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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 human ASCC2 (UniProt Q9H1I8), annotated as Activating Signal Cointegrator 1 Complex Subunit 2 (also called ASC-1 complex subunit p100; gene symbol ASCC2, synonym RQT3) and characterized by a CUE ubiquitin-binding domain and participation in the ASCC/ASC-1 complex and the ribosome quality control trigger (hRQT/RQT) module. This identity (name, organism, and domain/function context) is consistently matched by peer‑reviewed primary literature on the ASCC complex in DNA alkylation repair and ribosome-associated quality control (RQC). (lombardi2022theascc2cue pages 1-2, jia2020theinteractionof pages 4-5, hashimoto2020identificationofa pages 1-2)
ASCC (Activating Signal Co‑integrator Complex; sometimes discussed with the older “ASC-1” terminology) is a multi‑subunit assembly involved in multiple nucleic-acid–linked stress responses. ASCC2 functions as a ubiquitin-sensing adaptor within ASCC, coupling K63‑linked ubiquitin signaling to downstream actions of the ASCC motor subunit ASCC3 (a Ski2-like helicase) and, in DNA repair contexts, to the dioxygenase ALKBH3. (soll2018rnaligaselikedomain pages 1-2, fahrer2023dnaalkylationdamage pages 12-14)
A key organizing principle is that ASCC2 binds ASCC3 with very high affinity, enabling ASCC2’s ubiquitin recognition to be physically transmitted to an ASCC3-driven remodeling activity (DNA unwinding or ribosome splitting, depending on context). (jia2020theinteractionof pages 4-5, jia2020theinteractionof pages 3-4)
ASCC2 contains a CUE domain (≈50 aa, a three‑helix bundle) that binds ubiquitin. Detailed structural/biophysical work shows ASCC2’s CUE domain has strong preference for K63‑linked diubiquitin (K63Ub2) over monoubiquitin, K48Ub2, or linear (M1) diubiquitin, and achieves linkage preference by contacting both distal and proximal ubiquitin moieties in K63Ub2. (lombardi2022theascc2cue pages 1-2, lombardi2022theascc2cue pages 2-4)
Mechanistically, conserved hydrophobic motifs (including L479 and L506) contribute to canonical ubiquitin binding, while an additional interaction surface in the N‑terminal part of helix α1 (including E467 and S470) strengthens K63Ub2 binding and is important for cellular recruitment to alkylation‑damage foci. (lombardi2022theascc2cue pages 4-7, lombardi2022theascc2cue pages 2-4)
In mammalian RQC, stalled ribosomes are marked by ZNF598‑dependent ubiquitination of small‑subunit ribosomal proteins (notably uS10/eS10). The ASC-1/ASCC machinery then promotes ribosome dissociation (splitting). In this context, ASCC2 acts as a key ubiquitin recognition component that helps recruit/activate the ASCC splitting machinery on ubiquitinated ribosomes. (ford2024ubiquitindependenttranslationcontrol pages 4-6, hashimoto2020identificationofa pages 5-7)
Alkylating agents create cytotoxic N‑alkyl lesions such as N1‑methyladenine (N1‑MeA) and N3‑methylcytosine (N3‑MeC) that can be repaired by AlkB family dioxygenases. ALKBH3 acts preferentially on single‑stranded nucleic acid substrates, creating a mechanistic requirement for an unwind/ssDNA‑generating activity. The ASCC helicase ASCC3 supplies this activity, while ASCC2 provides ubiquitin-based targeting. (fahrer2023dnaalkylationdamage pages 12-14, jia2020theinteractionof pages 1-2)
Primary studies support a model in which RNF113A-dependent K63-linked ubiquitin signaling recruits ASCC2 (via its CUE domain) to alkylation-damage foci, and ASCC2 is required for robust recruitment of ASCC3 and ALKBH3 to these nuclear foci. Loss of ASCC2 increases sensitivity to alkylating agents, consistent with a functional requirement in damage tolerance/repair. (soll2018rnaligaselikedomain pages 1-2, brickner2019activationandregulation pages 139-144)
A 2023 review of alkylation damage repair explicitly places ASCC2 as the ubiquitin-binding ASCC subunit that mediates recruitment of the ASCC machinery to transcription-linked alkylation lesions and enables ASCC3-driven unwinding to generate ssDNA for ALKBH3 access. (fahrer2023dnaalkylationdamage pages 12-14)
The ASCC2 CUE domain recognizes adjacent ubiquitins in K63Ub2, providing a plausible biochemical basis for preferential recruitment to K63-polyubiquitinated damage-associated substrates. Mutations in the α1 helix interface (e.g., E467R/S470R) reduce recruitment of ASCC2 to alkylation-damage foci in cells, functionally linking K63Ub2 binding to nuclear targeting. (lombardi2022theascc2cue pages 4-7)
ASCC2’s N-terminal region (residues 1–434) forms the principal ASCC3-binding module and is clasped by the ASCC3 N-terminal arms. Specific conserved ASCC3 residues (e.g., R5, R11) form salt bridges/hydrogen bonds with ASCC2 acidic residues, explaining the strong and evolutionarily conserved interaction. (jia2020theinteractionof pages 4-5, jia2020theinteractionof pages 3-4)
In mammalian RQC, ZNF598 marks stalled ribosomal complexes by polyubiquitinating uS10/eS10 (often K63-linked). The ASCC machinery then splits ribosomes to enable downstream processing such as nascent-chain ubiquitination. (miscicka2024ribosomalcollisionis pages 1-1, ford2024ubiquitindependenttranslationcontrol pages 4-6)
Hashimoto et al. identify a mammalian hRQT complex composed of ASCC3, ASCC2, and TRIP4 and provide functional evidence that ASCC2’s ubiquitin-binding activity is crucial for RQC induction (with partial phenotypes upon knockdown/mutation), consistent with ASCC2 acting as an ubiquitin-dependent recognition factor upstream of ASCC3 motor action. (hashimoto2020identificationofa pages 1-2, hashimoto2020identificationofa pages 3-5)
A 2024 expert review summarizes a key mechanistic consensus: ubiquitin on uS10/eS10 recruits ASC-1/RQT via ASCC2 ubiquitin binding, and ubiquitin-binding–deficient ASCC2 fails to support splitting in vitro, even if in vivo results differ across systems (partial dispensability in some cellular assays). (ford2024ubiquitindependenttranslationcontrol pages 4-6, ford2024ubiquitindependenttranslationcontrol pages 2-4)
Miścicka et al. (2024) provide an in vitro reconstitution perspective showing that ribosome collision is not strictly required for ZNF598-mediated ubiquitination or for ASCC-mediated disassembly. Instead, ASCC can split a broad range of complexes—including stalled polysomal queues, monosomes, and even ubiquitinated 48S initiation complexes—provided two core conditions are met:
Additionally, ZNF598-generated ubiquitination is quantitatively characterized in stalled polysomes: with WT/K63-only ubiquitin, ZNF598 produces near-complete polyubiquitination of eS10 and about ~90% polyubiquitination of uS10, whereas K63R ubiquitin yields only 1–4 ubiquitin attachments, and splitting efficiency correspondingly decreases. (miscicka2024ribosomalcollisionis pages 6-7, miscicka2024ribosomalcollisionis pages 8-9)
ASCC2 participates in both nuclear and cytoplasmic pathways:
These dual roles are consistent with ASCC2 operating as a shared ubiquitin-sensing module that targets the same ASCC3 motor core to distinct substrates (damaged transcription-associated nucleic acids vs ubiquitinated ribosomes). (jia2023extendeddnathreading pages 2-3)
Jia et al. (2023) emphasize that ASCC3 can form distinct functional sub-complexes: TRIP4 and ALKBH3 bind ASCC3 mutually exclusively, supporting a model where ASCC3 is directed to either RQC-related functions (TRIP4-containing RQT complex) or DNA alkylation repair (ALKBH3-containing repair complex). ASCC2 is present in both the canonical ASCC and the RQT complex and is explicitly described as containing a K63-linked ubiquitin chain-binding CUE domain, aligning ASCC2’s biochemical specialization with pathway selection by ubiquitin signals. (jia2023extendeddnathreading pages 2-3)
The Miścicka et al. (2024) study provides experimentally defined rules (mRNA length and ubiquitin-chain requirements) that sharpen the mechanistic understanding of how ASCC (and, by extension, ASCC2’s ubiquitin recognition) triggers ribosome splitting across multiple ribosomal states. (miscicka2024ribosomalcollisionis pages 1-1, miscicka2024ribosomalcollisionis pages 12-13)
Ford et al. (2024) then integrate these mechanistic insights into a broader framework of ubiquitin-dependent translation control, including the role of ASCC2’s CUE domain in recruiting the splitting machinery to ubiquitylated uS10/eS10. (ford2024ubiquitindependenttranslationcontrol pages 4-6)
Because ASCC2 is required for effective recruitment of ALKBH3–ASCC to alkylation lesions and alkylation tolerance, ASCC2 (and especially the ASCC2–ASCC3 interface and CUE domain) is conceptually relevant to cancer cell responses to alkylating DNA damage (including clinically used alkylating agents). Mechanistic cancer-mutation studies explicitly connect reduced ASCC2–ASCC3 affinity to a plausible weakening of alkylation repair at nuclear foci. (jia2020theinteractionof pages 9-10, soll2018rnaligaselikedomain pages 1-2)
However, direct clinical implementation (e.g., validated ASCC2 biomarker assays in routine care) was not demonstrated in the retrieved primary sources.
ASCC2’s participation in RQC suggests a role in proteostasis and stress responses, which is frequently implicated in neurodegeneration. OpenTargets reports ASCC2 associations with neurodegenerative disease and diabetes traits largely through GWAS credible sets and a neuronal CRISPRi screen implicating lipid peroxidation phenotypes, but these represent hypothesis-generating associations rather than established clinical use. (OpenTargets Search: -ASCC2)
A pan-cancer analysis across 10,967 tumors reports ASCC2 altered in ~1.8% of patients, with certain tumor-type enrichments (e.g., endometrial cancer >5%), and notes survival associations (e.g., ACC OS p=0.016; DFS associations in ACC/STAD/THYM). The same study also reports tumor-specific ASCC2 phosphorylation changes (e.g., T157 hyperphosphorylation across multiple tumors), which could be explored as biomarkers, although causal mechanisms remain unclear. (pan2025pancanceranalysisreveals pages 2-3, pan2025pancanceranalysisreveals pages 3-5)
A prostate cancer ceRNA study proposes that ASCC2 can sit downstream of an lncRNA/miRNA axis (TCONS_00027385/miR-874-5p/ASCC2) affecting proliferation and apoptosis, implying possible biomarker/target hypotheses in that cancer type; this evidence is preprint-level and should be treated cautiously. (han2021longnoncodingrna pages 1-5)
Across DNA repair and RQC contexts, the strongest mechanistic consensus is that ASCC2’s primary biochemical specialization is ubiquitin binding with K63 linkage preference, positioning ASCC2 as the “reader” that couples a K63-ubiquitin signal to deployment of the ASCC3 motor (DNA unwinding or ribosome splitting). This is supported by direct CUE-domain binding biophysics and by functional recruitment phenotypes, and reiterated by recent review synthesis in the RQC field. (lombardi2022theascc2cue pages 2-4, ford2024ubiquitindependenttranslationcontrol pages 4-6)
The ASCC2–ASCC3 interface is exceptionally tight (nanomolar) and structurally conserved; cancer-associated substitutions that weaken this interface are proposed to disrupt proper localization at nuclear damage foci (without necessarily changing ASCC3’s intrinsic helicase activity), providing a concrete “molecular disease principle” (loss of scaffold coupling rather than catalytic inactivity). (jia2020theinteractionof pages 4-5, jia2020theinteractionof pages 9-10)
Authoritative review synthesis highlights a tension: some cellular rescue studies suggest partial dispensability of ASCC2’s CUE domain in vivo, while biochemical splitting assays support a strong requirement for ASCC2 ubiquitin recognition for recruitment/splitting. A parsimonious interpretation is context dependence (cell type, stall substrate, ubiquitin architecture), which aligns with reconstitution results showing chain length/linkage and mRNA geometry constraints. (ford2024ubiquitindependenttranslationcontrol pages 2-4, miscicka2024ribosomalcollisionis pages 12-13)
| Functional module/process | ASCC2 molecular role | Key interacting partners | Subcellular localization | Key mechanistic details | Quantitative data | Key citations |
|---|---|---|---|---|---|---|
| DNA alkylation damage response | Ubiquitin-binding adaptor/sensor in the ALKBH3–ASCC repair pathway; recruits/helps recruit ASCC3 and ALKBH3 to alkylation-damage foci through its CUE domain (brickner2019activationandregulation pages 139-144, lombardi2022theascc2cue pages 1-2, fahrer2023dnaalkylationdamage pages 12-14) | ASCC3, ALKBH3, RNF113A-dependent K63-polyubiquitin, spliceosomal factors including BRR2/PRP8; broader ASCC complex includes ASCC1 and TRIP4/ASC1 (brickner2019activationandregulation pages 139-144, soll2019theroleof pages 27-34, soll2018rnaligaselikedomain pages 1-2, fahrer2023dnaalkylationdamage pages 12-14, jia2020theinteractionof pages 1-2) | Predominantly cytoplasmic at steady state, then accumulates in the nucleus and forms nuclear foci after alkylation stress; foci co-localize with K63-Ub, elongating RNA Pol II, and spliceosomal proteins (brickner2019activationandregulation pages 139-144, soll2019theroleof pages 90-95, soll2019theroleof pages 27-34) | ASCC2 CUE domain (aa ~465–521; UniProt domain annotation consistent) preferentially recognizes K63-linked polyubiquitin; N-terminal region of ASCC2 (aa 1–434) binds ASCC3 N-terminus, positioning ASCC3 to help generate ssDNA for ALKBH3 access to lesions such as N1-methyladenine and N3-methylcytosine during transcription-associated repair (lombardi2022theascc2cue pages 4-7, lombardi2022theascc2cue pages 1-2, lombardi2022theascc2cue pages 2-4, jia2020theinteractionof pages 4-5, fahrer2023dnaalkylationdamage pages 12-14) | Kd: monoubiquitin 57.1 ± 5.0 μM; K63-Ub2 8.7–10.4 μM for isolated CUE and 8.8 ± 0.9 μM for full-length ASCC2; K48-Ub2 ~98 μM; linear diUb ~400 μM; E467A weakens binding 3.6–5.0× (Kd ~46.9–65.4 μM); S470R Kd ~90.9 ± 23.1 μM; E467R/S470R Kd ~92.6 ± 20.9 μM; ASCC2(1–434)-ASCC3(1–197) Kd 3.8 ± 1.2 nM; full-length ASCC2-ASCC3 NTR Kd 3.5 ± 0.4 nM (lombardi2022theascc2cue pages 4-7, lombardi2022theascc2cue pages 1-2, lombardi2022theascc2cue pages 2-4, jia2020theinteractionof pages 4-5, jia2020theinteractionof pages 3-4, jia2020theinteractionof pages 5-6) | Lombardi et al., 2022, J Biol Chem, https://doi.org/10.1016/j.jbc.2021.101545; Jia et al., 2020, Nat Commun, https://doi.org/10.1038/s41467-020-19221-x; Fahrer & Christmann, 2023, Int J Mol Sci, https://doi.org/10.3390/ijms24054684 (lombardi2022theascc2cue pages 1-2, jia2020theinteractionof pages 4-5, fahrer2023dnaalkylationdamage pages 12-14) |
| Ribosome-associated quality control (RQC) / hRQT | Ubiquitin-recognition subunit of the mammalian hRQT/ASCC ribosome-splitting machinery; helps target ASCC3/TRIP4 to ubiquitinated stalled ribosomes (hashimoto2020identificationofa pages 5-7, hashimoto2020identificationofa pages 3-5, hashimoto2020identificationofa pages 1-2) | ASCC3, TRIP4; upstream ZNF598-dependent K63-linked ubiquitination on small-subunit proteins (reported in Hashimoto for eS10; Miścicka shows ZNF598-dependent uS10/eS10 ubiquitination supports ASCC activity) (hashimoto2020identificationofa pages 3-5, hashimoto2020identificationofa pages 1-2, miscicka2024ribosomalcollisionis pages 11-12) | Cytoplasmic/ribosome-associated functional context; acts on stalled 80S monosomes, polysomes, and even 48S complexes once appropriately ubiquitinated (hashimoto2020identificationofa pages 5-7, miscicka2024ribosomalcollisionis pages 11-12) | hRQT is composed of ASCC3-ASCC2-TRIP4; ASCC2 ubiquitin-binding activity is required/crucial for efficient RQC, while ASCC3 ATPase/helicase activity powers subunit dissociation. Recent reconstitution work shows ASCC can dissociate ubiquitinated ribosomal complexes without obligatory ribosome collision, provided ZNF598-dependent K63-linked ubiquitination and sufficient mRNA extension are present (hashimoto2020identificationofa pages 5-7, hashimoto2020identificationofa pages 3-5, hashimoto2020identificationofa pages 1-2, miscicka2024ribosomalcollisionis pages 11-12) | Functional KD evidence: ASCC3 KD abolishes RQC; ASCC2 KD partially impairs RQC; TRIP4 KD partially impairs RQC; ASCC1 not required (hashimoto2020identificationofa pages 2-3). Miścicka 2024: ASCC can dissociate complexes with ≥30–35 nt 3' mRNA downstream of the P site; polysome stalling assays used 39 A residues/13 AAA Lys codons; ZNF598 generated near-complete eS10 and ~90% uS10 polyubiquitination with WT/K63-only Ub, whereas K63R Ub yielded only 1–4 Ub attachments (miscicka2024ribosomalcollisionis pages 11-12, miscicka2024ribosomalcollisionis pages 6-7) | Hashimoto et al., 2020, Sci Rep, https://doi.org/10.1038/s41598-020-60241-w; Miścicka et al., 2024, Nucleic Acids Res, https://doi.org/10.1093/nar/gkae087 (hashimoto2020identificationofa pages 5-7, hashimoto2020identificationofa pages 1-2, miscicka2024ribosomalcollisionis pages 11-12, miscicka2024ribosomalcollisionis pages 6-7) |
| ASCC2–ASCC3 structural module relevant to both pathways | High-affinity scaffold interface that physically links the ubiquitin-sensing ASCC2 subunit to the ASCC3 motor/helicase subunit, enabling downstream DNA-repair and ribosome-quality-control activities (jia2020theinteractionof pages 9-10, jia2020theinteractionof pages 4-5, jia2020theinteractionof pages 3-4) | ASCC3 N-terminal region (especially first ~16 aa and broader 1–197/207 region); cancer-associated substitutions in both ASCC2 and ASCC3 map to the interface (jia2020theinteractionof pages 4-5, jia2020theinteractionof pages 1-2, jia2020theinteractionof pages 10-11) | Applicable to nuclear DNA-damage complexes and cytoplasmic hRQT/ribosome complexes because the same ASCC2–ASCC3 core interaction is reused across functions (jia2020theinteractionof pages 10-11) | ASCC2(1–434) forms a compact helical unit clasped by ASCC3(1–207); ASCC3 R5 and R11 contact acidic residues in ASCC2 (D103, D63, D92). The interface is evolutionarily conserved, and cancer mutations can weaken or abolish binding, suggesting disease-relevant destabilization of the core module (jia2020theinteractionof pages 4-5, jia2020theinteractionof pages 3-4, jia2020theinteractionof pages 1-2) | ASCC3 minimal 1–22 peptide binds ASCC2(1–434) with Kd 2.0 μM; ASCC2(1–434)-ASCC3(1–161) Kd 47.7 ± 14.9 nM; truncation of ASCC3 N-terminus to aa 16–197 weakens to 483.0 ± 260.2 nM; deleting the N-arm abolishes detectable binding; ASCC3 R5L/G weaken affinity ~8–11×, R5H/C >20×, and R11H/C abolish binding (jia2020theinteractionof pages 4-5, jia2020theinteractionof pages 3-4, jia2020theinteractionof pages 5-6) | Jia et al., 2020, Nat Commun, https://doi.org/10.1038/s41467-020-19221-x; Jia et al., 2023, Nat Commun, https://doi.org/10.1038/s41467-023-37528-3 (context mainly for ASCC3/TRIP4 module update) (jia2020theinteractionof pages 9-10, jia2020theinteractionof pages 4-5, jia2020theinteractionof pages 3-4, jia2020theinteractionof pages 5-6) |
Table: This table summarizes the best-supported functional annotation for human ASCC2 across its two main mechanistic contexts: DNA alkylation repair and ribosome-associated quality control. It highlights domain function, partners, localization, mechanism, and quantitative measurements from primary studies, with 2023-2024 sources emphasized where available.
Key recent/authoritative sources used:
Foundational mechanistic sources:
Disease/target association platform:
References
(lombardi2022theascc2cue pages 1-2): Patrick M. Lombardi, Sara Haile, Timur Rusanov, Rebecca Rodell, Rita Anoh, Julia G. Baer, Kate A. Burke, Lauren N. Gray, Abigail R. Hacker, Kayla R. Kebreau, Christine K. Ngandu, Hannah A. Orland, Emmanuella Osei-Asante, Dhane P. Schmelyun, Devin E. Shorb, Shaheer H. Syed, Julianna M. Veilleux, Ananya Majumdar, Nima Mosammaparast, and Cynthia Wolberger. The ascc2 cue domain in the alkbh3–ascc dna repair complex recognizes adjacent ubiquitins in k63-linked polyubiquitin. Journal of Biological Chemistry, 298:101545, Feb 2022. URL: https://doi.org/10.1016/j.jbc.2021.101545, doi:10.1016/j.jbc.2021.101545. This article has 11 citations and is from a domain leading peer-reviewed journal.
(jia2020theinteractionof pages 4-5): Junqiao Jia, Eva Absmeier, Nicole Holton, Agnieszka J. Pietrzyk-Brzezinska, Philipp Hackert, Katherine E. Bohnsack, Markus T. Bohnsack, and Markus C. Wahl. The interaction of dna repair factors ascc2 and ascc3 is affected by somatic cancer mutations. Nature Communications, May 2020. URL: https://doi.org/10.1038/s41467-020-19221-x, doi:10.1038/s41467-020-19221-x. This article has 29 citations and is from a highest quality peer-reviewed journal.
(hashimoto2020identificationofa pages 1-2): Satoshi Hashimoto, Takato Sugiyama, Reina Yamazaki, Risa Nobuta, and Toshifumi Inada. Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells. Scientific Reports, Feb 2020. URL: https://doi.org/10.1038/s41598-020-60241-w, doi:10.1038/s41598-020-60241-w. This article has 125 citations and is from a peer-reviewed journal.
(soll2018rnaligaselikedomain pages 1-2): Jennifer M. Soll, Joshua R. Brickner, Miranda C. Mudge, and Nima Mosammaparast. Rna ligase-like domain in activating signal cointegrator 1 complex subunit 1 (ascc1) regulates ascc complex function during alkylation damage. Journal of Biological Chemistry, 293:13524-13533, Aug 2018. URL: https://doi.org/10.1074/jbc.ra117.000114, doi:10.1074/jbc.ra117.000114. This article has 39 citations and is from a domain leading peer-reviewed journal.
(fahrer2023dnaalkylationdamage pages 12-14): Jörg Fahrer and Markus Christmann. Dna alkylation damage by nitrosamines and relevant dna repair pathways. International Journal of Molecular Sciences, Feb 2023. URL: https://doi.org/10.3390/ijms24054684, doi:10.3390/ijms24054684. This article has 115 citations.
(jia2020theinteractionof pages 3-4): Junqiao Jia, Eva Absmeier, Nicole Holton, Agnieszka J. Pietrzyk-Brzezinska, Philipp Hackert, Katherine E. Bohnsack, Markus T. Bohnsack, and Markus C. Wahl. The interaction of dna repair factors ascc2 and ascc3 is affected by somatic cancer mutations. Nature Communications, May 2020. URL: https://doi.org/10.1038/s41467-020-19221-x, doi:10.1038/s41467-020-19221-x. This article has 29 citations and is from a highest quality peer-reviewed journal.
(lombardi2022theascc2cue pages 2-4): Patrick M. Lombardi, Sara Haile, Timur Rusanov, Rebecca Rodell, Rita Anoh, Julia G. Baer, Kate A. Burke, Lauren N. Gray, Abigail R. Hacker, Kayla R. Kebreau, Christine K. Ngandu, Hannah A. Orland, Emmanuella Osei-Asante, Dhane P. Schmelyun, Devin E. Shorb, Shaheer H. Syed, Julianna M. Veilleux, Ananya Majumdar, Nima Mosammaparast, and Cynthia Wolberger. The ascc2 cue domain in the alkbh3–ascc dna repair complex recognizes adjacent ubiquitins in k63-linked polyubiquitin. Journal of Biological Chemistry, 298:101545, Feb 2022. URL: https://doi.org/10.1016/j.jbc.2021.101545, doi:10.1016/j.jbc.2021.101545. This article has 11 citations and is from a domain leading peer-reviewed journal.
(lombardi2022theascc2cue pages 4-7): Patrick M. Lombardi, Sara Haile, Timur Rusanov, Rebecca Rodell, Rita Anoh, Julia G. Baer, Kate A. Burke, Lauren N. Gray, Abigail R. Hacker, Kayla R. Kebreau, Christine K. Ngandu, Hannah A. Orland, Emmanuella Osei-Asante, Dhane P. Schmelyun, Devin E. Shorb, Shaheer H. Syed, Julianna M. Veilleux, Ananya Majumdar, Nima Mosammaparast, and Cynthia Wolberger. The ascc2 cue domain in the alkbh3–ascc dna repair complex recognizes adjacent ubiquitins in k63-linked polyubiquitin. Journal of Biological Chemistry, 298:101545, Feb 2022. URL: https://doi.org/10.1016/j.jbc.2021.101545, doi:10.1016/j.jbc.2021.101545. This article has 11 citations and is from a domain leading peer-reviewed journal.
(ford2024ubiquitindependenttranslationcontrol pages 4-6): Pierce W. Ford, Mythreyi Narasimhan, and Eric J. Bennett. Ubiquitin-dependent translation control mechanisms: degradation and beyond. Cell reports, 43 12:115050, Dec 2024. URL: https://doi.org/10.1016/j.celrep.2024.115050, doi:10.1016/j.celrep.2024.115050. This article has 17 citations and is from a highest quality peer-reviewed journal.
(hashimoto2020identificationofa pages 5-7): Satoshi Hashimoto, Takato Sugiyama, Reina Yamazaki, Risa Nobuta, and Toshifumi Inada. Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells. Scientific Reports, Feb 2020. URL: https://doi.org/10.1038/s41598-020-60241-w, doi:10.1038/s41598-020-60241-w. This article has 125 citations and is from a peer-reviewed journal.
(jia2020theinteractionof pages 1-2): Junqiao Jia, Eva Absmeier, Nicole Holton, Agnieszka J. Pietrzyk-Brzezinska, Philipp Hackert, Katherine E. Bohnsack, Markus T. Bohnsack, and Markus C. Wahl. The interaction of dna repair factors ascc2 and ascc3 is affected by somatic cancer mutations. Nature Communications, May 2020. URL: https://doi.org/10.1038/s41467-020-19221-x, doi:10.1038/s41467-020-19221-x. This article has 29 citations and is from a highest quality peer-reviewed journal.
(brickner2019activationandregulation pages 139-144): Joshua R. Brickner. Activation and regulation of the alkbh3-ascc alkylation repair pathway. ArXiv, 2019. URL: https://doi.org/10.7936/gavm-wj49, doi:10.7936/gavm-wj49. This article has 0 citations.
(miscicka2024ribosomalcollisionis pages 1-1): Anna Miścicka, Alexander G Bulakhov, Kazushige Kuroha, Alexandra Zinoviev, Christopher U T Hellen, and Tatyana V Pestova. Ribosomal collision is not a prerequisite for znf598-mediated ribosome ubiquitination and disassembly of ribosomal complexes by ascc. Nucleic Acids Research, 52:4627-4643, Feb 2024. URL: https://doi.org/10.1093/nar/gkae087, doi:10.1093/nar/gkae087. This article has 21 citations and is from a highest quality peer-reviewed journal.
(hashimoto2020identificationofa pages 3-5): Satoshi Hashimoto, Takato Sugiyama, Reina Yamazaki, Risa Nobuta, and Toshifumi Inada. Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells. Scientific Reports, Feb 2020. URL: https://doi.org/10.1038/s41598-020-60241-w, doi:10.1038/s41598-020-60241-w. This article has 125 citations and is from a peer-reviewed journal.
(ford2024ubiquitindependenttranslationcontrol pages 2-4): Pierce W. Ford, Mythreyi Narasimhan, and Eric J. Bennett. Ubiquitin-dependent translation control mechanisms: degradation and beyond. Cell reports, 43 12:115050, Dec 2024. URL: https://doi.org/10.1016/j.celrep.2024.115050, doi:10.1016/j.celrep.2024.115050. This article has 17 citations and is from a highest quality peer-reviewed journal.
(miscicka2024ribosomalcollisionis pages 12-13): Anna Miścicka, Alexander G Bulakhov, Kazushige Kuroha, Alexandra Zinoviev, Christopher U T Hellen, and Tatyana V Pestova. Ribosomal collision is not a prerequisite for znf598-mediated ribosome ubiquitination and disassembly of ribosomal complexes by ascc. Nucleic Acids Research, 52:4627-4643, Feb 2024. URL: https://doi.org/10.1093/nar/gkae087, doi:10.1093/nar/gkae087. This article has 21 citations and is from a highest quality peer-reviewed journal.
(miscicka2024ribosomalcollisionis pages 11-11): Anna Miścicka, Alexander G Bulakhov, Kazushige Kuroha, Alexandra Zinoviev, Christopher U T Hellen, and Tatyana V Pestova. Ribosomal collision is not a prerequisite for znf598-mediated ribosome ubiquitination and disassembly of ribosomal complexes by ascc. Nucleic Acids Research, 52:4627-4643, Feb 2024. URL: https://doi.org/10.1093/nar/gkae087, doi:10.1093/nar/gkae087. This article has 21 citations and is from a highest quality peer-reviewed journal.
(miscicka2024ribosomalcollisionis pages 6-7): Anna Miścicka, Alexander G Bulakhov, Kazushige Kuroha, Alexandra Zinoviev, Christopher U T Hellen, and Tatyana V Pestova. Ribosomal collision is not a prerequisite for znf598-mediated ribosome ubiquitination and disassembly of ribosomal complexes by ascc. Nucleic Acids Research, 52:4627-4643, Feb 2024. URL: https://doi.org/10.1093/nar/gkae087, doi:10.1093/nar/gkae087. This article has 21 citations and is from a highest quality peer-reviewed journal.
(miscicka2024ribosomalcollisionis pages 8-9): Anna Miścicka, Alexander G Bulakhov, Kazushige Kuroha, Alexandra Zinoviev, Christopher U T Hellen, and Tatyana V Pestova. Ribosomal collision is not a prerequisite for znf598-mediated ribosome ubiquitination and disassembly of ribosomal complexes by ascc. Nucleic Acids Research, 52:4627-4643, Feb 2024. URL: https://doi.org/10.1093/nar/gkae087, doi:10.1093/nar/gkae087. This article has 21 citations and is from a highest quality peer-reviewed journal.
(jia2023extendeddnathreading pages 2-3): Junqiao Jia, Tarek Hilal, Katherine E. Bohnsack, Aleksandar Chernev, Ning Tsao, Juliane Bethmann, Aruna Arumugam, Lane Parmely, Nicole Holton, Bernhard Loll, Nima Mosammaparast, Markus T. Bohnsack, Henning Urlaub, and Markus C. Wahl. Extended dna threading through a dual-engine motor module of the activating signal co-integrator 1 complex. Nature Communications, Apr 2023. URL: https://doi.org/10.1038/s41467-023-37528-3, doi:10.1038/s41467-023-37528-3. This article has 13 citations and is from a highest quality peer-reviewed journal.
(jia2020theinteractionof pages 9-10): Junqiao Jia, Eva Absmeier, Nicole Holton, Agnieszka J. Pietrzyk-Brzezinska, Philipp Hackert, Katherine E. Bohnsack, Markus T. Bohnsack, and Markus C. Wahl. The interaction of dna repair factors ascc2 and ascc3 is affected by somatic cancer mutations. Nature Communications, May 2020. URL: https://doi.org/10.1038/s41467-020-19221-x, doi:10.1038/s41467-020-19221-x. This article has 29 citations and is from a highest quality peer-reviewed journal.
(OpenTargets Search: -ASCC2): Open Targets Query (-ASCC2, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(pan2025pancanceranalysisreveals pages 2-3): Yimin Pan, Jun Tan, Changwu Wu, Chunbo Liu, Zheng Chen, Yongye Zhu, Fushu Luo, and Qing Liu. Pan-cancer analysis reveals ascc family promotes the cancer progression of lung adenocarcinoma. Scientific Reports, Jul 2025. URL: https://doi.org/10.1038/s41598-025-03946-0, doi:10.1038/s41598-025-03946-0. This article has 1 citations and is from a peer-reviewed journal.
(pan2025pancanceranalysisreveals pages 3-5): Yimin Pan, Jun Tan, Changwu Wu, Chunbo Liu, Zheng Chen, Yongye Zhu, Fushu Luo, and Qing Liu. Pan-cancer analysis reveals ascc family promotes the cancer progression of lung adenocarcinoma. Scientific Reports, Jul 2025. URL: https://doi.org/10.1038/s41598-025-03946-0, doi:10.1038/s41598-025-03946-0. This article has 1 citations and is from a peer-reviewed journal.
(han2021longnoncodingrna pages 1-5): jianxin han, Ning Tao, Zhenlei Zhao, Yanpei Gu, Fan Xue, Yali Yan, Lihuan Chen, Hongrui Xiao, Ruiying Qiu, Ying Zhang, Hengqing An, and Wei Li. Long noncoding rna tcons_00027385 acts as a mir-874-5p sponge to suppress the progression of prostate cancer through regulating ascc2 expression. Unknown journal, Jul 2021. URL: https://doi.org/10.21203/rs.3.rs-728951/v1, doi:10.21203/rs.3.rs-728951/v1. This article has 0 citations.
(jia2020theinteractionof pages 5-6): Junqiao Jia, Eva Absmeier, Nicole Holton, Agnieszka J. Pietrzyk-Brzezinska, Philipp Hackert, Katherine E. Bohnsack, Markus T. Bohnsack, and Markus C. Wahl. The interaction of dna repair factors ascc2 and ascc3 is affected by somatic cancer mutations. Nature Communications, May 2020. URL: https://doi.org/10.1038/s41467-020-19221-x, doi:10.1038/s41467-020-19221-x. This article has 29 citations and is from a highest quality peer-reviewed journal.
(pan2025pancanceranalysisreveals pages 1-2): Yimin Pan, Jun Tan, Changwu Wu, Chunbo Liu, Zheng Chen, Yongye Zhu, Fushu Luo, and Qing Liu. Pan-cancer analysis reveals ascc family promotes the cancer progression of lung adenocarcinoma. Scientific Reports, Jul 2025. URL: https://doi.org/10.1038/s41598-025-03946-0, doi:10.1038/s41598-025-03946-0. This article has 1 citations and is from a peer-reviewed journal.
(soll2019theroleof pages 27-34): Jennifer M. Soll. The role of the ascc complex in the alkylation damage response. ArXiv, 2019. URL: https://doi.org/10.7936/05nr-fv98, doi:10.7936/05nr-fv98. This article has 0 citations.
(soll2019theroleof pages 90-95): Jennifer M. Soll. The role of the ascc complex in the alkylation damage response. ArXiv, 2019. URL: https://doi.org/10.7936/05nr-fv98, doi:10.7936/05nr-fv98. This article has 0 citations.
(miscicka2024ribosomalcollisionis pages 11-12): Anna Miścicka, Alexander G Bulakhov, Kazushige Kuroha, Alexandra Zinoviev, Christopher U T Hellen, and Tatyana V Pestova. Ribosomal collision is not a prerequisite for znf598-mediated ribosome ubiquitination and disassembly of ribosomal complexes by ascc. Nucleic Acids Research, 52:4627-4643, Feb 2024. URL: https://doi.org/10.1093/nar/gkae087, doi:10.1093/nar/gkae087. This article has 21 citations and is from a highest quality peer-reviewed journal.
(hashimoto2020identificationofa pages 2-3): Satoshi Hashimoto, Takato Sugiyama, Reina Yamazaki, Risa Nobuta, and Toshifumi Inada. Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells. Scientific Reports, Feb 2020. URL: https://doi.org/10.1038/s41598-020-60241-w, doi:10.1038/s41598-020-60241-w. This article has 125 citations and is from a peer-reviewed journal.
(jia2020theinteractionof pages 10-11): Junqiao Jia, Eva Absmeier, Nicole Holton, Agnieszka J. Pietrzyk-Brzezinska, Philipp Hackert, Katherine E. Bohnsack, Markus T. Bohnsack, and Markus C. Wahl. The interaction of dna repair factors ascc2 and ascc3 is affected by somatic cancer mutations. Nature Communications, May 2020. URL: https://doi.org/10.1038/s41467-020-19221-x, doi:10.1038/s41467-020-19221-x. This article has 29 citations and is from a highest quality peer-reviewed journal.