this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 20 citations 1 artifacts 2026-05-31T17:58:52.120386
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The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

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Research Report: Functional Annotation of Saccharomyces cerevisiae UBP3 (UniProt Q01477, ORF YER151C)

0) Target verification (critical identity checks)

The evidence assembled here consistently refers to Ubp3 from Saccharomyces cerevisiae (budding yeast; strain background varies by study), a deubiquitinase (DUB) that functions in a stable complex with Bre5 and is experimentally linked to deubiquitination of trafficking and ribosomal substrates (e.g., Sec23; ribosomal eS7A) and to processes including ER–Golgi trafficking, selective autophagy, and UPR-linked translational control (cohen2003deubiquitinationanew pages 1-1, 稲田2024grr1mediatedubp3degradation pages 1-5). This matches the UniProt-provided protein description “ubiquitin carboxyl-terminal hydrolase 3 / ubiquitin-specific-processing protease 3” for UniProt Q01477.

1) Key concepts and definitions (current understanding)

1.1 Deubiquitinases (DUBs) and Ubp3’s enzymatic role

DUBs remove ubiquitin from ubiquitinated proteins, thereby reversing or editing ubiquitin signals that control protein fate, localization, trafficking, and pathway signaling. A yeast-focused review synthesizes Ubp3 as an active DUB with multiple experimentally supported roles and emphasizes that Ubp3 activity is typically deployed via recruitment and cofactor control rather than acting as a constitutive “housekeeping” enzyme (suresh2020thestructureand pages 17-18).

1.2 Ubp3–Bre5 as a functional DUB complex

A core principle for Ubp3 biology is that it acts in a Ubp3·Bre5 complex. In the ER–Golgi trafficking context, Bre5 is described as an essential positive regulator of Ubp3’s activity (not merely a passive binding partner), consistent with a model where cofactors tune DUB substrate specificity and/or activity (cohen2003deubiquitinationanew pages 1-1).

2) Molecular function: reaction catalyzed and substrate specificity

2.1 Reaction catalyzed

Ubp3 catalyzes deubiquitination—hydrolysis of the isopeptide bond linking ubiquitin to a substrate lysine (or the corresponding bond types on ubiquitin chains)—thereby removing ubiquitin from target proteins (suresh2020thestructureand pages 17-18).

2.2 Experimentally supported substrates and substrate contexts

(A) COPII coat subunit Sec23 (ER-to-Golgi trafficking substrate).
A primary study reports that Ubp3, with Bre5, specifically deubiquitinates the COPII subunit Sec23, and in that report Ubp3 is described as the only yeast Ubp able to catalyze Sec23 deubiquitination (cohen2003deubiquitinationanew pages 1-1). This directly anchors Ubp3 in the COPII pathway and connects its enzymatic activity to vesicle-coat regulation at the ER.

(B) COPI subunit (Golgi-to-ER retrograde trafficking substrate).
The same work identifies a COPI subunit (β′-COP noted as a substrate) as another Ubp3·Bre5 target, consistent with Ubp3 coordinating both anterograde and retrograde trafficking between ER and Golgi (cohen2003deubiquitinationanew pages 1-1).

(C) Ribosomal ubiquitination targets: eS7A in UPR-linked translation control.
A 2024 preprint presents Ubp3 as the deubiquitinase that counteracts ubiquitination of ribosomal protein eS7A, placing Ubp3 activity directly in ribosome ubiquitination cycles that regulate stress-responsive translation (稲田2024grr1mediatedubp3degradation pages 1-5).

(D) Ribosome/60S-associated ubiquitin signals in ribophagy.
Ribophagy (selective autophagy of ribosomes) requires Ubp3–Bre5; Ubp3 is positioned as a DUB that removes an inhibitory ubiquitin signal from ribosomal components to permit delivery to the vacuole during starvation (ossarehnazari2014ubiquitylationbythe pages 9-9).

(E) Additional functional substrate areas supported by literature synthesis.
A yeast DUB review and a JBC study summarizing Ubp3 literature link Ubp3 to additional substrates/contexts (e.g., RNA polymerase II deubiquitination; proteasome-linked degradation control) while emphasizing Bre5 and other partners that tune Ubp3 function across pathways (suresh2020thestructureand pages 17-18, lan2021deubiquitinaseubp3enhances pages 13-13).

3) Key binding partners and regulators

3.1 Bre5 (core cofactor)

Bre5 is repeatedly supported as Ubp3’s key partner required for specific deubiquitination events, including Sec23/COPII regulation and ribosome-linked pathways (cohen2003deubiquitinationanew pages 1-1, 稲田2024grr1mediatedubp3degradation pages 1-5).

3.2 Grr1 (E3 ligase component regulating Ubp3 abundance during UPR; 2024)

A 2024 preprint identifies Grr1, an F-box component of the SCF ubiquitin ligase complex, as an E3 factor required for Ubp3 proteasomal degradation during ER stress, which increases eS7A monoubiquitination and enables robust translation of the spliced HAC1i mRNA (稲田2024grr1mediatedubp3degradation pages 1-5, 稲田2024grr1mediatedubp3degradation pages 5-7).

3.3 Not4 (E3 ligase for eS7A ubiquitination)

The same 2024 preprint positions Not4 as the E3 ligase that monoubiquitinates eS7A, with Ubp3 acting in opposition (as the DUB) and Grr1 acting upstream to reduce Ubp3 levels under UPR (稲田2024grr1mediatedubp3degradation pages 1-5).

3.4 Antagonistic ubiquitin-system components in DNA damage responses

In the DNA damage context, genetic evidence supports an antagonistic relationship between Ubp3/Bre5 and the Rsp5/Bul1 ligase pathway with respect to phleomycin sensitivity and NHEJ (bilsland2007thebre5ubp3ubiquitin pages 11-12, bilsland2007thebre5ubp3ubiquitin pages 9-11).

4) Biological processes and pathways (with localization context)

Functional area Key findings (1-2 sentences) Substrate/partner Assay/evidence type Source (authors/year/journal) URL Citation ID
Molecular function / DUB complex Ubp3 is a deubiquitinating enzyme in S. cerevisiae that acts in a stable complex with the cofactor Bre5. Bre5 is an essential positive regulator of Ubp3 activity rather than merely a passive binding factor. Bre5 Biochemical and genetic characterization; interaction studies Cohen, Stutz & Dargemont 2003, J. Biol. Chem. https://doi.org/10.1074/jbc.c300451200 (cohen2003deubiquitinationanew pages 1-1)
ER-to-Golgi anterograde trafficking Ubp3 specifically deubiquitinates the COPII coat subunit Sec23, and this activity requires Bre5. This places Ubp3 directly in secretory-pathway control at the ER/COPII interface. Sec23, Bre5 Substrate identification, deubiquitination/interaction studies Cohen, Stutz & Dargemont 2003, J. Biol. Chem.; Suresh, Pascoe & Andrews 2020, Open Biology https://doi.org/10.1074/jbc.c300451200 ; https://doi.org/10.1098/rsob.200279 (cohen2003deubiquitinationanew pages 1-1, suresh2020thestructureand pages 17-18)
Golgi-to-ER retrograde trafficking Disruption of BRE5 causes defects in Golgi-to-ER retrograde transport, and the Ubp3-Bre5 complex also targets a COPI subunit. Together these data indicate Ubp3 coordinates both forward and reverse ER-Golgi trafficking. Bre5, COPI subunit β′-COP Mutant phenotyping in trafficking assays; substrate assignment Cohen, Stutz & Dargemont 2003, J. Biol. Chem. https://doi.org/10.1074/jbc.c300451200 (cohen2003deubiquitinationanew pages 1-1)
Ribophagy / selective autophagy Ubp3-Bre5 is required for starvation-induced ribophagy, acting on ubiquitinated 60S ribosomal components so ribosomes can be selectively delivered for autophagic degradation. Ribosome ubiquitylation antagonizes this pathway, implying Ubp3 removes an inhibitory ubiquitin signal. Bre5, 60S ribosomal proteins; antagonistic E3 Ltn1 Starvation/ribophagy genetics and pathway analysis Ossareh-Nazari et al. 2014, J. Cell Biol.; Suresh, Pascoe & Andrews 2020, Open Biology https://doi.org/10.1083/jcb.201308139 ; https://doi.org/10.1098/rsob.200279 (ossarehnazari2014ubiquitylationbythe pages 9-9, suresh2020thestructureand pages 17-18)
Mitophagy regulation A genome-wide SQA screen showed that loss of Ubp3 or Bre5 increases rapamycin-induced mitophagy, identifying the Ubp3-Bre5 complex as a negative regulator of mitophagy. In the same study, the complex was linked positively to bulk autophagy, ribophagy, and the Cvt pathway. Bre5; mitochondrial autophagy pathway components Synthetic quantitative array screen; rapamycin-induced mitophagy assays Müller et al. 2015, Cell Reports https://doi.org/10.1016/j.celrep.2015.01.044 (muller2015syntheticquantitativearray pages 9-10)
DNA damage response / DSB repair Ubp3-Bre5 contributes to the cellular response to DNA damage by promoting non-homologous end joining and resistance to the DSB-inducing drug phleomycin. Catalytic activity of Ubp3 is required, and genetic antagonism with the Rsp5/Bul1 ligase pathway was reported. Bre5; antagonistic Bul1/Rsp5 pathway HO endonuclease survival assays, plasmid-repair/NHEJ assays, phleomycin sensitivity, co-IP, microarrays Bilsland et al. 2007, DNA Repair https://doi.org/10.1016/j.dnarep.2007.04.010 (bilsland2007thebre5ubp3ubiquitin pages 11-12, bilsland2007thebre5ubp3ubiquitin pages 1-2, bilsland2007thebre5ubp3ubiquitin pages 9-11, bilsland2007thebre5ubp3ubiquitin pages 3-5)
UPR / translational control During ER stress, SCF^Grr1 promotes Ubp3 degradation, which increases monoubiquitinated eS7A and enables efficient translation of spliced HAC1i mRNA. In grr1Δ, HAC1 translational efficiency is ~4-fold lower, and Ubp3 degradation is slowed; CHX-chase estimates gave an Ubp3 half-life of ~80 min with stress versus ~120 min without. eS7A, Bre5, Grr1, Not4, HAC1i mRNA Ribosome profiling, RNA-seq, CHX chase, co-IP, western blotting, tunicamycin sensitivity assays Inada et al. 2024, preprint https://doi.org/10.21203/rs.3.rs-4865151/v1 (稲田2024grr1mediatedubp3degradation pages 7-10, 稲田2024grr1mediatedubp3degradation pages 18-24, 稲田2024grr1mediatedubp3degradation pages 5-7)
Glucose repression / mitochondrial metabolism A DUB knockout screen identified Ubp3 as necessary for glucose-mediated mitochondrial repression. ubp3Δ cells show increased mitochondrial membrane potential, higher basal OCR, higher Cox2, and altered ATP partitioning; after azide treatment ATP remained ~60% of total in WT versus ~40% in ubp3Δ, indicating a larger mitochondrial ATP contribution in the mutant. Glycolytic enzymes Pfk1, Tdh2/Tdh3; mitochondrial ETC component Cox2 DUB knockout screen, OCR assays, ATP measurements, western blots, mitochondrial staining Vengayil et al. 2024, eLife https://doi.org/10.7554/elife.90293 (vengayil2024thedeubiquitinaseubp3usp10 pages 1-2, vengayil2024thedeubiquitinaseubp3usp10 pages 3-4)
Phosphate budgeting mechanism Ubp3 constrains mitochondrial activation by maintaining high glycolytic flux; loss of Ubp3 lowers Pfk1 and GAPDH/Tdh2-Tdh3, reroutes glucose toward trehalose synthesis and PPP, and increases cellular and mitochondrial inorganic phosphate. These experiments were typically reported with three biological replicates and significance thresholds of p<0.05, p<0.01, p*<0.001. Pfk1, Tdh2/Tdh3, Tps2, Mir1 Proteomics, ^13C pulse-labeling, Pi measurements, OCR, Mitotracker, growth assays across strain backgrounds Vengayil et al. 2024, eLife https://doi.org/10.7554/elife.90293 (vengayil2024thedeubiquitinaseubp3usp10 pages 9-10, vengayil2024thedeubiquitinaseubp3usp10 pages 15-17, vengayil2024thedeubiquitinaseubp3usp10 pages 14-15, vengayil2024thedeubiquitinaseubp3usp10 pages 17-18, vengayil2024thedeubiquitinaseubp3usp10 pages 6-7, vengayil2024thedeubiquitinaseubp3usp10 pages 8-9)
Proteostasis / sterol homeostasis Ubp3 has also been implicated in enhancing proteasomal degradation of key sterol-homeostasis enzymes, expanding its functional repertoire beyond trafficking and autophagy. Review/excerpted evidence further links Ubp3 to RNAPII deubiquitination, Rad4 proteasomal turnover, heat resistance, and replicative lifespan control. Sterol-homeostasis enzymes; RNAPII; Rad4; Cdc48; Ufd3 Quantitative proteomics/turnover assays; literature synthesis Lan et al. 2021, J. Biol. Chem.; Suresh, Pascoe & Andrews 2020, Open Biology https://doi.org/10.1016/j.jbc.2021.100348 ; https://doi.org/10.1098/rsob.200279 (lan2021deubiquitinaseubp3enhances pages 13-13, lan2021deubiquitinaseubp3enhances pages 12-13, suresh2020thestructureand pages 17-18)
Localization contexts Experimental contexts place Ubp3 at COPII/ER-Golgi trafficking sites (via Sec23/COPI), in the cytoplasm on ribosomal substrates during ribophagy, and functionally in mitochondrial regulation and ER-stress translation control. These localization inferences come from validated substrates and pathway assays rather than a single dedicated localization study in the provided evidence. Sec23/COPI, ribosomal proteins/eS7A, mitochondrial pathway factors Localization inferred from substrate/pathway-specific experiments across studies Cohen, Stutz & Dargemont 2003, J. Biol. Chem.; Müller et al. 2015, Cell Reports; Inada et al. 2024, preprint; Vengayil et al. 2024, eLife https://doi.org/10.1074/jbc.c300451200 ; https://doi.org/10.1016/j.celrep.2015.01.044 ; https://doi.org/10.21203/rs.3.rs-4865151/v1 ; https://doi.org/10.7554/elife.90293 (cohen2003deubiquitinationanew pages 1-1, muller2015syntheticquantitativearray pages 9-10, 稲田2024grr1mediatedubp3degradation pages 7-10, 稲田2024grr1mediatedubp3degradation pages 18-24, vengayil2024thedeubiquitinaseubp3usp10 pages 1-2, vengayil2024thedeubiquitinaseubp3usp10 pages 3-4)

Table: This table compiles experimentally supported functions, substrates, partners, pathways, and localization contexts for the yeast deubiquitinase Ubp3/YER151C. It is useful as a quick evidence map linking specific claims to the underlying primary literature and context IDs.

4.1 ER–Golgi trafficking (COPII/COPI coat regulation)

Ubp3·Bre5 deubiquitinates Sec23 (COPII) and a COPI subunit, and Bre5 disruption produces a Golgi-to-ER retrograde transport defect, implying that Ubp3 functionally operates at ER exit/trafficking interfaces and in ER–Golgi bidirectional transport regulation (cohen2003deubiquitinationanew pages 1-1). These substrates provide the strongest direct anchoring of Ubp3 to a specific subcellular “worksite” (ER–Golgi transport machinery).

4.2 Ribophagy (selective autophagy of ribosomes)

Ubp3–Bre5 is required for starvation-induced ribophagy; ubiquitination of ribosomes inhibits ribophagy, and Ubp3–Bre5 deubiquitination is required to set the effective rate of starvation-induced ribosomal protein degradation via ribophagy (ossarehnazari2014ubiquitylationbythe pages 9-9). This places Ubp3 function in a cytosolic-to-vacuolar selective autophagy pathway.

4.3 Mitophagy (negative regulator)

A genome-wide screen-based study identifies Ubp3–Bre5 as a negative regulator of rapamycin-induced mitophagy, while also connecting the complex to bulk autophagy and other autophagic routes (muller2015syntheticquantitativearray pages 9-10). This supports a model where Ubp3–Bre5 edits ubiquitin signals that, depending on context and substrate, can either permit or restrain selective organelle turnover.

4.4 DNA damage response: double-strand break repair by NHEJ

A primary DNA repair study reports that ubp3 and bre5 mutants are sensitive to the DSB-inducing drug phleomycin and display NHEJ defects; importantly, Ubp3 catalytic activity is required (a catalytic point mutant cannot complement), connecting enzymatic activity to the phenotype (bilsland2007thebre5ubp3ubiquitin pages 9-11). The work also supports pathway-level antagonism between Ubp3/Bre5 and Bul1/Rsp5 (bilsland2007thebre5ubp3ubiquitin pages 11-12).

4.5 Unfolded protein response (UPR): translational control via ribosome ubiquitination (2024)

A 2024 preprint proposes a detailed regulatory model: during UPR, SCF^Grr1 promotes Ubp3 degradation, raising monoubiquitinated eS7A (produced by Not4), which facilitates efficient translation of HAC1i mRNA and thus UPR output (稲田2024grr1mediatedubp3degradation pages 1-5, 稲田2024grr1mediatedubp3degradation pages 5-7). This provides a direct mechanistic role for Ubp3 in an ER-stress signaling pathway at the level of translation.

4.6 Glucose repression/mitochondrial repression via phosphate budgeting (eLife 2024)

A 2024 eLife study identifies Ubp3 in a DUB knockout screen as necessary for glucose-mediated mitochondrial repression (Crabtree-like behavior). Loss of Ubp3 rewires metabolism (lower Pfk1 and GAPDH/Tdh2-Tdh3; increased trehalose flux) and changes inorganic phosphate (Pi) budgeting between glycolysis and mitochondria, enabling mitochondrial activation despite high glucose (vengayil2024thedeubiquitinaseubp3usp10 pages 1-2, vengayil2024thedeubiquitinaseubp3usp10 pages 6-7).

5) Recent developments and latest research (prioritizing 2023–2024)

5.1 Ubp3 as a regulator of glucose-mediated mitochondrial repression (publication date: May 2024)

Vengayil et al. (eLife, 2024-05; https://doi.org/10.7554/elife.90293) report that Ubp3 catalytic activity is required for mitochondrial repression in high glucose (supported by a catalytic mutant analysis) and propose that Ubp3 controls mitochondrial activity indirectly via Pi availability by governing glycolytic flux and trehalose synthesis (vengayil2024thedeubiquitinaseubp3usp10 pages 3-4, vengayil2024thedeubiquitinaseubp3usp10 pages 17-18). The study further reports this phenotype is reproducible across multiple yeast genetic backgrounds (vengayil2024thedeubiquitinaseubp3usp10 pages 15-17).

5.2 Ubp3 degradation as a UPR control point (publication date: Aug 2024 preprint)

Inada et al. (preprint, 2024-08; https://doi.org/10.21203/rs.3.rs-4865151/v1) introduce a regulatory axis in which the E3 ligase component Grr1 promotes Ubp3 degradation during ER stress to increase ribosome monoubiquitination (eS7A) and enable translation of the spliced HAC1 mRNA (稲田2024grr1mediatedubp3degradation pages 5-7, 稲田2024grr1mediatedubp3degradation pages 18-24). This reframes Ubp3 not only as an enzyme acting on substrates but also as a regulated node whose abundance is dynamically tuned to remodel translation under stress.

5.3 2023 pathway framing: ubiquitin-dependent selective autophagy in yeast

While not Ubp3-centric, 2023 commentary/review literature on ubiquitin-binding autophagy receptors in yeast emphasizes that ubiquitin can drive selective autophagy through multiple receptor systems, motivating ongoing exploration of how ubiquitin editing enzymes (including DUBs) determine whether ubiquitinated cargo is degraded by proteasome or autophagy (Mensah et al., 2023; see retrieved paper metadata). In the current evidence base, Ubp3’s direct involvement is best supported for ribophagy/mitophagy and not yet mapped to specific ubiquitin-binding receptors (context not directly extracted here).

6) Subcellular localization: where Ubp3 acts

No single dedicated localization study was retrieved in the current evidence set; however, substrate- and pathway-anchored localization can be inferred with high confidence:

7) Expert opinions and analysis (authoritative synthesis)

A yeast-centered DUB review highlights Ubp3 as an example of a multifunctional DUB whose pathway outputs (ribophagy, stress granules, trafficking) depend on cofactor recruitment (Bre5) and context-specific deployment, aligning with a broader principle that DUB specificity is often “built” by interaction networks rather than by catalytic domain sequence alone (suresh2020thestructureand pages 17-18). The early trafficking-focused primary work similarly emphasizes Bre5 as an essential positive regulator of Ubp3 activity, reinforcing this mechanistic concept (cohen2003deubiquitinationanew pages 1-1).

8) Statistics, data, and quantitative findings (recent and/or mechanistically informative)

8.1 UPR translation control (2024 preprint)

8.2 Glucose/mitochondrial repression via Pi budgeting (eLife 2024)

8.3 DNA damage/NHEJ studies (2007)

Quantitative experimental design is described for NHEJ/plasmid repair assays (e.g., WT set to 100% repaired; multiple replicates), though explicit numeric survival values were not extractable from the provided excerpt (bilsland2007thebre5ubp3ubiquitin pages 1-2).

9) Current applications and real-world implementations

  1. Yeast as a model for conserved deubiquitinase biology. Ubp3 is discussed as orthologous to mammalian USP10 in a 2024 metabolic repression study, enabling cross-species hypothesis generation about DUB control of metabolism and mitochondrial activity (Vengayil et al., eLife, 2024-05; https://doi.org/10.7554/elife.90293) (vengayil2024thedeubiquitinaseubp3usp10 pages 1-2).
  2. Mechanistic dissection of stress responses relevant to ER stress and proteostasis. The Ubp3→eS7A ubiquitination→HAC1 translation axis provides a genetically tractable framework for studying how ubiquitin modifications on ribosomes reshape translation during UPR (Inada et al., 2024-08 preprint; https://doi.org/10.21203/rs.3.rs-4865151/v1) (稲田2024grr1mediatedubp3degradation pages 1-5, 稲田2024grr1mediatedubp3degradation pages 5-7).
  3. Trafficking/secretory pathway regulation. Ubp3–Bre5 modulation of COPII/COPI coat ubiquitination provides an experimental handle for probing how ubiquitin editing controls vesicle formation and ER–Golgi homeostasis—important both for fundamental cell biology and for optimizing secretion-related phenotypes in yeast-based production systems (cohen2003deubiquitinationanew pages 1-1).

10) Consolidated functional annotation (high-confidence statements)

Key references (with URLs and publication dates)

References

  1. (cohen2003deubiquitinationanew pages 1-1): Mickaël Cohen, Françoise Stutz, and Catherine Dargemont. Deubiquitination, a new player in golgi to endoplasmic reticulum retrograde transport*. Journal of Biological Chemistry, 278:51989-51992, Dec 2003. URL: https://doi.org/10.1074/jbc.c300451200, doi:10.1074/jbc.c300451200. This article has 90 citations and is from a domain leading peer-reviewed journal.

  2. (稲田2024grr1mediatedubp3degradation pages 1-5): 利文 稲田, Nichika Sato, Shota Tomomatsu, Sihan Li, Yoshitaka Matsuo, Yu Nakano, and Yasuko Matsuki. Grr1-mediated ubp3 degradation is crucial for hac1 mrna translation and unfolded stress response in yeast. Unknown journal, Aug 2024. URL: https://doi.org/10.21203/rs.3.rs-4865151/v1, doi:10.21203/rs.3.rs-4865151/v1.

  3. (suresh2020thestructureand pages 17-18): Harsha Garadi Suresh, Natasha Pascoe, and Brenda Andrews. The structure and function of deubiquitinases: lessons from budding yeast. Oct 2020. URL: https://doi.org/10.1098/rsob.200279, doi:10.1098/rsob.200279. This article has 60 citations and is from a peer-reviewed journal.

  4. (ossarehnazari2014ubiquitylationbythe pages 9-9): Batool Ossareh-Nazari, Carlos A. Niño, Mario H. Bengtson, Joong-Won Lee, Claudio A.P. Joazeiro, and Catherine Dargemont. Ubiquitylation by the ltn1 e3 ligase protects 60s ribosomes from starvation-induced selective autophagy. The Journal of Cell Biology, 204:909-917, Mar 2014. URL: https://doi.org/10.1083/jcb.201308139, doi:10.1083/jcb.201308139. This article has 122 citations.

  5. (lan2021deubiquitinaseubp3enhances pages 13-13): Qiuyan Lan, Yanchang Li, Fuqiang Wang, Zhaodi Li, Yuan Gao, Hui Lu, Yihao Wang, Zhenwen Zhao, Zixin Deng, Fuchu He, Junzhu Wu, and Ping Xu. Deubiquitinase ubp3 enhances the proteasomal degradation of key enzymes in sterol homeostasis. The Journal of Biological Chemistry, 296:100348, Jan 2021. URL: https://doi.org/10.1016/j.jbc.2021.100348, doi:10.1016/j.jbc.2021.100348. This article has 12 citations.

  6. (稲田2024grr1mediatedubp3degradation pages 5-7): 利文 稲田, Nichika Sato, Shota Tomomatsu, Sihan Li, Yoshitaka Matsuo, Yu Nakano, and Yasuko Matsuki. Grr1-mediated ubp3 degradation is crucial for hac1 mrna translation and unfolded stress response in yeast. Unknown journal, Aug 2024. URL: https://doi.org/10.21203/rs.3.rs-4865151/v1, doi:10.21203/rs.3.rs-4865151/v1.

  7. (bilsland2007thebre5ubp3ubiquitin pages 11-12): Elizabeth Bilsland, Malin Hult, Stephen D. Bell, Per Sunnerhagen, and Jessica A. Downs. The bre5/ubp3 ubiquitin protease complex from budding yeast contributes to the cellular response to dna damage. DNA repair, 6 10:1471-84, Oct 2007. URL: https://doi.org/10.1016/j.dnarep.2007.04.010, doi:10.1016/j.dnarep.2007.04.010. This article has 35 citations and is from a peer-reviewed journal.

  8. (bilsland2007thebre5ubp3ubiquitin pages 9-11): Elizabeth Bilsland, Malin Hult, Stephen D. Bell, Per Sunnerhagen, and Jessica A. Downs. The bre5/ubp3 ubiquitin protease complex from budding yeast contributes to the cellular response to dna damage. DNA repair, 6 10:1471-84, Oct 2007. URL: https://doi.org/10.1016/j.dnarep.2007.04.010, doi:10.1016/j.dnarep.2007.04.010. This article has 35 citations and is from a peer-reviewed journal.

  9. (muller2015syntheticquantitativearray pages 9-10): Matthias Müller, Peter Kötter, Christina Behrendt, Elena Walter, Christian Q. Scheckhuber, Karl-Dieter Entian, and Andreas S. Reichert. Synthetic quantitative array technology identifies the ubp3-bre5 deubiquitinase complex as a negative regulator of mitophagy. Cell reports, 10 7:1215-25, Feb 2015. URL: https://doi.org/10.1016/j.celrep.2015.01.044, doi:10.1016/j.celrep.2015.01.044. This article has 72 citations and is from a highest quality peer-reviewed journal.

  10. (bilsland2007thebre5ubp3ubiquitin pages 1-2): Elizabeth Bilsland, Malin Hult, Stephen D. Bell, Per Sunnerhagen, and Jessica A. Downs. The bre5/ubp3 ubiquitin protease complex from budding yeast contributes to the cellular response to dna damage. DNA repair, 6 10:1471-84, Oct 2007. URL: https://doi.org/10.1016/j.dnarep.2007.04.010, doi:10.1016/j.dnarep.2007.04.010. This article has 35 citations and is from a peer-reviewed journal.

  11. (bilsland2007thebre5ubp3ubiquitin pages 3-5): Elizabeth Bilsland, Malin Hult, Stephen D. Bell, Per Sunnerhagen, and Jessica A. Downs. The bre5/ubp3 ubiquitin protease complex from budding yeast contributes to the cellular response to dna damage. DNA repair, 6 10:1471-84, Oct 2007. URL: https://doi.org/10.1016/j.dnarep.2007.04.010, doi:10.1016/j.dnarep.2007.04.010. This article has 35 citations and is from a peer-reviewed journal.

  12. (稲田2024grr1mediatedubp3degradation pages 7-10): 利文 稲田, Nichika Sato, Shota Tomomatsu, Sihan Li, Yoshitaka Matsuo, Yu Nakano, and Yasuko Matsuki. Grr1-mediated ubp3 degradation is crucial for hac1 mrna translation and unfolded stress response in yeast. Unknown journal, Aug 2024. URL: https://doi.org/10.21203/rs.3.rs-4865151/v1, doi:10.21203/rs.3.rs-4865151/v1.

  13. (稲田2024grr1mediatedubp3degradation pages 18-24): 利文 稲田, Nichika Sato, Shota Tomomatsu, Sihan Li, Yoshitaka Matsuo, Yu Nakano, and Yasuko Matsuki. Grr1-mediated ubp3 degradation is crucial for hac1 mrna translation and unfolded stress response in yeast. Unknown journal, Aug 2024. URL: https://doi.org/10.21203/rs.3.rs-4865151/v1, doi:10.21203/rs.3.rs-4865151/v1.

  14. (vengayil2024thedeubiquitinaseubp3usp10 pages 1-2): Vineeth Vengayil, Shreyas Niphadkar, Swagata Adhikary, Sriram Varahan, and Sunil Laxman. The deubiquitinase ubp3/usp10 constrains glucose-mediated mitochondrial repression via phosphate budgeting. eLife, May 2024. URL: https://doi.org/10.7554/elife.90293, doi:10.7554/elife.90293. This article has 12 citations and is from a domain leading peer-reviewed journal.

  15. (vengayil2024thedeubiquitinaseubp3usp10 pages 3-4): Vineeth Vengayil, Shreyas Niphadkar, Swagata Adhikary, Sriram Varahan, and Sunil Laxman. The deubiquitinase ubp3/usp10 constrains glucose-mediated mitochondrial repression via phosphate budgeting. eLife, May 2024. URL: https://doi.org/10.7554/elife.90293, doi:10.7554/elife.90293. This article has 12 citations and is from a domain leading peer-reviewed journal.

  16. (vengayil2024thedeubiquitinaseubp3usp10 pages 9-10): Vineeth Vengayil, Shreyas Niphadkar, Swagata Adhikary, Sriram Varahan, and Sunil Laxman. The deubiquitinase ubp3/usp10 constrains glucose-mediated mitochondrial repression via phosphate budgeting. eLife, May 2024. URL: https://doi.org/10.7554/elife.90293, doi:10.7554/elife.90293. This article has 12 citations and is from a domain leading peer-reviewed journal.

  17. (vengayil2024thedeubiquitinaseubp3usp10 pages 15-17): Vineeth Vengayil, Shreyas Niphadkar, Swagata Adhikary, Sriram Varahan, and Sunil Laxman. The deubiquitinase ubp3/usp10 constrains glucose-mediated mitochondrial repression via phosphate budgeting. eLife, May 2024. URL: https://doi.org/10.7554/elife.90293, doi:10.7554/elife.90293. This article has 12 citations and is from a domain leading peer-reviewed journal.

  18. (vengayil2024thedeubiquitinaseubp3usp10 pages 14-15): Vineeth Vengayil, Shreyas Niphadkar, Swagata Adhikary, Sriram Varahan, and Sunil Laxman. The deubiquitinase ubp3/usp10 constrains glucose-mediated mitochondrial repression via phosphate budgeting. eLife, May 2024. URL: https://doi.org/10.7554/elife.90293, doi:10.7554/elife.90293. This article has 12 citations and is from a domain leading peer-reviewed journal.

  19. (vengayil2024thedeubiquitinaseubp3usp10 pages 17-18): Vineeth Vengayil, Shreyas Niphadkar, Swagata Adhikary, Sriram Varahan, and Sunil Laxman. The deubiquitinase ubp3/usp10 constrains glucose-mediated mitochondrial repression via phosphate budgeting. eLife, May 2024. URL: https://doi.org/10.7554/elife.90293, doi:10.7554/elife.90293. This article has 12 citations and is from a domain leading peer-reviewed journal.

  20. (vengayil2024thedeubiquitinaseubp3usp10 pages 6-7): Vineeth Vengayil, Shreyas Niphadkar, Swagata Adhikary, Sriram Varahan, and Sunil Laxman. The deubiquitinase ubp3/usp10 constrains glucose-mediated mitochondrial repression via phosphate budgeting. eLife, May 2024. URL: https://doi.org/10.7554/elife.90293, doi:10.7554/elife.90293. This article has 12 citations and is from a domain leading peer-reviewed journal.

  21. (vengayil2024thedeubiquitinaseubp3usp10 pages 8-9): Vineeth Vengayil, Shreyas Niphadkar, Swagata Adhikary, Sriram Varahan, and Sunil Laxman. The deubiquitinase ubp3/usp10 constrains glucose-mediated mitochondrial repression via phosphate budgeting. eLife, May 2024. URL: https://doi.org/10.7554/elife.90293, doi:10.7554/elife.90293. This article has 12 citations and is from a domain leading peer-reviewed journal.

  22. (lan2021deubiquitinaseubp3enhances pages 12-13): Qiuyan Lan, Yanchang Li, Fuqiang Wang, Zhaodi Li, Yuan Gao, Hui Lu, Yihao Wang, Zhenwen Zhao, Zixin Deng, Fuchu He, Junzhu Wu, and Ping Xu. Deubiquitinase ubp3 enhances the proteasomal degradation of key enzymes in sterol homeostasis. The Journal of Biological Chemistry, 296:100348, Jan 2021. URL: https://doi.org/10.1016/j.jbc.2021.100348, doi:10.1016/j.jbc.2021.100348. This article has 12 citations.

Artifacts

Citations

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  2. cohen2003deubiquitinationanew pages 1-1
  3. ossarehnazari2014ubiquitylationbythe pages 9-9
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