Affinage

Showing DDRGK1 — UFBP1 is a alias.

DDRGK1

DDRGK domain-containing protein 1 · UniProt Q96HY6

Length
314 aa
Mass
35.6 kDa
Annotated
2026-06-09
29 papers in source corpus 21 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/8 claims corpus-supported (88%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DDRGK1 (UFBP1) is an endoplasmic reticulum membrane protein that serves as a core component and substrate adaptor of the UFM1 conjugation (ufmylation) system, governing ER homeostasis and the stability of multiple client proteins (PMID:21494687, PMID:28128204). Within a UFL1/UFBP1 complex it both transfers UFM1 and is itself ufmylated, and its own stability is maintained by UFL1, which protects it from proteasomal degradation (PMID:20228063). A recurrent theme across its targets is control of client protein turnover: DDRGK1 stabilizes the ER-stress sensor IRE1α by binding its kinase domain in a ufmylation-dependent manner, sustaining IRE1α-XBP1 signaling and suppressing the PERK-eIF2α-CHOP apoptotic arm (PMID:28128204, PMID:37781516). The same protective logic extends to the chondrogenic master regulator SOX9, whose ubiquitination DDRGK1 blocks to drive cartilage development (PMID:28263186), and to FASN and IP3R, which DDRGK1 stabilizes by competitively inhibiting their ubiquitination (PMID:41671397, PMID:42171880). Through these activities DDRGK1 controls embryonic development and hematopoiesis, where its loss elevates ER stress and represses erythroid transcription factors via ASC1-dependent promoter association (PMID:26544067), and promotes plasma cell development by restraining PERK (PMID:30842412). Site-specific ufmylation of DDRGK1 (K267/K268) is required for several functions including IRE1α stabilization, control of hepatic lipogenesis, and FASN-dependent adiposity (PMID:37781516, PMID:37660122, PMID:41671397), though this modification is dispensable for embryonic, cardiac, and intestinal homeostasis (PMID:37566002). The UFL1/UFBP1 complex additionally attenuates mTORC1 by directly engaging the mTOR/GβL complex (PMID:37131258), and DDRGK1 modulates autophagy and ER-phagy (PMID:33879777, PMID:38233375). Reported effects on NRF2 stability are conflicting, with evidence for both promoting (PMID:33219317) and inhibiting (PMID:36965071) its degradation.

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 2010 Medium

    Established DDRGK1 as a stable member of a UFL1 (RCAD)/CDK5RAP3 (C53/LZAP) protein complex and showed its abundance is set by UFL1-dependent protection from proteasomal degradation, defining the molecular context for its later adaptor roles.

    Evidence Co-IP, gel filtration, and ubiquitination assays with proteasome inhibition

    PMID:20228063

    Open questions at the time
    • Did not define the E3 ligase responsible for DDRGK1 ubiquitination
    • Did not connect complex assembly to ufmylation enzymology
  2. 2011 Medium

    Placed DDRGK1 at the ER as a UFM1-conjugation partner required to prevent ER-stress-induced apoptosis, linking the ufmylation machinery (UFM1, UFL1, UFBP1) to ER homeostasis.

    Evidence Immunofluorescence co-localization, reciprocal Co-IP, and siRNA knockdown with apoptosis readout in pancreatic beta cells

    PMID:21494687

    Open questions at the time
    • No molecular target of the protective effect identified
    • Mechanism connecting ufmylation to apoptosis suppression unresolved
  3. 2013 Low

    Proposed DDRGK1 regulates NF-κB signaling by controlling IκBα stability, extending its client-stabilization role to inflammatory transcription.

    Evidence Co-IP, NF-κB target microarray, and siRNA knockdown with proliferation/invasion assays

    PMID:23675531

    Open questions at the time
    • Single Co-IP without reciprocal validation for IκBα binding
    • Direction and mechanism of stability control not biochemically dissected
  4. 2015 High

    Demonstrated DDRGK1 is essential for embryonic development and hematopoiesis in vivo, tying ER-stress control to stem/progenitor survival and erythroid transcription factor expression.

    Evidence Germline and conditional KO mice, ChIP for ASC1 at GATA-1/KLF1 promoters, siRNA in K562 cells

    PMID:26544067

    Open questions at the time
    • How UFBP1 controls ASC1 promoter recruitment mechanistically unclear
    • Direct versus indirect regulation of GATA-1/KLF1 not fully separated
  5. 2017 High

    Defined the key mechanistic principle that DDRGK1 stabilizes IRE1α by binding its kinase domain in a ufmylation-dependent manner, balancing the IRE1α-XBP1 versus PERK-CHOP arms of the UPR.

    Evidence Domain-mapped Co-IP, siRNA knockdown, ufmylation mutant analysis, UPR pathway readouts

    PMID:28128204

    Open questions at the time
    • The E3 ligase degrading IRE1α in DDRGK1's absence not identified
    • Structural basis of kinase-domain recognition unresolved
  6. 2017 High

    Showed DDRGK1 directly binds and protects SOX9 from ubiquitination, establishing a developmental client and a genetic role in chondrogenesis confirmed by rescue.

    Evidence Co-IP, ubiquitination assay, zebrafish knockdown with sox9 rescue, Ddrgk1-/- mouse with SOX9/Col2a1 readouts

    PMID:28263186

    Open questions at the time
    • Whether SOX9 protection requires DDRGK1 ufmylation not established here
    • E3 ligase acting on SOX9 not identified
  7. 2018 Medium

    Reframed DDRGK1 as a broad interactome hub that, contrary to its IRE1α/SOX9 stabilizing role, can promote client ubiquitination by enhancing substrate-E3 ligase engagement.

    Evidence IP-MS interactome (~80 proteins), ubiquitination assays using ANT3 as model substrate

    PMID:29533670

    Open questions at the time
    • What determines whether DDRGK1 stabilizes versus degrades a client unresolved
    • Which E3 ligases are recruited not systematically mapped
  8. 2019 High

    Identified UFBP1 ufmylation at K267 as functionally required for immunoglobulin production and ER expansion in plasma cells, while showing it promotes plasma cell development by suppressing PERK in a feedback loop with IRE1α/XBP1.

    Evidence Conditional KO mice, K267R mutant, plasma cell differentiation and immunoglobulin assays

    PMID:30842412

    Open questions at the time
    • Downstream effectors of K267 ufmylation in ER expansion not defined
    • Distinction between K267 ufmylation-dependent and -independent functions partial
  9. 2020 Medium

    Reported UFBP1 promotes K48-linked ubiquitination and degradation of NRF2, suppressing antioxidant gene expression and sensitizing gastric cancer cells to cisplatin.

    Evidence SILAC proteomics, K48-linkage ubiquitination assay, knockdown/overexpression, ROS flow cytometry, xenografts

    PMID:33219317

    Open questions at the time
    • Directly contradicts later report of NRF2 stabilization (idx 9)
    • E3 ligase mediating NRF2 degradation not specified
  10. 2021 Medium

    Revealed a dual, opposing role of DDRGK1 in autophagy: it restrains mTOR to permit autophagy induction while being required for autophagosome-lysosome fusion and lysosomal function.

    Evidence Inducible conditional KO MEFs, autophagy flux and mTOR assays, lysosomal pH, Cathepsin D, v-ATPase analysis

    PMID:33879777

    Open questions at the time
    • Molecular link between DDRGK1 and lysosomal acidification machinery unknown
    • Whether mTOR and fusion effects are mechanistically connected unclear
  11. 2021 Low

    Proposed DDRGK1 binds Smad3 and suppresses its phosphorylation, limiting hepatic fibrosis through a TGF-β/Smad-restraining role distinct from its degradation functions.

    Evidence Endogenous Co-IP, conditional KO mice, overexpression, phospho-Smad2/3 analysis

    PMID:34307359

    Open questions at the time
    • Single endogenous Co-IP without reciprocal validation
    • Mechanism of selective Smad3 (not Smad2) phospho-suppression unresolved
  12. 2023 Medium

    Confirmed in vivo, with K268R knockin mice, that DDRGK1 ufmylation drives IRE1α ufmylation and protection from ubiquitin-mediated degradation in chondrocytes, validating the modification's physiological importance.

    Evidence Conditional KO and K268R knockin mice, UFMylation/ubiquitylation competitive assays, PERK/CHOP/Caspase3 analysis

    PMID:37781516

    Open questions at the time
    • How IRE1α ufmylation status determines its ubiquitination not biochemically resolved
    • Tissue-specificity of K268 requirement unclear
  13. 2023 Medium

    Showed the UFL1/UFBP1 complex directly binds the mTOR/GβL complex to attenuate mTORC1 activity, with loss driving hepatocellular carcinoma, providing a direct molecular basis for the earlier mTOR/autophagy phenotype.

    Evidence Co-IP of the complex, hepatocyte conditional KO mice, iTRAQ proteomics, HCC tumor models

    PMID:37131258

    Open questions at the time
    • Whether mTOR attenuation requires ufmylation activity unclear
    • Direct site of mTOR/GβL engagement not mapped
  14. 2023 Medium

    Reported the opposite of the 2020 NRF2 finding: DDRGK1 competitively binds KEAP1 to stabilize NRF2 and promote antioxidant responses, modulating chemosensitivity in osteosarcoma.

    Evidence Quantitative proteomics, competitive Co-IP, DDRGK1 KO, ROS measurement, xenografts

    PMID:36965071

    Open questions at the time
    • Directly contradicts idx 8 on the direction of NRF2 regulation
    • Context dependence (cancer type) of the opposing effects unresolved
  15. 2023 Medium

    Established that UFBP1 ufmylation at K267 alleviates ER-stress-driven hepatic lipogenesis, linking the modification to metabolic disease phenotypes via rescue with WT but not K267R protein.

    Evidence K267R rescue in vitro, HFD mouse model with WT vs K267R UFBP1, ER stress and lipid assays

    PMID:37660122

    Open questions at the time
    • Lipogenic effector downstream of K267 ufmylation not identified
    • Relationship to IRE1α/XBP1 axis in liver not dissected
  16. 2023 Medium

    Demonstrated that UFBP1 K268 ufmylation is dispensable for ER stress signaling, embryonic, cardiac, and intestinal homeostasis, sharpening the boundaries of where the modification is functionally required.

    Evidence K268R knockin mice, MEF ER stress assays, echocardiography, DSS colitis model

    PMID:37566002

    Open questions at the time
    • Why K268 ufmylation matters in some tissues (chondrocytes, adipose) but not others unresolved
    • Compensatory ufmylation sites not excluded
  17. 2024 Low

    Proposed DDRGK1-UFL1-mediated ER-phagy as a protective mechanism that mitigates ER stress and apoptosis in renal tubular cells.

    Evidence DDRGK1 overexpression in HK-2 cells, murine AKI models, ER-phagy flux assays

    PMID:38233375

    Open questions at the time
    • No direct mechanistic dissection of ER-phagy receptor function
    • Causal role of DDRGK1 versus correlation not separated
  18. 2024 Low

    Implicated DDRGK1 and the UFMylation machinery in suppressing Type I IFN during mycobacterial infection in macrophages.

    Evidence Genome-wide CRISPRi screen with siRNA validation, IFN-β ELISA, transcriptional profiling (preprint)

    Open questions at the time
    • Preprint, not peer-reviewed
    • Single functional readout; molecular target of IFN suppression not identified
  19. 2026 Medium

    Extended DDRGK1's client-stabilization role to FASN, IP3R, and to upstream regulation by XIAP, connecting ufmylation to lipogenesis/adiposity, mitochondrial calcium/bioenergetics, and ER-phagy-mediated cochlear protection.

    Evidence K268R knockin mice with HFD and FASN ubiquitination assay; Co-IP and ubiquitination assays for IP3R; XIAP-DDRGK1 Co-IP with ER-phagy and noise-exposure models

    PMID:41588674 PMID:41671397 PMID:42171880

    Open questions at the time
    • IP3R and XIAP findings are abstract/single-Co-IP level (Low confidence)
    • E3 ligases acting on FASN and IP3R not identified
    • Whether these stabilizations require DDRGK1 ufmylation not uniformly tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved what molecular feature determines whether DDRGK1 stabilizes a client (IRE1α, SOX9, FASN, IP3R) versus promotes its degradation (ANT3, NRF2 per idx 8), and the contradictory directionality of NRF2 regulation is unexplained.
  • No unifying biochemical model for substrate fate selection
  • E3 ligase recruitment specificity uncharacterized
  • Structural basis of client recognition unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 4 GO:0031386 protein tag activity 3
Localization
GO:0005783 endoplasmic reticulum 2
Pathway
R-HSA-392499 Metabolism of proteins 4 R-HSA-8953897 Cellular responses to stimuli 3 R-HSA-1266738 Developmental Biology 2 R-HSA-9612973 Autophagy 2 R-HSA-168256 Immune System 1
Partners
CDK5RAP3ERN1 (IRE1Α)FASNKEAP1MTORSOX9UFL1UFM1
Complex memberships
UFL1/UFBP1 (UFM1 E3 ligase) complexUFL1/UFBP1/CDK5RAP3 (C53/LZAP) complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2011 DDRGK1 (UFBP1) localizes to the endoplasmic reticulum in a UFBP1-dependent manner and interacts with UFM1. siRNA-mediated knockdown of Ufbp1 or Ufm1 enhances apoptosis upon ER stress in pancreatic beta cells, and silencing the E3 enzyme UFL1 produces the same outcome, indicating that UFM1-UFBP1 conjugation is required to prevent ER stress-induced apoptosis. Co-localization by immunofluorescence, co-immunoprecipitation, siRNA knockdown with apoptosis readout PloS one Medium 21494687
2010 DDRGK1 interacts with C53/LZAP (CDK5RAP3) and with RCAD (UFL1) as part of a large protein complex. RCAD knockdown leads to proteasome-mediated degradation of both C53/LZAP and DDRGK1, while RCAD overexpression attenuates their ubiquitination, indicating RCAD stabilizes DDRGK1 by protecting it from proteasomal degradation. Co-immunoprecipitation, gel filtration, proteasome inhibitor experiments, ubiquitination assays The Journal of biological chemistry Medium 20228063
2013 DDRGK1 interacts with IκBα and regulates its stability, thereby modulating NF-κB transcriptional activity. Depletion of DDRGK1 inhibits NF-κB target gene expression and reduces cell proliferation and invasion. Co-immunoprecipitation, microarray analysis of NF-κB targets, siRNA knockdown with proliferation/invasion assays PloS one Low 23675531
2017 DDRGK1 is an ER membrane protein that stabilizes the ER-stress sensor IRE1α by interacting with the kinase domain of IRE1α, protecting it from degradation. This interaction is dependent on DDRGK1's ufmylation modification. Depletion of DDRGK1 represses IRE1α-XBP1 signaling and activates the PERK-eIF2α-CHOP apoptotic pathway. Co-immunoprecipitation (DDRGK1 with IRE1α kinase domain), siRNA knockdown, ufmylation mutant analysis, UPR pathway readouts Nature communications High 28128204
2017 DDRGK1 directly binds SOX9 and inhibits its ubiquitination and proteasomal degradation. Loss of DDRGK1 in zebrafish and mouse models decreases SOX9 protein levels and causes defective chondrogenesis; overexpression of sox9 rescues the chondrogenic phenotype caused by ddrgk1 knockdown. Co-immunoprecipitation (DDRGK1-SOX9 binding), ubiquitination assay, zebrafish knockdown with genetic rescue, Ddrgk1-/- mouse model with SOX9/Col2a1 readouts The Journal of clinical investigation High 28263186
2015 DDRGK1 (UFBP1) is required for embryonic development and hematopoiesis. UFBP1 deficiency causes elevated ER stress, activation of UPR, and cell death in hematopoietic stem/progenitor cells. Additionally, UFBP1 loss suppresses expression of erythroid transcription factors GATA-1 and KLF1, and the transcriptional co-activator ASC1 associates with GATA-1 and Klf1 promoters in a UFBP1-dependent manner. Germline and conditional knockout mouse models, ChIP for ASC1 at promoters, siRNA knockdown of Uba5 and ASC1 in K562 cells, UPR/ER stress assays PLoS genetics High 26544067
2019 UFBP1 (DDRGK1) promotes plasma cell development by suppressing PERK activation, while the IRE1α/XBP1 axis upregulates UFBP1 expression. Structure-function analysis shows lysine 267 (the main ufmylation site) is required for immunoglobulin production and ER expansion in IRE1α-deficient plasmablasts but is dispensable for plasmablast development itself. Conditional knockout mice, UFBP1 K267R mutant knockin/overexpression, plasma cell differentiation assays, ER expansion measurements, immunoglobulin production assays Nature communications High 30842412
2018 UFBP1 interacts with approximately 80 proteins (identified by IP-MS) and promotes ubiquitination and degradation of interacting proteins by enhancing their interaction with cognate E3 ligases. Using ANT3 as a model substrate, UFBP1 was shown to enhance the ANT3-E3 ligase interaction, promoting ANT3 ubiquitination and proteasomal degradation. Co-immunoprecipitation, label-free quantitative proteomics (IP-MS), proteasome inhibitor assays, protein synthesis inhibition assays, ubiquitination assays Journal of proteome research Medium 29533670
2020 UFBP1 promotes K48-linked polyubiquitination and proteasomal degradation of NRF2, thereby suppressing NRF2-driven antioxidant gene expression (AKR1Cs) and enhancing cisplatin sensitivity in gastric cancer cells. SILAC quantitative proteomics, ubiquitination assay (K48-linkage specific), siRNA knockdown, overexpression, flow cytometry for ROS, in vivo xenograft experiments Oncogene Medium 33219317
2023 DDRGK1 competitively binds KEAP1 to inhibit KEAP1-mediated ubiquitination and proteasomal degradation of NRF2, stabilizing NRF2 and promoting antioxidant responses. DDRGK1 knockout reduces NRF2 stability, causes ROS accumulation, and enhances chemosensitivity to doxorubicin and etoposide in osteosarcoma. Quantitative proteomics, co-immunoprecipitation (DDRGK1-KEAP1 competitive binding), DDRGK1 knockout (genetic), ROS measurement, in vivo xenograft experiments Advanced science Medium 36965071
2021 DDRGK1 deficiency in MEFs has a dual effect on autophagy: it promotes autophagy induction by impairing mTOR signaling, while simultaneously blocking autophagosome-lysosome fusion. DDRGK1 loss is associated with suppressed lysosomal function including impaired Cathepsin D expression, aberrant lysosomal pH, and v-ATPase accumulation. Inducible conditional KO MEFs (4-OHT-driven CreERT2), autophagy flux assays, mTOR activity readouts, lysosomal pH measurement, Cathepsin D assays, v-ATPase analysis Cell death & disease Medium 33879777
2023 The UFL1/UFBP1 complex directly interacts with the mTOR/GβL complex and attenuates mTORC1 activity. Ablation of Ufl1 or Ufbp1 in hepatocytes dissociates them from the mTOR/GβL complex and activates mTOR signaling, driving hepatocellular carcinoma development. Co-immunoprecipitation (Ufl1/Ufbp1 with mTOR/GβL), hepatocyte-specific conditional KO mice, iTRAQ proteomics, HCC tumor models Journal of experimental & clinical cancer research Medium 37131258
2023 Loss of DDRGK1 decreases UFMylation of IRE1α and leads to increased ubiquitylation-mediated IRE1α degradation in chondrocytes, causing ER dysfunction and activating the PERK/CHOP/Caspase3 apoptosis pathway. DDRGK1 K268R-mutant mice confirm the importance of K268 UFMylation for IRE1α stability in vivo. Conditional KO mice (Col2a1-ERT Cre), DDRGK1 K268R knockin mice, UFMylation and ubiquitylation assays, PERK/CHOP/Caspase3 pathway analysis International journal of biological sciences Medium 37781516
2021 UFBP1 directly binds Smad3 (demonstrated by endogenous co-immunoprecipitation) and suppresses Smad3 phosphorylation. UFBP1 deficiency leads to increased Smad3 phosphorylation and nuclear translocation, without affecting Smad2 phosphorylation, contributing to hepatic fibrosis. Endogenous co-immunoprecipitation (UFBP1-Smad3), conditional KO mice, UFBP1 overexpression in HeLa cells, phospho-Smad2/3 analysis Frontiers in cell and developmental biology Low 34307359
2024 DDRGK1-UFL1-mediated ER-phagy mitigates ER stress and apoptosis in renal tubular epithelial cells. Overexpression of DDRGK1 in HK-2 cells enhances ER-phagy levels and ameliorates contrast-induced ER stress and apoptosis. DDRGK1 overexpression in HK-2 cells, four murine AKI models, ER-phagy flux assays, ER stress and apoptosis markers Cell death & disease Low 38233375
2023 Ufmylation on UFBP1 (at K267) is required for alleviating ER stress-dependent lipogenesis in hepatocytes. Wild-type UFBP1 but not UFBP1 K267R mutant rescues lipid accumulation caused by UFBP1 knockdown, and ufmylation on UFBP1 ameliorates hepatic steatosis, dyslipidemia, and insulin resistance in vivo. UFBP1 K267R knockin/rescue experiments in vitro, HFD mouse model with WT vs. K267R UFBP1, ER stress markers, lipid accumulation assays Cell death & disease Medium 37660122
2023 UFBP1 K268 ufmylation is dispensable for ER stress response in mouse embryonic fibroblasts, embryonic development, cardiac homeostasis, and intestinal homeostasis under DSS-induced colitis. The K268R knockin mutation reduces total ufmylated proteins without altering ER stress signaling or causing morphological abnormalities up to one year of age. UFBP1 K268R knockin mice, MEF ER stress assays, serial echocardiography, DSS-induced colitis model Cells Medium 37566002
2009 DDRGK1 (Dashurin/C20orf116) contains a C-terminal PCI domain. Cell compartment fractionation showed presence in peroxisomes/mitochondria, microsomes, cytosol, and nucleus. GFP-Dashurin fusion protein shuttles between cytosol and nucleus. Luciferase reporter assays showed 2-3 fold increase in promoter activity upon overexpression. Cell fractionation, GFP fusion protein live imaging, luciferase reporter assay Biochimica et biophysica acta Low 20036718
2026 XIAP binds to DDRGK1 and increases DDRGK1 protein stability, activating ER-phagy. Noise exposure reduces both XIAP and DDRGK1 protein levels in cochlear cells; gastrodin promotes XIAP expression, increasing DDRGK1 levels and activating ER-phagy to protect cochlear hair cells. Co-immunoprecipitation (XIAP-DDRGK1), DDRGK1 stability assays, ER-phagy flux assays, in vivo CBA/CaJ mouse noise exposure model Advanced science Low 41588674
2026 DDRGK1 acts as a UFMylation effector that stabilizes FASN by competitively inhibiting its ubiquitination. DDRGK1 K268R mutant mice show reduced FASN protein and are protected from HFD-induced obesity, with 12% reduced body weight and 18% decreased fat mass. DDRGK1 K268R knockin mice, HFD model, FASN ubiquitination competitive assay, single-nucleus RNA sequencing, lipidomics, in vitro adipocyte lipid droplet assays Advanced science Medium 41671397
2026 DDRGK1 directly interacts with and stabilizes IP3R (inositol trisphosphate receptor), preventing its ubiquitin-mediated degradation. DDRGK1 deficiency reduces IP3R protein levels, impairing mitochondrial calcium uptake and oxidative phosphorylation, and activating CHOP while suppressing PGC-1α-mediated mitochondrial biogenesis. Co-immunoprecipitation (DDRGK1-IP3R), ubiquitination assays, respirometry, ATP measurements, calcium uptake assays, CHOP/PGC-1α pathway analysis Molecular biology reports Low 42171880
2024 Depletion of DDRGK1 (along with UFL1 and UFM1) in human macrophages results in increased IFN-β production and secretion during Mycobacterium marinum and M. tuberculosis infection, indicating that UFMylation activity (including DDRGK1) is required to suppress Type I IFN signaling during mycobacterial infection. Genome-wide CRISPRi screen in human macrophages, siRNA depletion of DDRGK1, IFN-β ELISA, transcriptional profiling bioRxivpreprint Low

Source papers

Stage 0 corpus · 29 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect pancreatic beta cells from ER stress-induced apoptosis. PloS one 167 21494687
2015 UFBP1, a Key Component of the Ufm1 Conjugation System, Is Essential for Ufmylation-Mediated Regulation of Erythroid Development. PLoS genetics 150 26544067
2017 A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability. Nature communications 128 28128204
2010 A novel C53/LZAP-interacting protein regulates stability of C53/LZAP and DDRGK domain-containing Protein 1 (DDRGK1) and modulates NF-kappaB signaling. The Journal of biological chemistry 110 20228063
2019 Ufbp1 promotes plasma cell development and ER expansion by modulating distinct branches of UPR. Nature communications 97 30842412
2011 Genome-wide association study identified ITPA/DDRGK1 variants reflecting thrombocytopenia in pegylated interferon and ribavirin therapy for chronic hepatitis C. Human molecular genetics 74 21659334
2023 DDRGK1 Enhances Osteosarcoma Chemoresistance via Inhibiting KEAP1-Mediated NRF2 Ubiquitination. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 60 36965071
2017 Loss of DDRGK1 modulates SOX9 ubiquitination in spondyloepimetaphyseal dysplasia. The Journal of clinical investigation 60 28263186
2013 DDRGK1 regulates NF-κB activity by modulating IκBα stability. PloS one 44 23675531
2024 DDRGK1-mediated ER-phagy attenuates acute kidney injury through ER-stress and apoptosis. Cell death & disease 31 38233375
2023 Loss of Ufl1/Ufbp1 in hepatocytes promotes liver pathological damage and carcinogenesis through activating mTOR signaling. Journal of experimental & clinical cancer research : CR 30 37131258
2020 UFBP1, a key component in ufmylation, enhances drug sensitivity by promoting proteasomal degradation of oxidative stress-response transcription factor Nrf2. Oncogene 30 33219317
2023 Ufmylation on UFBP1 alleviates non-alcoholic fatty liver disease by modulating hepatic endoplasmic reticulum stress. Cell death & disease 26 37660122
2021 DDRGK1, a crucial player of ufmylation system, is indispensable for autophagic degradation by regulating lysosomal function. Cell death & disease 25 33879777
2018 Proteomic and Biochemical Analyses Reveal a Novel Mechanism for Promoting Protein Ubiquitination and Degradation by UFBP1, a Key Component of Ufmylation. Journal of proteome research 22 29533670
2009 Cloning and molecular characterization of Dashurin encoded by C20orf116, a PCI-domain containing protein. Biochimica et biophysica acta 19 20036718
2023 Loss of DDRGK1 impairs IRE1α UFMylation in spondyloepiphyseal dysplasia. International journal of biological sciences 13 37781516
2022 DDRGK1 is required for the proper development and maintenance of the growth plate cartilage. Human molecular genetics 13 35377455
2021 Ufbp1, a Key Player of Ufm1 Conjugation System, Protects Against Ketosis-Induced Liver Injury via Suppressing Smad3 Activation. Frontiers in cell and developmental biology 12 34307359
2024 Bombyx mori UFBP1 regulates apoptosis and promotes BmNPV proliferation by affecting the expression of ER chaperone BmBIP. International journal of biological macromolecules 9 39551318
2023 Ufmylation of UFBP1 Is Dispensable for Endoplasmic Reticulum Stress Response, Embryonic Development, and Cardiac and Intestinal Homeostasis. Cells 7 37566002
2022 A missense mutation in DDRGK1 gene associated to Shohat-type spondyloepimetaphyseal dysplasia: Two case reports and a review of literature. American journal of medical genetics. Part A 6 35670300
2016 DDRGK1 in urine indicative of tubular cell injury in intensive care patients with serious infections. Journal of nephropathology 5 27152292
2025 Bombyx mori UFBP1 regulates the IRE1α-SEC61α axis to facilitate BmNPV proliferation in silkworms. International journal of biological macromolecules 3 40555317
2025 UFBP1 Ameliorates Heat Stress-Induced Apoptosis via Mitochondria-Mediated Pathway in Bovine Mammary Epithelial Cells. Animals : an open access journal from MDPI 2 40362048
2026 XIAP Stabilizes DDRGK1 to Promote ER-Phagy and Protects Against Noise-Induced Hearing Loss. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 0 41588674
2026 Ufmylation-Deficient DDRGK1 Ameliorates Obesity by Inhibiting FASN-Mediated Adipocyte Lipogenesis. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 0 41671397
2026 DDRGK1 regulates muscle development by maintaining mitochondrial calcium homeostasis and oxidative phosphorylation via stabilizing IP3R. Molecular biology reports 0 42171880
2025 DDRGK1 preserves intervertebral disc development through ufmylation. Cellular and molecular life sciences : CMLS 0 41460352

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