Affinage

ADRM1

Proteasomal ubiquitin receptor ADRM1 · UniProt Q16186

Length
407 aa
Mass
42.2 kDa
Annotated
2026-04-28
94 papers in source corpus 29 papers cited in narrative 30 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ADRM1 (hRpn13) is a stoichiometric 19S proteasome subunit that functions as a ubiquitin receptor and scaffold for deubiquitination at the proteasome, coupling substrate recognition to ubiquitin chain processing. Its N-terminal Pru domain docks onto the C-terminus of RPN2/PSMD1 and simultaneously recognizes K48-linked polyubiquitin chains through bivalent contacts with proximal and distal ubiquitin moieties, while its C-terminal DEUBAD domain recruits and allosterically activates UCH37/UCHL5 by disrupting UCH37 autoinhibitory oligomerization (PMID:18497817, PMID:16906146, PMID:25702870, PMID:24752541, PMID:30962947). ADRM1 functions redundantly with RPN10 as proteasomal ubiquitin receptors; simultaneous loss of both in mouse liver causes massive ubiquitin-conjugate accumulation and organ failure, and its autoubiquitination by proteasome-associated Ube3c under proteotoxic stress serves as a feedback mechanism to reduce substrate engagement (PMID:26222436, PMID:24811749). Beyond canonical proteasomal proteolysis, ADRM1 participates in MHC class I antigen processing, parkin recruitment during mitophagy, and DNA double-strand break resection control, where its CRL4-WDR70-mediated removal from a proteasome variant permits MRE11/EXO1 nuclease activity (PMID:26903513, PMID:25666615, PMID:37815873).

Mechanistic history

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

    Establishing ADRM1 as a bona fide stoichiometric proteasome subunit answered whether it was a transient interactor or an integral 19S component, and revealed it as the anchor for deubiquitinase UCH37.

    Evidence Co-IP, native PAGE, gel filtration, and in vitro DUB assays in reconstituted subcomplexes and human cells

    PMID:16815440 PMID:16906146 PMID:17139257

    Open questions at the time
    • How ADRM1 is incorporated during proteasome assembly was not addressed
    • Whether ADRM1 directly binds ubiquitin was unknown at this stage
  2. 2008 High

    Identifying ADRM1 as a direct ubiquitin receptor via its Pru domain resolved how ubiquitinated substrates are recognized at the proteasome beyond RPN10, and genetic epistasis in yeast established functional redundancy between the two receptors.

    Evidence ITC, NMR, and yeast double-mutant synthetic lethality

    PMID:18497817

    Open questions at the time
    • Structural basis for polyubiquitin chain linkage selectivity was not yet determined
    • How Pru domain simultaneously accommodates RPN2 docking and ubiquitin binding was unclear
  3. 2010 Medium

    Mouse knockout studies revealed that Rpn13 loss produces tissue-specific rather than globally lethal phenotypes (unlike UCH37 deletion), establishing that Rpn13 is dispensable for viability but critical for gametogenesis and specific tissues.

    Evidence Whole-body Rpn13 and Uch37 knockout mice with tissue proteasome activity profiling

    PMID:21048919

    Open questions at the time
    • Why certain tissues (testes, brain) are selectively vulnerable to Rpn13 loss is unexplained
    • Compensatory mechanisms by RPN10 or shuttle receptors in surviving tissues were not dissected
  4. 2010 Medium

    Linking the Rpn13/UCH37 axis to specific substrate degradation (iNOS, IκB-α) and to transcriptional regulation of RPN13 by ΔNp63α established that the receptor can direct selective proteolysis with pathway-level consequences for NF-κB signaling.

    Evidence siRNA knockdown, co-IP, ChIP on RPN13 promoter, substrate degradation assays

    PMID:20634424 PMID:20959455

    Open questions at the time
    • Whether Rpn13/UCH37 selectivity for iNOS/IκB-α reflects direct substrate recognition or indirect effects was not resolved
    • Generality of transcriptional regulation of RPN13 expression beyond the cisplatin/ΔNp63α axis is unknown
  5. 2014 High

    Demonstration that only one of two 19S caps in double-capped 26S proteasomes contains Rpn13 established intrinsic structural asymmetry, raising the possibility that the two caps have distinct substrate-processing capabilities.

    Evidence AQUA mass spectrometry and biochemical fractionation in yeast and mammals

    PMID:24429290

    Open questions at the time
    • Functional consequences of this asymmetry for substrate selection and processing are unknown
    • What determines which cap receives Rpn13 is not established
  6. 2014 High

    Discovery of Rpn13 autoubiquitination by proteasome-associated Ube3c under proteotoxic stress revealed a feedback mechanism that reduces the proteasome's ability to capture new ubiquitinated substrates when proteolysis is impaired.

    Evidence In vitro ubiquitination with purified proteasomes, mass spectrometry, proteasome inhibitor treatments in cells

    PMID:24811749

    Open questions at the time
    • How autoubiquitinated Rpn13 is subsequently resolved (deubiquitinated or degraded) is unclear
    • Whether this feedback operates physiologically outside of inhibitor treatment is not demonstrated
  7. 2014 High

    Structural and biophysical dissection of how Rpn13 disrupts UCH37 autoinhibitory oligomers into active 1:1 complexes resolved the allosteric activation mechanism, explaining how deubiquitination is spatially coupled to substrate recognition.

    Evidence Mutagenesis, NMR, SAXS, FRET, and in vitro DUB assays

    PMID:24752541

    Open questions at the time
    • How the Rpn13–UCH37 complex coordinates with other proteasomal DUBs (Rpn11/USP14) during substrate processing was not addressed
  8. 2015 High

    Crystal structures of the DEUBAD–UCH37 complex revealed the molecular basis for Rpn13-mediated activation versus INO80G-mediated inhibition of the same enzyme, establishing a paradigm of DEUBAD-domain molecular mimicry.

    Evidence Crystal structures with mutagenesis and activity assays

    PMID:25702870

    Open questions at the time
    • How the switch between activating (Rpn13) and inhibiting (INO80G) DEUBAD contexts is regulated in vivo is not known
  9. 2015 High

    In vivo double-knockout of Rpn13 and Rpn10 in mouse liver proved their functional redundancy as the essential proteasomal ubiquitin receptors and showed that UBL-UBA shuttle proteins require at least one intrinsic receptor for proteasome docking.

    Evidence Liver-specific conditional double-knockout mice with co-IP and rescue experiments

    PMID:26222436

    Open questions at the time
    • Whether other tissues exhibit the same strict redundancy or have additional compensatory mechanisms is untested
    • Individual contribution of each receptor to specific substrate classes in vivo is unresolved
  10. 2015 High

    Identification of Rpn13 as the major proteasomal receptor for the E3 ligase parkin, with its Ubl domain binding the Pru domain at higher affinity than ubiquitin, connected Rpn13 to mitophagy and Parkinson's disease-relevant biology.

    Evidence NMR, quantitative binding assays, reciprocal co-IP, siRNA, and cell-based mitophagy assay

    PMID:25666615

    Open questions at the time
    • Whether Rpn13-dependent parkin recruitment is relevant in dopaminergic neurons in vivo is untested
    • Competition between parkin-Ubl and ubiquitin for the Pru domain under physiological conditions is not quantified
  11. 2017 High

    Crystal structures of the Pru–RPN2 and Pru–ubiquitin interfaces resolved the overlapping binding surfaces, explaining how Rpn13 integrates proteasome docking with ubiquitin recognition and clarifying how RA190 targets this interface.

    Evidence X-ray crystallography, SPR, NMR, mutagenesis in HCT116 ADRM1-deleted cells

    PMID:28442575 PMID:28598414

    Open questions at the time
    • How Rpn13 simultaneously engages RPN2 and ubiquitin on a shared surface in the context of the intact proteasome is structurally unresolved at full 26S resolution
  12. 2019 High

    NMR structure of the Pru–K48-diubiquitin complex revealed bivalent chain recognition through distinct proximal and distal ubiquitin contacts, providing the structural basis for K48-linkage selectivity; RPN2 Tyr-950 phosphorylation was shown to enhance Rpn13 binding, adding a layer of post-translational regulation.

    Evidence NMR structures, smFRET, charge-reversal mutagenesis with cellular validation; crystal structure of pTyr-950–RPN2–Rpn13–Ub

    PMID:30962947 PMID:31064842

    Open questions at the time
    • The kinase(s) responsible for RPN2 Tyr-950 phosphorylation in vivo and its regulation are not identified
    • How bivalent K48-diUb binding transitions to chain handoff to UCH37 or Rpn11 is mechanistically unclear
  13. 2023 Medium

    Discovery of ADRM1 as a resection inhibitor in DNA double-strand break repair, removed by CRL4-WDR70 ubiquitination to permit MRE11/EXO1 activity, established a non-proteasomal function for ADRM1 in genome integrity.

    Evidence Co-IP, chromatin fractionation, knockout, in vitro and cell-based resection assays, xenograft models

    PMID:37815873

    Open questions at the time
    • The mechanism by which ADRM1 physically blocks resection is not structurally defined
    • Whether this function is independent of UCH37 and proteasome catalytic activity is not fully dissected
    • Confirmation by independent laboratories is needed
  14. 2025 Medium

    Identification of a cancer-associated splice variant (ADRM1-ΔEx9) that switches partner binding from UCH37 to BAP1 and creates a neo-binding site for FBXW7, directing its proteasomal degradation, revealed how alternative splicing can reprogram Rpn13 substrate specificity to promote hepatocellular carcinoma.

    Evidence SMRT sequencing, human organoids, hydrodynamic transfection mouse models, co-IP, patient-derived xenografts

    PMID:39788431

    Open questions at the time
    • Prevalence and regulation of the ΔEx9 splice variant across cancer types is not characterized
    • Structural basis for BAP1 binding by the shortened C-terminus is not determined
    • Independent replication is needed

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include how Rpn13 coordinates with other proteasomal deubiquitinases (Rpn11, USP14) during processive substrate degradation, what determines asymmetric Rpn13 occupancy on double-capped proteasomes, and the in vivo physiological relevance of the Rpn13 autoubiquitination feedback loop.
  • No full-resolution cryo-EM structure of Rpn13-engaged substrate processing intermediate exists
  • In vivo dynamics of Rpn13 autoubiquitination and its reversal are unmeasured
  • Tissue-specific proteasome composition incorporating Rpn13 splice variants has not been systematically profiled

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 4 GO:0060090 molecular adaptor activity 3
Localization
GO:0005829 cytosol 2
Pathway
R-HSA-392499 Metabolism of proteins 6 R-HSA-168256 Immune System 1 R-HSA-73894 DNA Repair 1
Partners
PRKNPSMD1PSMD4SGTAUBE3CUCHL5
Complex memberships
26S proteasome 19S regulatory particle

Evidence

Reading pass · 30 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2008 ADRM1/Rpn13 is a proteasomal ubiquitin receptor that binds K48-linked diubiquitin (~90 nM affinity) through a conserved N-terminal pleckstrin-like receptor for ubiquitin (Pru) domain, and also binds UBL domains of UBL-UBA shuttle proteins; functional linkage with Rpn10 was established by synthetic lethality in yeast when both ubiquitin-binding sites are mutated. Biochemical binding assays, NMR, isothermal titration calorimetry, yeast genetics (double-mutant epistasis) Nature High 18497817
2006 ADRM1 (hRpn13) recruits the deubiquitinating enzyme Uch37 to the 19S proteasome by binding Uch37's C-terminal tail; this binding relieves Uch37 autoinhibition and accelerates ubiquitin-AMC hydrolysis, but processing of polyubiquitin chains requires full 19S incorporation. ADRM1 is itself anchored to the S1/Rpn2 subunit of the 19S complex. Co-IP, mass spectrometry, in vitro DUB activity assay (ubiquitin-AMC), biochemical reconstitution of sub-complexes Nature cell biology High 16906146
2006 The C-terminal half of hRpn13/ADRM1 directly binds UCH37 and enhances its isopeptidase activity; knockdown of hRpn13 in 293T cells increases ubiquitin conjugates and decreases short-lived protein degradation, while overexpression or dominant-negative C-terminal fragment also reduces proteolysis and induces cell death. Affinity purification, co-IP, in vitro isopeptidase assay, siRNA knockdown, transfection/dominant-negative analysis The EMBO journal High 17139257
2006 ADRM1 is a stoichiometric component of the 26S proteasome regulatory ATPase complex, present in cells in amounts equimolar with core 19S subunit S6a, with no detectable free pool; recombinant ADRM1 can bind to pre-existing 26S proteasomes in cell extracts. Co-immunoprecipitation, gel-filtration chromatography, native PAGE, Western blot quantification Journal of molecular biology High 16815440
2013 The bis-benzylidine piperidone RA190 covalently binds to cysteine 88 of RPN13/ADRM1 in the 19S regulatory particle, inhibiting proteasome function and triggering accumulation of polyubiquitinated proteins, ER stress-related apoptosis, and tumor growth inhibition in xenograft models. Covalent drug-protein adduct characterization, cell-based proteasome reporter assay, xenograft mouse models Cancer cell High 24332045
2014 When proteolysis is inhibited in cells or purified 26S proteasomes, the proteasome-associated ubiquitin ligase Ube3c/Hul5 selectively poly-ubiquitinates Rpn13, strongly decreasing the proteasome's ability to bind and degrade ubiquitin-conjugated proteins (but not peptide substrates), acting as an autoinhibitory mechanism. In vitro ubiquitination assay with purified proteasomes, mass spectrometry, cell-based accumulation assay with various proteasome inhibitors The EMBO journal High 24811749
2015 The DEUBAD domain of RPN13 activates UCH-L5/Uch37 by positioning its C-terminal ULD domain and crossover loop to promote substrate binding and catalysis; crystal structures reveal that the related DEUBAD domain of INO80G inhibits UCH-L5 by exploiting the same structural elements but driving a radically different conformation that blocks ubiquitin docking via molecular mimicry. Crystal structure determination, biochemical activity assays, mutagenesis Molecular cell High 25702870
2017 Crystal structure of hRpn13 Pru domain bound to a C-terminal segment of hRpn2 shows that a proline-rich hRpn2 extension stretches across the ubiquitin-binding canyon of the Pru domain, overlapping the RA190-binding surface; hRpn13 binds preferentially to hRpn2/proteasomes over RA190; RA190 directly binds and inactivates Uch37 in addition to targeting hRpn13. X-ray crystallography, SPR biophysics, NMR, cell-based assays, ADRM1 deletion in HCT116 cells Nature communications High 28598414
2017 Crystal structures of the RPN13 PRU domain with RPN2 C-terminal peptide and with ubiquitin reveal that both bind the same PRU domain surface; the C-terminal 14 residues of RPN2 constitute the primary RPN13-docking epitope on the proteasome; ubiquitin, RPN2, and UCH37 bind RPN13 with independent energetics. X-ray crystallography, surface plasmon resonance, fluorescence polarization, mutational analysis The Journal of biological chemistry High 28442575
2014 Rpn13 activates Uch37 by disrupting Uch37 oligomeric autoinhibition: full-length Uch37 forms oligomers where catalytic domains block each other's ubiquitin-binding site; the C-terminal domain of Rpn13 (residues 270–407) sequesters Uch37 monomers into a 1:1 complex with 12-fold higher activity, as demonstrated by mutagenesis, NMR, SAXS, and FRET. Mutagenesis, NMR, SAXS, FRET, in vitro DUB activity assay (Ub-AMC) Protein & cell High 24752541
2019 NMR structure of Rpn13 Pru domain with K48-diubiquitin shows bivalent interaction: proximal Ub binds similarly to monoubiquitin, while distal Ub contacts a largely electrostatic surface of Rpn13; a charge-reversal mutation weakening distal Ub binding causes accumulation of ubiquitinated proteins in cells, establishing the structural basis for Rpn13 K48-chain linkage selectivity. NMR structure determination, single-molecule FRET, mutagenesis, cell-based ubiquitin conjugate accumulation assay Cell discovery High 30962947
2020 NMR structure of hRpn13 Pru:hRpn2(940-953):K48-diubiquitin reveals that hRpn2-bound hRpn13 selects a dynamic, extended conformation of K48-diubiquitin distinct from the closed crystallographic conformation; hRpn13 exchanges between the two ubiquitins within 100 ms but prefers the proximal ubiquitin via interactions with the K48 linker region. NMR structure determination, NMR dynamics experiments Structure High 32160516
2010 Rpn13 is required for iNOS interaction with UCH37 and for iNOS degradation; IκB-α is also a substrate for the Rpn13/UCH37 complex, linking the Rpn13 pathway to NF-κB activation. siRNA knockdown, co-IP, degradation assays in cells Proceedings of the National Academy of Sciences Medium 20634424
2014 The double-capped 26S proteasome is structurally asymmetric: while both 19S particles contain Rpn10/S5a, only one of the two 19S caps contains Rpn13, as demonstrated by AQUA mass spectrometry and biochemical fractionation in both yeast and mammals. AQUA-MS quantification, biochemical fractionation, validated in yeast and mammals The Journal of biological chemistry High 24429290
2015 Rpn13 is the major proteasomal receptor for the E3 ubiquitin ligase parkin: the N-terminal Ubl domain of parkin binds directly to the Pru domain of Rpn13 with >10-fold higher affinity than ubiquitin; Rpn13 knockdown increases parkin levels, abrogates parkin recruitment to the proteasome, delays clearance of mitochondrial proteins during mitophagy, and enhances parkin autoubiquitination. NMR, mutational analysis, Co-IP, siRNA knockdown, affinity measurements, cell-based mitophagy assay The Journal of biological chemistry High 25666615
2015 Rpn13 and Rpn10 function as redundant ubiquitin receptors in the mammalian liver: simultaneous liver-specific knockout of both causes severe liver injury and massive accumulation of ubiquitin conjugates, and mHR23B and ubiquilin/Plic-1/4 shuttle proteins fail to bind the proteasome only when both receptors are absent. Conditional double-knockout mice (liver-specific), co-IP, Western blot for ubiquitin conjugates, rescue experiments PLoS genetics High 26222436
2014 SUMOylation of proteasomal scaffolding protein Psmd1/RPN2 at a lysine immediately adjacent to its Adrm1-binding domain, catalyzed by PIASy, regulates the association of Adrm1 with Psmd1; the SUMO deconjugating enzyme xSENP1 interacts with Psmd1 and its disruption delays mitotic exit. Xenopus egg extract system, SUMO site mapping, co-IP, cell-based mitotic exit assay Cell reports Medium 24910440
2015 The C-terminal region of Rpn13 binds the TPR domain of SGTA (cochaperone for mislocalised membrane proteins); SGTA overexpression increases mislocalised membrane protein levels in a manner dependent on its interaction with Rpn13, suggesting SGTA can regulate substrate access to the proteasome via Rpn13. Co-IP, pulldown, SGTA/Rpn13 mutational analysis, cell-based substrate degradation assay Journal of cell science Medium 26169395
2016 SGTA interacts with the proteasomal ubiquitin receptor Rpn13 through a carboxylate clamp mechanism involving the TPR domain of SGTA and a defined region of the Rpn13 C-terminal domain; structural and biophysical characterization confirmed this interface mediates Rpn13-SGTA association in cells. Structural and biophysical characterization (ITC, NMR, X-ray), mutagenesis, cell-based co-IP Scientific reports High 27827410
2010 In mice, Rpn13 deletion produces tissue-specific effects on proteasomal function (increased activity in adrenal gland and lymphoid organs, decreased in testes and brain), infertility due to defective gametogenesis, and elevated serum growth hormone/FSH, while Uch37 deletion causes prenatal lethality with severe embryonic brain defects. Whole-body knockout mice, proteasome activity assays in tissues, hormone measurements, histology PloS one Medium 21048919
2019 Phosphorylation of RPN2 Tyr-950 by Jurkat cell kinase(s) enhances RPN13 binding affinity; a 1.76-Å crystal structure of the RPN2-RPN13 pTyr-950-ubiquitin complex reveals specific interactions with positively charged RPN13 residues that explain affinity increase without conformational change. X-ray crystallography, mutagenesis, quantitative binding assays The Journal of biological chemistry High 31064842
2015 A 38-amino acid peptide from the C-terminus of hRpn2/PSMD1 binds the hRpn13 Pru domain with 12 nM affinity and displaces endogenous Rpn13 from the proteasome in 293T cells; overexpression of this peptide leads to accumulation of ubiquitinated proteins. NMR epitope mapping, fluorescence polarization binding assay, co-IP, cell-based ubiquitin conjugate assay PloS one High 26466095
2010 Phospho-ΔNp63α binds to the RPN13 promoter (via a TP63-responsive element, in association with DDIT3/CHOP, NF-Y, NF-κB) to activate RPN13 gene transcription in response to cisplatin; this leads to NOS2/iNOS degradation, and RPN13 knockdown rescues NOS2 from cisplatin-dependent inactivation. ChIP, promoter-reporter assay, siRNA knockdown, protein degradation assay The Journal of biological chemistry Medium 20959455
2018 HDAC8 physically interacts with the proteasome receptor ADRM1; inhibition of HDAC8 decreases MGMT protein levels in glioblastoma cells, and this regulation is disrupted by temozolomide specifically in TMZ-sensitive cells, suggesting that the HDAC8-ADRM1 interaction regulates MGMT levels independently of promoter methylation. Co-IP (HDAC8-ADRM1 interaction), HDAC8 inhibitor/shRNA, Western blot for MGMT Genes & cancer Low 31798765
2009 Adrm1 interacts with Atp6v0d2 (V-ATPase V0 domain d2 subunit) as identified by yeast two-hybrid and confirmed by co-immunoprecipitation in vivo; Adrm1 is required for osteoclast cell migration and maturation. Yeast two-hybrid, co-immunoprecipitation, siRNA knockdown in osteoclast differentiation assay Biochemical and biophysical research communications Low 19818731
2016 RPN13/ADRM1 Pru domain functions as a proteasomal receptor for MHC class I antigen processing: both Rpn10 and Rpn13 regulate processing of the NY-ESO-1 cancer/testis antigen and supply of HLA-A*0201-restricted peptides, with non-lysine ubiquitination sites governing this process. siRNA knockdown of Rpn13/Rpn10, antigen presentation assay, ubiquitination site mutagenesis The Journal of biological chemistry Medium 26903513
2023 ADRM1/Rpn13 acts as a resection inhibitor in DNA end processing; during DNA double-strand break repair, ADRM1 is removed from the CDW19S complex (a proteasome variant decorated with CRL4WDR70 ubiquitin ligase) by CRL4WDR70-catalyzed ubiquitination, permitting MRE11 and EXO1 nuclease-mediated resection; HBx stabilizes ADRM1, imposing a resection barrier and causing viral homologous recombination deficiency. Co-IP, chromatin fractionation, knockdown/knockout, in vitro and cell-based resection assays, xenograft models The Journal of clinical investigation Medium 37815873
2023 ADRM1/Rpn13 upregulates UCH37 expression and activates its deubiquitination activity; activated UCH37 then deubiquitinates ALK5 to stabilize it, maintaining extracellular matrix homeostasis in articular cartilage; global ADRM1 KO accelerates cartilage degeneration in a DMM mouse model. Knockout mice, overexpression in vivo, in vitro deubiquitination assay, co-IP (ADRM1-UCH37), Western blot for ALK5 ubiquitination International journal of biological macromolecules Medium 37406898
2025 A novel splice variant of ADRM1 lacking exon 9 (ADRM1-ΔEx9) interacts with deubiquitinase BAP1 (instead of UCH37) via its shortened C-terminus, altering proteasome specificity; the exon 8-10 fusion creates a de novo binding site for tumor suppressor FBXW7, leading to its selective proteasome-mediated degradation and promoting hepatocellular carcinoma. SMRT sequencing, human organoids, hydrodynamic in vivo transfection mouse model, Proteome Profiler Ubiquitin Array, co-IP (ADRM1-ΔEx9-BAP1, ADRM1-ΔEx9-FBXW7), patient-derived xenografts Journal of hepatology Medium 39788431
2025 Protea-Tac, a heterobifunctional degrader using ADRM1/Rpn13 as the proteasome-targeting moiety fused to a target-specific intracellular antibody, integrates into 26S proteasomes without altering their integrity and degrades substrates (c-Fos, BRD4, tau, TDP43, GFP-ODC) in a ubiquitin-independent manner via direct proteasomal targeting. Reconstitution of chimeric degrader in cells, proteasome structural/functional integrity assays, in vivo xenograft mouse model bioRxivpreprint Medium

Source papers

Stage 0 corpus · 94 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2008 Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 541 18497817
2006 Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nature cell biology 292 16906146
2006 hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37. The EMBO journal 206 17139257
1989 Susceptibility to rheumatoid arthritis maps to a T-cell epitope shared by the HLA-Dw4 DR beta-1 chain and the Epstein-Barr virus glycoprotein gp110. Proceedings of the National Academy of Sciences of the United States of America 183 2472638
2013 A bis-benzylidine piperidone targeting proteasome ubiquitin receptor RPN13/ADRM1 as a therapy for cancer. Cancer cell 142 24332045
2014 Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiquitin conjugates. The EMBO journal 137 24811749
2002 Glycoprotein gp110 of Epstein-Barr virus determines viral tropism and efficiency of infection. Proceedings of the National Academy of Sciences of the United States of America 129 12409611
2015 Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G. Molecular cell 106 25702870
1990 Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110. Journal of virology 100 2157039
2010 Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development. PloS one 80 21048919
1994 Merosin promotes neurite growth and Schwann cell migration in vitro and nerve regeneration in vivo: evidence using an antibody to merosin, ARM-1. Developmental biology 80 8026618
1990 Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: an analysis by tissue distribution, purification and N-terminal amino acid sequence. Hepatology (Baltimore, Md.) 78 1970322
2017 Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets. Nature communications 72 28598414
2015 Redundant Roles of Rpn10 and Rpn13 in Recognition of Ubiquitinated Proteins and Cellular Homeostasis. PLoS genetics 71 26222436
2015 A reversible and highly selective inhibitor of the proteasomal ubiquitin receptor rpn13 is toxic to multiple myeloma cells. Journal of the American Chemical Society 69 25914958
2016 Targeting proteasome ubiquitin receptor Rpn13 in multiple myeloma. Leukemia 68 27118409
2010 Regulation of NF-kappaB activity and inducible nitric oxide synthase by regulatory particle non-ATPase subunit 13 (Rpn13). Proceedings of the National Academy of Sciences of the United States of America 59 20634424
2020 The CCDC43-ADRM1 axis regulated by YY1, promotes proliferation and metastasis of gastric cancer. Cancer letters 56 32278016
2006 Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-associated factor. Journal of molecular biology 55 16815440
1994 Characterization of murine gammaherpesvirus 68 glycoprotein B (gB) homolog: similarity to Epstein-Barr virus gB (gp110). Journal of virology 49 8083987
2017 Structure and energetics of pairwise interactions between proteasome subunits RPN2, RPN13, and ubiquitin clarify a substrate recruitment mechanism. The Journal of biological chemistry 46 28442575
2013 Amplification Target ADRM1: Role as an Oncogene and Therapeutic Target for Ovarian Cancer. International journal of molecular sciences 42 23377018
2009 Knockdown of the novel proteasome subunit Adrm1 located on the 20q13 amplicon inhibits colorectal cancer cell migration, survival and tumorigenicity. Oncology reports 41 19148532
2008 Comprehensive analysis of 20q13 genes in ovarian cancer identifies ADRM1 as amplification target. Genes, chromosomes & cancer 41 18615678
2000 Decreased T cell precursor frequencies to Epstein-Barr virus glycoprotein Gp110 in peripheral blood correlate with disease activity and severity in patients with rheumatoid arthritis. Annals of the rheumatic diseases 40 10873963
2019 Development and preclinical validation of a novel covalent ubiquitin receptor Rpn13 degrader in multiple myeloma. Leukemia 39 30962579
2015 The E3 ubiquitin ligase parkin is recruited to the 26 S proteasome via the proteasomal ubiquitin receptor Rpn13. The Journal of biological chemistry 37 25666615
2001 Distinctly different gene structure of KLK4/KLK-L1/prostase/ARM1 compared with other members of the kallikrein family: intracellular localization, alternative cDNA forms, and Regulation by multiple hormones. DNA and cell biology 35 11506707
2019 HDAC8 affects MGMT levels in glioblastoma cell lines via interaction with the proteasome receptor ADRM1. Genes & cancer 33 31798765
1999 Functional cloning of ARM-1, an adhesion-regulating molecule upregulated in metastatic tumor cells. Clinical & experimental metastasis 33 10919708
2014 ADRM1 gene amplification is a candidate driver for metastatic gastric cancers. Clinical & experimental metastasis 32 24968865
1993 Characterisation of the ATP-dependent taurocholate-carrier protein (gp110) of the hepatocyte canalicular membrane. European journal of biochemistry 31 8513803
1988 A molecular mechanism of inhibition of HIV-1 binding to CD4+ cells by monoclonal antibodies to gp110. AIDS (London, England) 31 2456085
2019 Structural basis for the recognition of K48-linked Ub chain by proteasomal receptor Rpn13. Cell discovery 30 30962947
2014 Mechanism of the Rpn13-induced activation of Uch37. Protein & cell 30 24752541
2018 Covalent Rpn13-Binding Inhibitors for the Treatment of Ovarian Cancer. ACS omega 28 30288466
2010 Phospho-ΔNp63α/Rpn13-dependent regulation of LKB1 degradation modulates autophagy in cancer cells. Aging 28 21191146
2020 An Extended Conformation for K48 Ubiquitin Chains Revealed by the hRpn2:Rpn13:K48-Diubiquitin Structure. Structure (London, England : 1993) 27 32160516
2018 RA190, a Proteasome Subunit ADRM1 Inhibitor, Suppresses Intrahepatic Cholangiocarcinoma by Inducing NF-KB-Mediated Cell Apoptosis. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 27 29913454
1988 Membrane orientation of rat gp110 as studied by in vitro translation. The Journal of biological chemistry 27 3182821
2015 A High Affinity hRpn2-Derived Peptide That Displaces Human Rpn13 from Proteasome in 293T Cells. PloS one 26 26466095
2015 Structural plasticity allows UCH37 to be primed by RPN13 or locked down by INO80G. Molecular cell 24 25747657
2016 RPN13/ADRM1 inhibitor reverses immunosuppression by myeloid-derived suppressor cells. Oncotarget 23 27655678
2020 Physical and Functional Analysis of the Putative Rpn13 Inhibitor RA190. Cell chemical biology 22 32857985
2015 ADRM1-amplified metastasis gene in gastric cancer. Genes, chromosomes & cancer 22 26052681
2015 Binding of SGTA to Rpn13 selectively modulates protein quality control. Journal of cell science 22 26169395
1995 A short isoform of carcinoembryonic-antigen-related rat liver cell-cell adhesion molecule (C-CAM/gp110) mediates intercellular adhesion. Sequencing and recombinant functional analysis. European journal of biochemistry 20 8536699
2020 Proteomic analysis identifies mechanism(s) of overcoming bortezomib resistance via targeting ubiquitin receptor Rpn13. Leukemia 19 32424294
2016 Major Histocompatibility Complex (MHC) Class I Processing of the NY-ESO-1 Antigen Is Regulated by Rpn10 and Rpn13 Proteins and Immunoproteasomes following Non-lysine Ubiquitination. The Journal of biological chemistry 19 26903513
2014 Inherent asymmetry in the 26S proteasome is defined by the ubiquitin receptor RPN13. The Journal of biological chemistry 19 24429290
2009 Adrm1 interacts with Atp6v0d2 and regulates osteoclast differentiation. Biochemical and biophysical research communications 19 19818731
2006 A Phg2-Adrm1 pathway participates in the nutrient-controlled developmental response in Dictyostelium. Molecular biology of the cell 18 16987957
1990 Large fragments of nef-protein and gp110 envelope glycoprotein from HIV-1. Synthesis, CD analysis and immunoreactivity. International journal of peptide and protein research 17 2182558
1989 Localization of a putative cell adhesion molecule (gp110) in Wistar and Fischer rat tissues. Histochemistry 17 2613547
2014 SUMOylation of Psmd1 controls Adrm1 interaction with the proteasome. Cell reports 16 24910440
2011 Knockdown of ovarian cancer amplification target ADRM1 leads to downregulation of GIPC1 and upregulation of RECK. Genes, chromosomes & cancer 16 21432940
2020 Bis-benzylidine Piperidone RA190 treatment of hepatocellular carcinoma via binding RPN13 and inhibiting NF-κB signaling. BMC cancer 15 32375699
2016 The Ubiquitin Receptor ADRM1 Modulates HAP40-Induced Proteasome Activity. Molecular neurobiology 15 27815841
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