenge of defining UFM1 substrate-receptor relationships, we develop a fully functional, photo-crosslinkable UFM1 probe for recepto...
ORGANISM(S): Homo sapiens (Human) 
2026-06-25 | PXD069136 | Pride
Ufm1  ubiquitin-like proteins (ubls)  dna repair  dna double-strand breaks (dsbs)  non-homologous end-joining (nhej)  xrcc4  genetic code expansion  photo-crosslinking  proximity labelling 
ProteomicsIdentification of UFM1 candidate targets from mouse brain
Genetic variants that hinder post-translational protein modifications by the ubiquitin-like modifier UFM1 (UFMylation) cause encephalopathies. UFMylation regulates endoplasmic reticulum (ER) homeostasis, but how UFMylation-deficiencies cause selective neurological defects is unknown. In the framewor...
ORGANISM(S): Mus musculus (Mouse) 
2026-01-28 | PXD071267 | Pride
Gel electrophoresis Brain Affinity purification Mass spectrometry Encephalopathy Ubiquitin-like modifier Ufm1 
ProteomicsIdentify UFM1 targeted protein
we want to identify UFM1 target protein in human cells
ORGANISM(S): Homo sapiens (Human) 
2019-04-02 | PXD012729 | Pride
293t cell Ufm1 Human 
ProteomicsUFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER
Supporting MS data for paper (doi: 10.1038/s41586-024-07073-0) by DaRosa P.A., Penchev I. et al., titled "UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER". Index of MS supporting files uploaded: Related to Related to Fig. 1b, c (xb01004(UFM1), xb01005(SBP-UFM1): LFQ IP-MS (Un...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-12-22 | MSV000093721 | MassIVE
GenomicsEncephalopathy-linked UFM1 variants impede neuronal protein translation, development and function
Encephalopathy-linked UFM1 variants impede neuronal protein translation, development and function
PRJNA1273747 | ENA
ProteomicsHuman UFSP1 is an active protease that regulates UFM1 maturation and UFMylation
An essential first step in the posttranslational modification of proteins with UFM1, UFMylation, is the proteolytic cleavage of pro-UFM1 to expose a C-terminal glycine. Of the two UFM1-specific proteases (UFSPs) identified in humans, only UFSP2 is reported to be active since the annotated sequence o...
ORGANISM(S): Homo sapiens (Human) 
2022-08-22 | PXD035142 | Pride
Ribosome Ufm1 Endoplasmic reticulum (er) Cysteine protease Ubiquitin like modifier 
ProteomicsLC-MS/MS of co-immunoprecipitation of 3xFLAG-UFM1 from ribosomal pellet in control and upon anisomycin treatment
Clearance of arrested nascent polypeptides resulting from ribosomal stalling is essential for proteostasis. Stalled endoplasmic reticulum (ER)-bound ribosomes are marked by ubiquitin-fold modifier 1 (UFM1) on large ribosomal subunit protein RPL26, but the precise role of this process in ribosome-ass...
ORGANISM(S): Homo sapiens (Human) 
2026-03-23 | PXD071028 | Pride
Ufm1 Ufmylation Ribosome Anisomycin 
ProteomicsHuman UFSP1 is an active UFM1-specific protease
In order to confirm the translation initiation site of human UFSP1 (UFM1-specific protease 1), we sought to obtain direct evidence using mass spectrometry (MS) for peptide sequencing.
ORGANISM(S): Homo sapiens (Human) 
2022-04-08 | PXD033083 | Pride
Ufmylation  ufm1-specific protease  ufsp1  ufsp2 
TranscriptomicsEncephalopathy-linked UFM1 variants impede neuronal protein translation, development and function
Genetic variants that hinder post-translational protein modifications by UFM1, UFMylation, cause encephalopathies. UFMylation regulates endoplasmic reticulum (ER) homeostasis, but how UFMylation-deficiencies cause selective neurological defects is unknown. Using Ufm1 knock-out mice, we investigated ...
ORGANISM(S): Mus musculus 
2026-04-22 | GSE299278 | GEO
ProteomicsUFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER
Supporting MS data for paper (doi: 10.1038/s41586-024-07073-0) by DaRosa P.A., Penchev I. et al., titled "UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER". Index of MS supporting files uploaded: - Related to Fig. 1a and Extended Data Fig. 1a (AO3435-AO3440: TMT proteomics (Un...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-11-27 | MSV000093510 | MassIVE
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