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.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target is the fission-yeast gene ulp2 (systematic locus SPAC17A5.07c), encoding ubiquitin-like-specific protease 2 in Schizosaccharomyces pombe strain 972. The organism-specific experimental literature identifies this protein as a SUMO/Pmt3-specific cysteine isopeptidase whose principal function is to remove SUMO from high-molecular-weight SUMO conjugates—probably including poly-SUMO chains—rather than to mature precursor SUMO. This biochemical behavior agrees with the supplied UniProt assignment to peptidase family C48 and its papain-like/SENP catalytic domain architecture. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7)
Ulp2 is found mainly in intranuclear foci, with a smaller cytoplasmic pool and little detectable nuclear-envelope localization. It participates in large protein assemblies and helps maintain SUMO-chain homeostasis in pathways involving SUMO-targeted ubiquitin ligases (STUbLs) and PP2A-Pab1B55. Its deletion is viable but produces severe growth and morphological abnormalities, accumulation of high-molecular-weight SUMO species, and sensitivity to heat, hydroxyurea, cycloheximide, and osmotic stress. A second experimentally supported context is association with RNA-processing, ribosome-biogenesis, and translation proteins, including SUMOylated eIF4G; however, eIF4G has not been proven to be a direct catalytic substrate of Ulp2. (nie2016functionalcrosstalkbetween pages 7-10, jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7, jongjitwimol2014thes.pombe pages 7-9)
The relevant literature explicitly studies S. pombe Ulp2, not merely a same-named protein from another organism. It describes Ulp2 as a fission-yeast SUMO-specific cysteine protease and compares it with S. pombe Ulp1 and with budding-yeast proteases only for evolutionary interpretation. Thus, the experimental target matches the supplied identity: ulp2 / SPAC17A5.07c / UniProt O13769, from Schizosaccharomyces pombe. The primary paper passages do not print the O13769 accession, so accession-to-locus mapping derives from the supplied UniProt record, while protein function and organism are independently concordant with the literature. (jongjitwimol2014thes.pombe pages 2-3, jongjitwimol2014thes.pombe pages 4-5)
The supplied annotations—peptidase C48, Peptidase_C48_C/PF02902, sentrin-specific protease, and a papain-like cysteine-peptidase fold—are fully consistent with the experimental result that purified Ulp2 is inhibited by the cysteine-reactive reagent N-ethylmaleimide and deconjugates SUMO. The literature therefore supports the family-level annotation experimentally, even though a structure of this specific protein was not identified in the retrieved corpus. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7)
The symbol ULP2 is also widely used for the Saccharomyces cerevisiae SUMO protease. Those proteins are homologous and share broad biochemical behavior, but results obtained only in budding yeast—such as particular centromeric, nucleolar, DDK, or cohesin substrates—must not be assigned directly to O13769. This report uses budding-yeast findings only as explicitly labeled orthology context, not as evidence for the fission-yeast protein.
The best-supported reaction is hydrolysis of the isopeptide bond connecting the C-terminal carboxyl group of SUMO/Pmt3 to a lysine side chain on a substrate or another SUMO molecule:
SUMO–substrate + H₂O → free SUMO + deSUMOylated substrate
For a SUMO chain, repeated cleavage shortens or dismantles the chain. Purified S. pombe Ulp2 removed SUMO from high-molecular-weight conjugates, and this activity was inhibited by 5 mM NEM, identifying it as cysteine-protease-dependent deSUMOylation. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7)
Ulp2 is substantially poorer than Ulp1 at processing precursor SUMO. In the reported assay, 2.32 µg Ulp2 had markedly less precursor-processing activity than 0.72 µg Ulp1, whereas Ulp2 efficiently depleted high-molecular-weight SUMO conjugates when tested over 0.6–4.8 µg. These results support deconjugation—and particularly disassembly of heavily SUMOylated species—as its principal physiological reaction rather than exposure of the mature SUMO C terminus. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7)
The strongest substrate assignment is a class, not a single named protein: Ulp2 preferentially acts on high-molecular-weight SUMO-containing species, consistent with multiply SUMOylated proteins and/or poly-SUMO chains. Loss of ulp2 slightly increased these species, and chain-deficient SUMO alleles suppress ulp2-deletion phenotypes, strengthening the conclusion that harmful SUMO-chain accumulation is physiologically relevant. (nie2016functionalcrosstalkbetween pages 7-10, jongjitwimol2014thes.pombe pages 4-5, nie2016functionalcrosstalkbetween pages 1-2)
No kinetic constants, linkage-specific cleavage rates, or complete substrate repertoire were reported. It is therefore premature to claim that O13769 exclusively recognizes a particular Pmt3-chain linkage or a defined sequence motif.
Immunofluorescence of genomically tagged Ulp2 showed predominantly nuclear foci, a smaller cytoplasmic component, frequent overlap with SUMO, and little if any signal at the nuclear periphery. Its distribution was broadly similar in S phase, early and late G2, and mitosis. This differs from S. pombe Ulp1, which is associated with nuclear pores for much of the cell cycle and relocalizes during mitosis. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7)
Accordingly, Ulp2 most likely carries out its principal SUMO-chain-editing function in the nucleoplasm or intranuclear bodies, rather than at nuclear pores. The minor cytoplasmic pool could support additional functions, but the available microscopy did not quantify nuclear/cytoplasmic partitioning or identify specific nuclear subcompartments.
Gel filtration supports localization within macromolecular assemblies: Ulp2 appeared both in the column void and in fractions corresponding to approximately 670 kDa, indicating at least two high-molecular-weight complexes. Most Ulp2 was not associated with actively translating polysomes because its sedimentation persisted after EDTA disrupted polysomes. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7, jongjitwimol2014thes.pombe pages 9-11)
The central pathway role is to restrain accumulation of high-molecular-weight or poly-SUMO conjugates. In fission yeast, excessive SUMO chains are associated with growth defects, genotoxic sensitivity, and genome instability; reducing chain formation suppresses phenotypes caused by loss of Ulp2. Ulp2 therefore acts as a corrective or editing enzyme that prevents SUMO-chain signaling from becoming excessive or persistent. (nie2016functionalcrosstalkbetween pages 7-10, nie2016functionalcrosstalkbetween pages 1-2)
Current SUMO biology places this reaction in balance with STUbLs, which recognize poly-SUMO-modified proteins and add ubiquitin, promoting extraction from complexes and/or proteasomal destruction. A 2024 review emphasizes that SUMO proteases tune or reverse SUMO-dependent events, while SUMO chains provide interaction scaffolds and STUbLs terminate or redirect those events during replication, repair, mitosis, and chromatin regulation. That review does not, however, directly analyze S. pombe Ulp2, so it supplies pathway context rather than protein-specific evidence. (thu2024multifacetedrolesof pages 14-15, thu2024multifacetedrolesof pages 1-2)
The S. pombe STUbL system comprises Rfp1/Rfp2 and Slx8. Genetic evidence indicates that reducing SUMO-chain abundance makes STUbL activity less critical, supporting a model in which both Ulp2 and STUbL prevent toxic persistence of poly-SUMO species through different biochemical routes: Ulp2 removes SUMO, whereas STUbL directs selected SUMOylated targets into ubiquitin-dependent processing. (nie2016functionalcrosstalkbetween pages 7-10, nie2016functionalcrosstalkbetween pages 1-2, chang2021sumotargetedubiquitinligases pages 11-12)
This is a pathway-level relationship; the retrieved studies did not establish a stable Ulp2–STUbL physical complex or identify a common named substrate whose fate was directly tracked through both systems.
A 2016 genetic study found that the hypomorphic pab1-1 allele, which reduces PP2A-Pab1B55 activity, strongly suppressed the hydroxyurea sensitivity of ulp2Δ cells. The double mutant showed a small but detectable reduction in high-molecular-weight SUMO conjugates relative to ulp2Δ alone. Pab1 overproduction had the opposite general effect, increasing high-molecular-weight SUMO conjugates, especially when STUbL function was compromised. (nie2016functionalcrosstalkbetween pages 13-14, nie2016functionalcrosstalkbetween pages 7-10)
The suppression was not explained simply by altered cell-cycle timing or generalized genotoxin resistance: pab1-1 failed to rescue several checkpoint, recombination, and replication-stress mutants. The most defensible interpretation is that PP2A-Pab1B55 influences SUMO-pathway output, directly or indirectly, thereby changing the burden placed on Ulp2 and STUbL. The precise PP2A substrate responsible remains unresolved. (nie2016functionalcrosstalkbetween pages 4-7, nie2016functionalcrosstalkbetween pages 7-10)
Affinity purification of Ulp2-TAP recovered many proteins involved in RNA synthesis and processing, ribosome biogenesis, translation initiation, and elongation. Examples included eIF2 and eIF3 subunits, eIF4G, elongation factors, PABP, Rrp5, Exo2, Dhp1, Upf1, Nop2, Dbp2, and Prp19; fewer DNA-metabolism proteins, including Rfc5, were also detected. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 7-9)
These observations indicate that Ulp2 occupies complexes connected to RNA and protein synthesis, but co-purification does not demonstrate direct binding or catalytic substrate status. The predominance of nuclear Ulp2 and lack of stable polysome association suggest that its translation-related role may involve nuclear RNA maturation, ribosome assembly, or regulation of translation factors before or outside active polysomes. (jongjitwimol2014thes.pombe pages 2-3, jongjitwimol2014thes.pombe pages 9-11)
Most eIF4G co-eluted with Ulp2, and denaturing His-SUMO pull-downs established that S. pombe eIF4G is SUMOylated in vivo. By contrast, eIF3h co-purified with Ulp2 but was not detectably SUMOylated, suggesting indirect association through the eIF3 complex. (jongjitwimol2014thes.pombe pages 5-7, jongjitwimol2014thes.pombe pages 7-9, jongjitwimol2014thes.pombe pages 9-11)
After 30 minutes in 1 M KCl, a stress that produces cytoplasmic stress granules, relative eIF4G SUMOylation rose from 1.0 to 1.5; treatment with cycloheximide left it at 1.0. eIF4G and SUMO occasionally colocalized in cytoplasmic stress granules, while a significant fraction of nuclear eIF4G overlapped SUMO under basal conditions. (jongjitwimol2014thes.pombe pages 7-9)
Nevertheless, eIF4G should be described only as a candidate Ulp2-regulated substrate. The study did not show increased eIF4G SUMOylation in ulp2Δ cells, direct cleavage of SUMO–eIF4G by purified Ulp2, or dependence of eIF4G localization or turnover on Ulp2. The authors explicitly left open whether SUMO directs eIF4G toward stress granules, altered interactions, or degradation. (jongjitwimol2014thes.pombe pages 11-12, jongjitwimol2014thes.pombe pages 7-9)
Disruption of ulp2 was not lethal, but mutant cells formed very small colonies and displayed pronounced morphological abnormalities. Cultures contained enough dead cells that approximately tenfold more mutant cells had to be plated than wild type in serial-dilution assays. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7)
The deletion strain was sensitive to:
These are assay conditions rather than formal effect sizes; no IC50 values, survival percentages, or catalytic rates were reported. The phenotypes are consistent with a broad failure of SUMO homeostasis but do not independently identify specific substrates.
The evidence is summarized below.
| Annotation aspect | Best-supported conclusion | Evidence type | Key experiment/statistic | Confidence/caveat |
|---|---|---|---|---|
| Identity/domain concordance | S. pombe ulp2 encodes a SUMO-specific cysteine protease consistent with O13769 and the supplied peptidase-C48/SENP-family annotation. | Organism-specific biochemical characterization and sequence comparison | Purified fission-yeast Ulp2 displayed NEM-sensitive SUMO-deconjugating activity, as expected for a cysteine SENP-family protease. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7) | High for protein class and identity; the examined paper passage does not explicitly state accession O13769. |
| Catalytic reaction | Ulp2 hydrolyzes the isopeptide linkage joining SUMO/Pmt3 to proteins or SUMO chains. Its principal role is deconjugation rather than precursor-SUMO maturation. | Purified-enzyme assays | Ulp2 removed SUMO from high-molecular-weight conjugates after 2 h at 20°C; 5 mM NEM inhibited activity. Even 2.32 µg Ulp2 processed precursor SUMO much less effectively than 0.72 µg Ulp1. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7) | High for deconjugation; EC 3.4.22.- is nonspecific, and kinetic constants were not reported. |
| Substrate preference | The best-supported substrate class is high-molecular-weight SUMO conjugates, including poly-SUMO-containing species; precursor SUMO is a poor substrate. | In vitro deconjugation, mutant conjugate profiles, and genetic chain-blocking evidence | Increasing purified Ulp2 from 0.6 to 4.8 µg depleted high-Mr SUMO species; ulp2Δ modestly increased those species, while chain-deficient SUMO suppressed ulp2Δ phenotypes. (nie2016functionalcrosstalkbetween pages 7-10, jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7) | High for substrate class; low–moderate for individual physiological substrates because direct turnover of a named substrate was not demonstrated. |
| Localization | Ulp2 occurs predominantly in intranuclear foci, with a smaller cytoplasmic pool; it is largely absent from the nuclear periphery and changes little across the cell cycle. | Immunofluorescence of genomically tagged protein | Ulp2-Myc foci were examined in S phase, early and late G2, and mitosis; many overlapped SUMO, whereas little or no nuclear-envelope signal was detected. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7) | High under the tested conditions; nuclear and cytoplasmic fractions were not quantified. |
| Complexes/interactors | Ulp2 resides in at least two large complexes and associates with proteins involved in RNA processing, ribosome biogenesis, translation, and, less prominently, DNA metabolism. | Gel filtration and Ulp2-TAP affinity purification followed by LC-MS/MS | Ulp2 eluted in the column void and near 670 kDa. Co-purifying proteins included eIF2/eIF3 subunits, eIF4G, elongation factors, PABP, Rrp5, Exo2, Dhp1, Upf1, Nop2, Prp19, and Rfc5. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7, jongjitwimol2014thes.pombe pages 7-9) | Moderate; co-elution and co-purification indicate shared complexes but not direct binding or substrate status. |
| eIF4G relationship | Fission-yeast eIF4G is SUMOylated and co-complexes with Ulp2, making it a candidate Ulp2-regulated protein. eIF3h associates with Ulp2 but was not detectably SUMOylated. | Gel filtration, denaturing His-SUMO pull-down, and microscopy | Most eIF4G co-eluted with Ulp2. After 30 min in 1 M KCl, relative eIF4G SUMOylation increased from 1.0 to 1.5; cycloheximide-treated cells remained at 1.0. (jongjitwimol2014thes.pombe pages 5-7, jongjitwimol2014thes.pombe pages 7-9) | Moderate for association; low for eIF4G as a direct Ulp2 substrate because Ulp2-dependent deSUMOylation was not demonstrated. |
| Stress/deletion phenotypes | ulp2 is nonessential under standard laboratory conditions, but deletion causes severe growth and morphological defects and sensitivity to heat, replication stress, translation inhibition, and osmotic stress. | Targeted deletion and serial-dilution growth assays | ulp2Δ formed very small colonies; approximately 10-fold more mutant cells had to be plated. Sensitivity occurred with 2 mM HU, 10–20 mg/ml cycloheximide, and 1 M KCl. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7) | High for phenotypes; assay concentrations are not quantitative effect sizes, and pleiotropy does not identify a unique substrate. |
| SUMO-chain/STUbL/PP2A pathway | Ulp2 restricts harmful high-Mr or poly-SUMO accumulation and interacts genetically with the Rfp1/Rfp2-Slx8 STUbL system and PP2A-Pab1B55 regulation of SUMO output. | Genetic suppression and SUMO immunoblotting | Hypomorphic pab1-1 strongly suppressed ulp2Δ HU sensitivity and produced a small but detectable reduction in high-Mr SUMO species; chain-deficient SUMO alleles also suppressed ulp2Δ phenotypes. (nie2016functionalcrosstalkbetween pages 7-10, nie2016functionalcrosstalkbetween pages 1-2) | High for genetic interaction; moderate for mechanism because PP2A may affect SUMO-chain abundance directly or indirectly. |
| Recent-literature status | No retrieved 2023–2024 peer-reviewed primary study directly advanced annotation of O13769. A September 2024 review supports the general SUMO-protease and STUbL framework but does not specifically analyze S. pombe Ulp2. | Targeted recent-literature search and authoritative review synthesis | The latest direct protein-specific evidence retrieved was chiefly from 2014 and 2016; the 2024 review addresses SUMO chains, STUbLs, DNA repair, replication, and mitosis. (thu2024multifacetedrolesof pages 14-15, thu2024multifacetedrolesof pages 1-2) | High for the retrieved-corpus assessment, but this does not prove that no other relevant publication exists; budding-yeast findings remain orthology context only. |
Table: Compact evidence assessment for Schizosaccharomyces pombe Ulp2/O13769, separating direct biochemical and cellular results from pathway inference and unresolved substrate assignments. Findings from budding-yeast Ulp2 are not treated as direct evidence.
The most parsimonious model is that S. pombe Ulp2 is a nuclear SUMO-chain editor. Its catalytic C48/SENP domain hydrolyzes SUMO isopeptide linkages on highly modified proteins or chains. This limits both direct poly-SUMO signaling and the production of substrates recognized by STUbLs. By controlling the lifetime of these conjugates in large nuclear assemblies, Ulp2 supports genome maintenance, stress tolerance, RNA metabolism, and ribosome/translation-factor regulation. (nie2016functionalcrosstalkbetween pages 7-10, jongjitwimol2014thes.pombe pages 4-5, thu2024multifacetedrolesof pages 14-15, nie2016functionalcrosstalkbetween pages 1-2)
The genome-stability and RNA/translation observations are not mutually exclusive. SUMOylation often regulates groups of physically associated proteins rather than isolated substrates, and SUMO chains can act as scaffolds for SUMO-interacting proteins. Consequently, loss of one chain-editing protease can perturb multiple large assemblies without implying that every co-purifying protein is an Ulp2 substrate. (thu2024multifacetedrolesof pages 14-15, thu2024multifacetedrolesof pages 1-2)
Claims that Ulp2 directly regulates fission-yeast condensin, cohesin, centromeres, DDK, or particular nucleolar factors remain insufficiently supported by the retrieved S. pombe-specific evidence. Many precise examples in these areas derive from S. cerevisiae Ulp2 or mammalian SENP6/7 and should be tested directly before transfer to O13769.
A targeted search retrieved no 2023–2024 peer-reviewed primary study that directly advanced the molecular annotation of O13769/SPAC17A5.07c. The most recent direct protein-specific studies recovered here are principally the 2014 biochemical/localization/interactome paper and the 2016 PP2A–SUMO genetic study.
The main relevant 2024 development is a broad review published in September 2024, which integrates SUMO proteases, SUMO chains, and STUbLs across DNA replication, repair, mitosis, and chromatin biology. It reinforces the contemporary view that SUMO chains are dynamic interaction platforms and that proteases and STUbLs jointly determine their duration and outcome, but it does not provide new direct evidence about S. pombe Ulp2. (thu2024multifacetedrolesof pages 14-15, thu2024multifacetedrolesof pages 1-2)
A 2024 doctoral thesis on SUMOylation, centromere biology, and replication-fork restart in S. pombe appeared in the search results, but full text was unavailable through the retrieval system; it was therefore not used as evidence. This limitation is preferable to importing detailed conclusions from a same-named budding-yeast protein.
There is no established clinical, industrial, or agricultural application specific to S. pombe Ulp2. Its current practical value is as a research-system component for:
The ulp2Δ strain’s strong but viable phenotypes make it experimentally useful for suppressor screens, chemical-genetic assays, and quantitative SUMO-proteomics. Translational relevance lies in conserved pathway logic—SENP/STUbL regulation and genome stability—not in direct therapeutic targeting of the yeast protein.
Molecular function: SUMO/Pmt3-specific cysteine isopeptidase; preferentially deconjugates SUMO from high-molecular-weight, likely poly-SUMO-containing conjugates; weak precursor-SUMO-processing activity.
Biological process: maintenance of SUMO-chain homeostasis; protection against replication/genotoxic stress; functional coordination with the Rfp1/Rfp2–Slx8 STUbL and PP2A-Pab1B55 pathways; probable regulation of nuclear RNA-processing, ribosome-biogenesis, and translation-factor assemblies.
Cellular component: predominantly intranuclear foci/high-molecular-weight nuclear complexes, with a minor cytoplasmic pool; little or no nuclear-pore localization.
Best-supported substrate class: high-molecular-weight SUMO conjugates/poly-SUMO species.
Candidate named substrate: eIF4G, based on SUMOylation and shared complexes, but direct Ulp2-dependent deSUMOylation remains unproven.
Jongjitwimol J. et al. “The S. pombe Translation Initiation Factor eIF4G Is Sumoylated and Associates with the SUMO Protease Ulp2.” PLOS ONE 9:e94182. Published May 2014. https://doi.org/10.1371/journal.pone.0094182. Principal source for catalytic activity, localization, complexes, deletion phenotypes, and eIF4G association. (jongjitwimol2014thes.pombe pages 4-5, jongjitwimol2014thes.pombe pages 5-7, jongjitwimol2014thes.pombe pages 7-9, jongjitwimol2014thes.pombe pages 9-11)
Nie M. et al. “Functional Crosstalk between the PP2A and SUMO Pathways Revealed by Analysis of STUbL Suppressor, razor 1-1.” PLOS Genetics 12:e1006165. Published 11 July 2016. https://doi.org/10.1371/journal.pgen.1006165. Principal source for PP2A-Pab1B55 suppression, SUMO-chain burden, and Ulp2/STUbL pathway relationships. (nie2016functionalcrosstalkbetween pages 13-14, nie2016functionalcrosstalkbetween pages 4-7, nie2016functionalcrosstalkbetween pages 7-10, nie2016functionalcrosstalkbetween pages 1-2)
Thu YM. “Multifaceted roles of SUMO in DNA metabolism.” Nucleus 15. Published September 2024. https://doi.org/10.1080/19491034.2024.2398450. Current general review of SUMO chains, proteases, STUbLs, and genome maintenance; not direct evidence for S. pombe Ulp2. (thu2024multifacetedrolesof pages 14-15, thu2024multifacetedrolesof pages 1-2)
O13769 is correctly annotated as the S. pombe Ulp2 SUMO-specific protease. Its experimentally established primary function is cysteine-dependent hydrolysis of SUMO isopeptide bonds, with preference for high-molecular-weight SUMO conjugates rather than SUMO-precursor maturation. It works mainly in nuclear foci and large complexes, where it constrains potentially toxic SUMO-chain accumulation and interfaces genetically with STUbL and PP2A-dependent control. Associations with RNA-processing, ribosome-biogenesis, and translation proteins—especially SUMOylated eIF4G—extend its likely functional scope, but named physiological substrates remain incompletely validated. The major annotation gap is therefore not enzyme class or localization, but precise substrate identity, chain-linkage preference, and complex-specific recruitment mechanisms.
References
(jongjitwimol2014thes.pombe pages 4-5): Jirapas Jongjitwimol, Min Feng, Lihong Zhou, Oliver Wilkinson, Lauren Small, Robert Baldock, Deborah L. Taylor, Duncan Smith, Lucas D. Bowler, Simon J. Morley, and Felicity Z. Watts. The s. pombe translation initiation factor eif4g is sumoylated and associates with the sumo protease ulp2. PLoS ONE, 9:e94182, May 2014. URL: https://doi.org/10.1371/journal.pone.0094182, doi:10.1371/journal.pone.0094182. This article has 15 citations and is from a peer-reviewed journal.
(jongjitwimol2014thes.pombe pages 5-7): Jirapas Jongjitwimol, Min Feng, Lihong Zhou, Oliver Wilkinson, Lauren Small, Robert Baldock, Deborah L. Taylor, Duncan Smith, Lucas D. Bowler, Simon J. Morley, and Felicity Z. Watts. The s. pombe translation initiation factor eif4g is sumoylated and associates with the sumo protease ulp2. PLoS ONE, 9:e94182, May 2014. URL: https://doi.org/10.1371/journal.pone.0094182, doi:10.1371/journal.pone.0094182. This article has 15 citations and is from a peer-reviewed journal.
(nie2016functionalcrosstalkbetween pages 7-10): Minghua Nie, Emily Arner, John Prudden, Lana Schaffer, Steven Head, and Michael N. Boddy. Functional crosstalk between the pp2a and sumo pathways revealed by analysis of stubl suppressor, razor 1-1. Jul 2016. URL: https://doi.org/10.1371/journal.pgen.1006165, doi:10.1371/journal.pgen.1006165. This article has 4 citations and is from a domain leading peer-reviewed journal.
(jongjitwimol2014thes.pombe pages 7-9): Jirapas Jongjitwimol, Min Feng, Lihong Zhou, Oliver Wilkinson, Lauren Small, Robert Baldock, Deborah L. Taylor, Duncan Smith, Lucas D. Bowler, Simon J. Morley, and Felicity Z. Watts. The s. pombe translation initiation factor eif4g is sumoylated and associates with the sumo protease ulp2. PLoS ONE, 9:e94182, May 2014. URL: https://doi.org/10.1371/journal.pone.0094182, doi:10.1371/journal.pone.0094182. This article has 15 citations and is from a peer-reviewed journal.
(jongjitwimol2014thes.pombe pages 2-3): Jirapas Jongjitwimol, Min Feng, Lihong Zhou, Oliver Wilkinson, Lauren Small, Robert Baldock, Deborah L. Taylor, Duncan Smith, Lucas D. Bowler, Simon J. Morley, and Felicity Z. Watts. The s. pombe translation initiation factor eif4g is sumoylated and associates with the sumo protease ulp2. PLoS ONE, 9:e94182, May 2014. URL: https://doi.org/10.1371/journal.pone.0094182, doi:10.1371/journal.pone.0094182. This article has 15 citations and is from a peer-reviewed journal.
(nie2016functionalcrosstalkbetween pages 1-2): Minghua Nie, Emily Arner, John Prudden, Lana Schaffer, Steven Head, and Michael N. Boddy. Functional crosstalk between the pp2a and sumo pathways revealed by analysis of stubl suppressor, razor 1-1. Jul 2016. URL: https://doi.org/10.1371/journal.pgen.1006165, doi:10.1371/journal.pgen.1006165. This article has 4 citations and is from a domain leading peer-reviewed journal.
(jongjitwimol2014thes.pombe pages 9-11): Jirapas Jongjitwimol, Min Feng, Lihong Zhou, Oliver Wilkinson, Lauren Small, Robert Baldock, Deborah L. Taylor, Duncan Smith, Lucas D. Bowler, Simon J. Morley, and Felicity Z. Watts. The s. pombe translation initiation factor eif4g is sumoylated and associates with the sumo protease ulp2. PLoS ONE, 9:e94182, May 2014. URL: https://doi.org/10.1371/journal.pone.0094182, doi:10.1371/journal.pone.0094182. This article has 15 citations and is from a peer-reviewed journal.
(thu2024multifacetedrolesof pages 14-15): Yee Mon Thu. Multifaceted roles of sumo in dna metabolism. Nucleus, Sep 2024. URL: https://doi.org/10.1080/19491034.2024.2398450, doi:10.1080/19491034.2024.2398450. This article has 5 citations and is from a peer-reviewed journal.
(thu2024multifacetedrolesof pages 1-2): Yee Mon Thu. Multifaceted roles of sumo in dna metabolism. Nucleus, Sep 2024. URL: https://doi.org/10.1080/19491034.2024.2398450, doi:10.1080/19491034.2024.2398450. This article has 5 citations and is from a peer-reviewed journal.
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