Affinage

UFSP2

Ufm1-specific protease 2 · UniProt Q9NUQ7

Length
469 aa
Mass
53.3 kDa
Annotated
2026-06-10
41 papers in source corpus 21 papers cited in narrative 21 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

UFSP2 is a papain-like cysteine protease that serves as the principal de-UFMylating enzyme of the cell, both maturing pro-UFM1 and removing UFM1 from conjugated substrates (PMID:17182609, PMID:35926457). It is a thiol protease that specifically processes the UFM1 C-terminal extension—and not ubiquitin, SUMO-1, or ISG15—through an active-site cysteine that can be covalently trapped with UFM1-based probes (PMID:17182609, PMID:35756382). Structurally, the enzyme comprises a C-terminal catalytic domain bearing a Cys294/Asp418/His420 triad and oxyanion-hole tyrosine, plus a novel N-terminal domain that recognizes the ER-resident substrate DDRGK1/UFBP1 (C20orf116) and recruits the enzyme to the endoplasmic reticulum, where it counteracts the UFL1/UFBP1 E3 machinery to set steady-state UFM1-conjugate levels (PMID:21228277, PMID:27926783). Through this deconjugating activity UFSP2 regulates the stability and activity of diverse substrates, including the ribosomal protein RPL26 (PMID:35926457), the coactivator ASC1 and estrogen receptor ERα (PMID:25219498, PMID:35680375), PD-L1 (PMID:36893266), and the pyruvate dehydrogenase E2 subunit DLAT at K118 (PMID:41890053). UFSP2 also functions at sites of DNA damage: it is recruited to double-strand breaks under ATM-phosphorylation and WIP1-phosphatase control to deufmylate histone H4 and suppress ATM activation, and its de-UFMylase activity modulates replication-fork protection and PARP-inhibitor sensitivity in BRCA1/2-deficient cells (PMID:36042814, PMID:38649452). Separately from proteolysis, UFSP2 acts catalytically-independently in GPCR biogenesis, forming an ER complex with ODR4 and C1orf27 that promotes receptor export from the ER (PMID:24603482, PMID:42088365). Loss-of-function mutations cause distinct human disorders depending on the affected domain: catalytic-domain mutations (p.Y290H, p.D426A) cause skeletal dysplasias including Beukes hip dysplasia and spondyloepimetaphyseal dysplasia, whereas an N-terminal-domain variant (p.V115E) underlies a neurodevelopmental presentation (PMID:26428751, PMID:28892125, PMID:33473208).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2006 High

    Established that UFSP2 is a dedicated protease for the UFM1 modifier system, distinguishing it from ubiquitin/SUMO/ISG15 proteases and defining its catalytic chemistry.

    Evidence In vitro protease assays with recombinant protein, active-site Cys→Ser mutagenesis, UFM1-vinylmethylester covalent labeling, and NEM inhibitor sensitivity

    PMID:17182609

    Open questions at the time
    • Cellular substrates beyond bulk UFM1 conjugates not yet identified
    • Domain organization and localization not resolved
  2. 2008 High

    Solved the catalytic fold and UFM1-binding mode for the UfSP family, defining a novel papain-like cysteine protease subfamily with an Asp-Pro-His configuration.

    Evidence X-ray crystallography of mouse UfSP1 at 1.7 Å, active-site mutagenesis, ITC and NMR epitope mapping of UFM1 binding

    PMID:18321862

    Open questions at the time
    • Structure is of UfSP1, not UFSP2
    • Does not address the second domain and substrate recognition specific to UFSP2
  3. 2011 High

    Showed that UFSP2's two-domain architecture couples catalysis to localization—the N-terminal domain recognizes DDRGK1/UFBP1 and targets the enzyme to the ER—and provided a structural basis for disease mutation Y290H.

    Evidence X-ray crystallography of mouse UfSP2 at 2.6 Å with domain deletion/mutation and subcellular localization analysis

    PMID:21228277

    Open questions at the time
    • How the N-terminal domain engages the broader ER E3 machinery not detailed
    • Full substrate range unknown
  4. 2014 High

    Identified physiological de-UFMylation substrates and a catalysis-independent function, showing UFSP2 controls ERα/ASC1 coactivation and that the ortholog mediates GPCR ER export without protease activity.

    Evidence Co-IP, knockdown, in vivo tumor models, and ChIP (ASC1/ERα); C. elegans genetic epistasis with catalytic-dead rescue and human Co-IP (ODR-4/GPCR maturation)

    PMID:24603482 PMID:25219498

    Open questions at the time
    • Mechanism by which catalytic-dead UFSP2 supports GPCR export unresolved
    • Generality of UFM1-independent role across receptor families unknown
  5. 2016 Medium

    Positioned UFSP2 as the dominant ER de-conjugase opposing the UFL1/UFBP1 E3, and clarified that the N-terminal MPN-like domain is the substrate/ER-targeting module.

    Evidence UFSP2 KO/knockdown with UFL1+UFBP1 overexpression and immunoblotting; C. elegans UfSP crystal structure with domain deletion and deufmylation/localization assays

    PMID:27240952 PMID:27926783

    Open questions at the time
    • Quantitative balance between conjugation and deconjugation in vivo not measured
    • MPN domain lacks metalloprotease activity; its precise recognition determinants unclear
  6. 2018 Medium

    Extended the genotype-phenotype map by linking another catalytic-residue mutation (D426A) to a distinct skeletal dysplasia.

    Evidence Exome sequencing with structural mapping of the variant to the active site and comparison to prior in vitro data

    PMID:28892125

    Open questions at the time
    • No new in vitro activity assay performed for D426A
    • Tissue-specific basis of skeletal phenotype unexplained
  7. 2021 Medium

    Showed that disrupting the N-terminal domain (V115E) impairs de-UFMylation through reduced protein abundance and produces a phenotype distinct from catalytic-domain skeletal dysplasias.

    Evidence Patient-fibroblast immunoblotting, wild-type UFSP2 reconstitution rescue, and structural domain mapping

    PMID:33473208

    Open questions at the time
    • Whether V115E destabilizes folding or only impairs localization not distinguished
    • Single lab/single family
  8. 2022 High

    Defined UFSP2's substrate selectivity and central role: it specifically deufmylates RPL26, is the dominant active de-UFMylase in living cells, and is required (with UFSP1) for UFM1 maturation.

    Evidence UFSP1/UFSP2 double-knockout cells with substrate-specific immunoblotting and reconstitution; UFM1 α-chloroacetyl activity-based probe labeling in cellulo

    PMID:35756382 PMID:35926457

    Open questions at the time
    • Division of labor between UFSP1 and UFSP2 in maturation incompletely mapped
    • Substrate-specificity determinants for RPL26 vs other targets unknown
  9. 2022 Medium

    Demonstrated that UFSP2 tunes substrate stability by removing UFM1 marks that antagonize ubiquitination, exemplified by ERα stabilization and transactivity.

    Evidence UFSP2 knockdown, ERα K171R/K180R mutagenesis, ubiquitination, luciferase transactivation, and colony-formation assays

    PMID:35680375

    Open questions at the time
    • Crosstalk geometry between UFMylation and ubiquitination sites not structurally resolved
    • Single lab
  10. 2022 Medium

    Established a regulated DNA-damage function: UFSP2 is recruited to double-strand breaks under ATM/WIP1 phosphorylation control to deufmylate histone H4 and dampen ATM activation.

    Evidence Reciprocal Co-IP with MRN, irradiation-induced foci, phosphorylation assays, WIP1 perturbation, and ATM kinase assays

    PMID:36042814

    Open questions at the time
    • Direct H4 deufmylation in chromatin context not structurally validated
    • Single lab
  11. 2023 Medium

    Connected UFSP2 to immune evasion by showing its inhibition raises PD-L1 UFMylation, destabilizing PD-L1 and enhancing anti-tumor immunity.

    Evidence UFMylation and stability assays, UFSP2 covalent inhibitor, and in vitro/in vivo immune-killing assays with PD-1 blockade

    PMID:36893266

    Open questions at the time
    • Whether UFSP2 directly deufmylates PD-L1 vs acts on the pathway not pinned down
    • Single lab
  12. 2024 Medium

    Linked UFSP2 de-UFMylase activity to replication-fork protection and PARP-inhibitor resistance via reversal of PTIP UFMylation, and to stress-pathway integrity in neurons.

    Evidence UFSP2 overexpression with DNA fiber fork-degradation and PARPi resistance assays plus UFL1-knockdown epistasis; CRISPR UFSP2 KO neurons with DDR and UPR readouts

    PMID:38649452 PMID:39696466

    Open questions at the time
    • Direct PTIP deufmylation by UFSP2 not biochemically reconstituted
    • Neuronal stress-pathway link is phenotypic, not mechanistic
  13. 2026 Medium

    Resolved the catalysis-independent ER role mechanistically and revealed a mitochondrial-metabolic axis, identifying C1orf27 as an ER recruiter for GPCR export and DLAT-K118 as a UFMylation substrate controlling PDH activity.

    Evidence Co-IP and catalytic-mutant rescue with GPCR ER-export assays (C1orf27); quantitative proteomics, K118R mutagenesis, PDH activity and Seahorse assays in UFSP2-deficient cells (DLAT, preprint)

    PMID:41890053 PMID:42088365

    Open questions at the time
    • DLAT findings are from a preprint, single lab
    • How UFSP2 partitions between ER, nucleus, and mitochondrial-substrate compartments is unclear
  14. 2026 Medium

    Defined a structural limit of UFSP2 activity: it cannot efficiently cleave H4K31-UFM1 within the nucleosome due to steric occlusion of the isopeptide bond.

    Evidence Cryo-EM of H4K31UFM1-nucleosome with in vitro deufmylation assays using chemoenzymatically synthesized ufmylated histones

    PMID:41964563

    Open questions at the time
    • Reconciliation with prior H4 deufmylation at DSBs unresolved
    • Whether accessory factors relieve steric hindrance in cells unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How UFSP2 is spatially and temporally partitioned among its ER, DNA-damage, and metabolic functions—and what determines substrate choice and the switch between catalytic and non-catalytic roles—remains unresolved.
  • No unified model of compartment-specific recruitment
  • Substrate-specificity code for the protease undefined
  • Mechanism of catalysis-independent GPCR function not structurally explained

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 3 GO:0016787 hydrolase activity 2 GO:0140098 catalytic activity, acting on RNA 2
Localization
GO:0005783 endoplasmic reticulum 3 GO:0005634 nucleus 1 GO:0005739 mitochondrion 1
Pathway
GO:0140096 catalytic activity, acting on a protein 1
Partners
ASC1C1ORF27DDRGK1ODR4RPL26UFL1
Complex memberships
MRN complex (transient interaction)UFSP2–C1orf27–GPCR ER export complex

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2006 UFSP2 (and UFSP1) are novel thiol proteases that specifically process the C-terminal extension of UFM1 but not ubiquitin, SUMO-1, or ISG15. The active-site Cys residue is essential: replacement of conserved Cys with Ser abolishes activity, and UFSP2 can be covalently labeled with UFM1-vinylmethylester. Both enzymes are sensitive to sulfhydryl-blocking agents (e.g., N-ethylmaleimide) and can release UFM1 from UFM1-conjugated cellular proteins. In vitro protease activity assays with recombinant protein, active-site Cys→Ser mutagenesis, covalent labeling with UFM1-vinylmethylester, inhibitor (NEM) sensitivity assays The Journal of biological chemistry High 17182609
2008 The crystal structure of mouse UfSP1 at 1.7 Å reveals a novel cysteine protease with a papain-like fold; the catalytic triad is Cys53, Asp175, His177, with Tyr41 forming the oxyanion hole. The Asp-Pro-His configuration defines a new subfamily of cysteine proteases. Mutagenesis of active-site residues confirms their catalytic roles. ITC shows UFM1 binds UfSP1 with KD ≈ 1.6 μM; NMR shows the β3–α2 loop and C-terminal region of UFM1 are involved in binding. X-ray crystallography (1.7 Å), active-site mutagenesis, isothermal titration calorimetry, NMR The Journal of biological chemistry High 18321862
2011 Crystal structure of mouse UfSP2 at 2.6 Å reveals two domains: a C-terminal catalytic domain (cysteine protease with Cys294, Asp418, His420, Tyr282, and a regulatory loop) and a novel N-terminal domain. The N-terminal domain is required for recognition of the cellular substrate C20orf116 (DDRGK1/UFBP1) and for recruitment of UfSP2 to the endoplasmic reticulum where C20orf116 localizes. The BHD-associated mutation Y290H (equivalent position) abolishes catalytic activity, providing structural basis for disease. X-ray crystallography (2.6 Å), active-site mutagenesis, subcellular localization experiments, domain deletion/mutation analysis The Journal of biological chemistry High 21228277
2014 In the absence of estradiol (E2), UFSP2 binds the nuclear receptor coactivator ASC1 and maintains it in a non-UFMylated state. E2 induces ERα binding to ASC1, which displaces UFSP2, allowing polyufmylation of ASC1. UFSP2 knockdown promotes ERα-mediated tumor formation in vivo, an effect abrogatable by tamoxifen. Co-immunoprecipitation, knockdown (siRNA/shRNA), in vivo tumor formation assays, promoter ChIP, reconstitution experiments Molecular cell High 25219498
2014 In C. elegans, ODR-8/UfSP2 (the ortholog of UFSP2) and ODR-4 physically interact at the ER membrane in chemosensory neurons and together promote GPCR (ODR-10) maturation/export from the ER. This function is independent of UfSP2 protease activity: catalytically dead ODR-8/UfSP2 mutants rescue all odr-8 phenotypes. Human ODR4 and UFSP2 also physically interact, suggesting evolutionary conservation. Deletion of C. elegans ufm-1 does not affect chemoreceptor trafficking, demonstrating a UFM1-independent role. Genetic epistasis (C. elegans mutants), co-immunoprecipitation (human proteins), rescue experiments with catalytic mutants, GPCR localization assays PLoS genetics High 24603482
2015 A UFSP2 missense mutation p.Tyr290His (c.868T>C) segregates with Beukes hip dysplasia in all 17 affected family members. In vitro functional assays with purified recombinant wild-type and mutant UFSP2 demonstrate that the Y290H substitution abolishes UFSP2-mediated C-terminal cleavage of UFM1, establishing loss of proteolytic function as the disease mechanism. In vitro protease activity assay with recombinant wild-type and p.Y290H UFSP2, linkage analysis, Sanger sequencing South African medical journal High 26428751
2016 In the absence of UFSP2, ectopic co-expression of E3 components UFL1 and UFBP1 dramatically increases UFM1-conjugate formation at the ER, establishing UFSP2 as the primary deconjugating enzyme controlling UFM1 modification levels at the ER. UFSP2 knockout/knockdown combined with UFL1+UFBP1 overexpression, immunoblotting for UFM1 conjugates, subcellular fractionation FEBS letters Medium 27926783
2016 The C. elegans UfSP crystal structure reveals an N-terminal MPN domain (136 residues extra vs. UfSP2) that lacks metalloprotease activity but is required for recognition and deufmylation of the substrate UfBP1, and also for ER localization of cUfSP. X-ray crystallography, domain deletion mutagenesis, substrate deufmylation assay, subcellular localization Biochemical and biophysical research communications High 27240952
2018 A novel UFSP2 heterozygous missense mutation p.D426A (c.1277A>C) causes spondyloepimetaphyseal dysplasia. Asp426 is a catalytic residue in the active site, and the mutation is predicted (and consistent with prior in vitro data for related mutations) to inactivate UFSP2 proteolytic activity, extending the genotype-phenotype relationship to different skeletal dysplasia presentations. Exome sequencing, structural mapping of mutant to catalytic site, comparison to prior in vitro functional data Clinical genetics Medium 28892125
2021 A homozygous UFSP2 variant p.V115E reduces UFSP2 protein abundance and increases UFMylated targets in patient-derived fibroblasts, indicating impaired de-UFMylation. Reconstitution of patient-derived fibroblasts with wild-type UFSP2 reduces UFMylation marks. Structural analysis shows V115 localizes to the N-terminal domain, distinct from catalytic-domain mutations causing skeletal dysplasia. Immunoblotting of patient fibroblasts, wild-type UFSP2 reconstitution rescue experiment, structural domain mapping Genetics in medicine Medium 33473208
2022 Human UFSP2, but not UFSP1, specifically removes UFM1 from the ribosomal subunit RPL26. UFSP2 is also the primary protease for UFM1 maturation, though UFSP1 (translated from a non-canonical start site) acts earlier in the pathway. Cells lacking both UFSPs show complete loss of UFMylation due to absence of mature UFM1. UFSP1/UFSP2 double-knockout cells, immunoblotting for UFM1 maturation and RPL26 UFMylation, reconstitution experiments, biochemical fractionation Cell reports High 35926457
2022 UFMylation of ERα at Lys171 and Lys180 promotes ERα stability by inhibiting its ubiquitination; UFSP2 knockdown (which elevates UFMylation) dramatically increases ERα stability, while the ufmylation-deficient ERα 2KR mutant is destabilized and shows abrogated E2-induced transactivity and downstream gene expression. UFSP2 knockdown, ERα K171R/K180R mutagenesis, ubiquitination assay, luciferase transactivation assay, colony formation Molecules and cells Medium 35680375
2022 A UFM1 α-chloroacetyl activity-based probe selectively and covalently modifies the active-site cysteine of UFSP2 in cellulo, demonstrating that UFSP2 is the dominant active de-UFMylase accessible in living cells. Chemical biology/activity-based protein profiling with UFM1 electrophilic probes in cell lysates and living cells ACS central science Medium 35756382
2022 UfSP2 binds to the MRN complex in the absence of DNA double-strand breaks (DSBs). After irradiation, ATM phosphorylates UfSP2, causing its dissociation from MRN. WIP1 phosphatase removes this phosphorylation, allowing UfSP2 recruitment to DSBs where it deufmylates histone H4 and suppresses ATM activation in a negative-feedback manner. Co-immunoprecipitation, irradiation-induced foci formation assays, phosphorylation assays, WIP1 inhibition/knockdown, ATM kinase assay Genome instability & disease Medium 36042814
2023 PD-L1 is a UFMylation substrate; UFMylation destabilizes PD-L1 by synergizing with its ubiquitination. UFSP2 inhibition (via a covalent inhibitor) promotes PD-L1 UFMylation and enhances anti-tumor immunity in combination with PD-1 blockade. UFMylation assay, PD-L1 stability assays, UFSP2 covalent inhibitor, in vitro and in vivo immune killing assays, immunoprecipitation Proceedings of the National Academy of Sciences of the United States of America Medium 36893266
2024 Overexpression of UFSP2 (de-UFMylase) protects nascent DNA strands from degradation and confers resistance to PARP inhibitors in BRCA1/2-deficient cells, by reversing PTIP UFMylation at K148 that would otherwise promote MRE11 recruitment and fork degradation. UFSP2 overexpression, fork degradation assay (DNA fiber), PARP inhibitor resistance assay, genetic epistasis with UFL1 knockdown Nature chemical biology Medium 38649452
2024 In UFSP2 knockout neurons, the DNA damage response and unfolded protein response are perturbed, linking UFSP2-mediated de-UFMylation to these cellular stress pathways. CRISPR-Cas9 UFSP2 knockout in gene-edited neurons, functional assays for DNA damage response and UPR Molecular neurodegeneration Medium 39696466
2026 UFSP2 interacts with the ER-anchored protein C1orf27, which recruits UFSP2 to the ER. UFSP2 protease activity is dispensable for ER recruitment but required for ER export of GPCRs. UFSP2, C1orf27, and cargo GPCRs form a multi-protein complex at the ER, and GPCR interaction with C1orf27 is required for ER export. Co-immunoprecipitation, catalytic mutant rescue experiments, GPCR ER-export assays, structural analysis, subcellular localization iScience Medium 42088365
2026 UFSP2 deficiency leads to accumulation of UFMylated mitochondrial ribosome, ETC, and pyruvate dehydrogenase (PDH) complex components. DLAT (E2 subunit of PDH) is a direct UFMylation substrate at K118; K118R mutation abolishes DLAT UFMylation and reduces pyruvate oxidation, establishing that UFMylation activates PDH and that UFSP2 negatively regulates this modification. Quantitative proteomics in UFSP2-deficient cells, site-directed mutagenesis (K118R), PDH enzymatic activity assay, glucose oxidation/TCA flux assays, mitochondrial respiration (Seahorse) bioRxivpreprint Medium 41890053
2026 Cryo-EM analysis and biochemical assays with synthetic ufmylated histones (H4K31UFM1) show that neither UFSP1 nor UFSP2 can efficiently cleave H4 UFMylation at K31 in the nucleosome context, likely due to steric hindrance imposed by the nucleosome around the isopeptide bond. Cryo-EM structure of H4K31UFM1-nucleosome, in vitro deufmylation assay with recombinant UFSP1 and UFSP2, chemoenzymatic synthesis of ufmylated histones ACS chemical biology Medium 41964563
2025 UFM1 signaling promotes NHEJ by UFMylating Ku70; XRCC4 engages UFMylated Ku70 via a non-canonical UFM1-binding region (identified by NMR and photo-crosslinkable UFM1 probe) to promote chromatin assembly of NHEJ factors. UFSP2 depletion (which elevates UFMylation) was used to demonstrate that perturbation of UFM1 signaling impairs these DSB-repair processes. Proximity-dependent proteomics, photo-crosslinkable UFM1 probe, NMR, UFSP2 depletion, NHEJ reporter assay, patient-derived fibroblasts bioRxivpreprint Medium bio_10.1101_2025.06.16.659844

Source papers

Stage 0 corpus · 41 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 Modification of ASC1 by UFM1 is crucial for ERα transactivation and breast cancer development. Molecular cell 186 25219498
2006 Two novel ubiquitin-fold modifier 1 (Ufm1)-specific proteases, UfSP1 and UfSP2. The Journal of biological chemistry 172 17182609
2015 Novel genetic causes for cerebral visual impairment. European journal of human genetics : EJHG 131 26350515
2023 Dysregulation of PD-L1 by UFMylation imparts tumor immune evasion and identified as a potential therapeutic target. Proceedings of the National Academy of Sciences of the United States of America 61 36893266
2011 Structure of ubiquitin-fold modifier 1-specific protease UfSP2. The Journal of biological chemistry 60 21228277
2022 Human UFSP1 is an active protease that regulates UFM1 maturation and UFMylation. Cell reports 59 35926457
2015 Identification of a mutation in the ubiquitin-fold modifier 1-specific peptidase 2 gene, UFSP2, in an extended South African family with Beukes hip dysplasia. South African medical journal = Suid-Afrikaanse tydskrif vir geneeskunde 57 26428751
2008 Structural basis for Ufm1 processing by UfSP1. The Journal of biological chemistry 50 18321862
2014 An ER complex of ODR-4 and ODR-8/Ufm1 specific protease 2 promotes GPCR maturation by a Ufm1-independent mechanism. PLoS genetics 46 24603482
2018 Novel spondyloepimetaphyseal dysplasia due to UFSP2 gene mutation. Clinical genetics 40 28892125
2016 A novel approach to assess the ubiquitin-fold modifier 1-system in cells. FEBS letters 36 27926783
2024 UFL1 triggers replication fork degradation by MRE11 in BRCA1/2-deficient cells. Nature chemical biology 27 38649452
2024 VCP/p97 UFMylation stabilizes BECN1 and facilitates the initiation of autophagy. Autophagy 27 38762759
2021 A pathogenic UFSP2 variant in an autosomal recessive form of pediatric neurodevelopmental anomalies and epilepsy. Genetics in medicine : official journal of the American College of Medical Genetics 27 33473208
2020 UFSP2-related spondyloepimetaphyseal dysplasia: A confirmatory report. European journal of medical genetics 25 32755715
2022 Modification of ERα by UFM1 Increases Its Stability and Transactivity for Breast Cancer Development. Molecules and cells 24 35680375
2022 Facile Preparation of UFMylation Activity-Based Probes by Chemoselective Installation of Electrophiles at the C-Terminus of Recombinant UFM1. ACS central science 20 35756382
2022 Developmental dysplasia of the hip: A systematic review of susceptibility genes and epigenetics. Gene 15 36435507
2024 The UFMylation pathway is impaired in Alzheimer's disease. Molecular neurodegeneration 13 39696466
2011 Identification of a novel locus for autosomal dominant primary open angle glaucoma on 4q35.1-q35.2. Investigative ophthalmology & visual science 11 21896847
2023 Proximity Proteomics and Biochemical Analysis Reveal a Noncanonical Function for UFM1-Specific Protease 1 in the p62 Body Formation. Journal of proteome research 10 37285312
2022 Dynamic recruitment of UFM1-specific peptidase 2 to the DNA double-strand breaks regulated by WIP1. Genome instability & disease 10 36042814
2016 The MPN domain of Caenorhabditis elegans UfSP modulates both substrate recognition and deufmylation activity. Biochemical and biophysical research communications 10 27240952
2024 Genetic heterogeneity in epilepsy and comorbidities: insights from Pakistani families. BMC neurology 5 38783254
2025 Genetic aetiologies in relation to response to the ketogenic diet in 226 children with epilepsy. Brain communications 4 40290421
2024 Systematic Analysis of UFMylation Family Genes in Tissues of Mice with Metabolic Dysfunction-Associated Steatotic Liver Disease. Genes 4 39858578
2022 Nontraditional translation is the key to UFMylation and beyond. The Journal of biological chemistry 4 36037969
2008 Comparative FISH-mapping of twelve loci in river buffalo and sheep chromosomes: comparison with HSA8p and HSA4q. Cytogenetic and genome research 4 18253036
2025 Succinate-mediated Ufsp2 transcription promotes high glucose-stimulated pyroptosis in rat retinal Müller cells by activating NLRP3 inflammasome. Biochemical and biophysical research communications 3 40946554
2024 The UFMylation pathway is impaired in Alzheimer's disease. bioRxiv : the preprint server for biology 3 38903110
2024 Mithramycin targets head and neck cancer stem cells by inhibiting Sp1 and UFMylation. Cancer cell international 3 39702263
2021 The UFSP2/UFMylation Pathway Is Involved in Silica-Induced Pulmonary Injury. DNA and cell biology 3 33600261
2026 Optimization of protein UFMylation modification method and its application in substrate identification in human cells. The Journal of biological chemistry 1 41759738
2026 UFMylation: Biological mechanisms, functions, and clinical implications. Journal of genetics and genomics = Yi chuan xue bao 0 41713676
2026 Studies on intellectual disability identify variants in established genes as well as confirm candidature of new genes. Scientific reports 0 41714691
2026 The UFM1 Conjugation System: A Master Regulator of Cellular Stress Surveillance in Human Disease. Biology 0 41823810
2026 UFMylation of Pyruvate Dehydrogenase Regulates Mitochondrial Metabolism. bioRxiv : the preprint server for biology 0 41890053
2026 Expedient Chemical Synthesis of Ufmylated Histones Using Chemoenzymatic C-Terminal Hydrazinolysis of Ubiquitin-Fold Modifier 1. ACS chemical biology 0 41964563
2026 The UFSP2-C1orf27 complex positions nascent GPCRs to the ufmylation system for ER export control. iScience 0 42088365
2025 Identification of Endoplasmic Reticulum Stress-Related Genes in Osteoporosis Pathogenesis. Mediators of inflammation 0 40918403
2025 Comprehensive Analysis of Hub Telomere-Related Genes and Synovial Immune Characteristics in Osteoarthritis. Folia biologica 0 41165157

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