ArticleThe EMBO journal2003
A conserved catalytic residue in the ubiquitin-conjugating enzyme family.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 102 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
102 citing papers in PubMed, 195 citations in OpenAlex.
- Article
- UFMylation System: Biological Functions, Molecular Mechanisms, Diseases, and Drug Discovery.MedComm · 2025Review
- Insights into Noncanonical and Diversified Functions of ABCF1: From Health to Disease.Journal of molecular biology · 2025Review
- Structural Insights into the GABARAP-ATG3 Backside Interaction and Apo ATG3 Conformation.Biochemistry · 2025Article
- The Lysine Deprotonation Mechanism in a Ubiquitin Conjugating Enzyme.The journal of physical chemistry. B · 2025Article
- UFC1 reveals the multifactorial and plastic nature of oxyanion holes in E2 conjugating enzymes.Nature communications · 2025Article
- Determinants of chemoselectivity in ubiquitination by the J2 family of ubiquitin-conjugating enzymes.The EMBO journal · 2024Article
- The role of ubiquitin-conjugating enzyme in the process of spermatogenesis.Reproductive biology and endocrinology : RB&E · 2024Review
- Structural Analyses of a GABARAP~ATG3 Conjugate Uncover a Novel Non-covalent Ubl-E2 Backside Interaction.bioRxiv : the preprint server for biology · 2024Article
- Tracking of Ubiquitin Signaling through 3.5 Billion Years of Combinatorial Conjugation.International journal of molecular sciences · 2024Review
- Discovery and characterization of noncanonical E2-conjugating enzymes.Science advances · 2024Article
- UBE2A and UBE2B are recruited by an atypical E3 ligase module in UBR4.Nature structural & molecular biology · 2024Article
- In vitro Di-ubiquitin Formation Assay and E3 Cooperation Assay.Bio-protocol · 2022Article
- A non-canonical scaffold-type E3 ligase complex mediates protein UFMylation.The EMBO journal · 2022Article
- A new dawn beyond lysine ubiquitination.Nature chemical biology · 2022Review
- Ubiquitin-conjugating activity by PEX4 is required for efficient protein transport to peroxisomes in Arabidopsis thaliana.The Journal of biological chemistry · 2022Article
- MUL1-RING recruits the substrate, p53-TAD as a complex with UBE2D2-UB conjugate.The FEBS journal · 2022Article
- Nedd4-2 binding to 14-3-3 modulates the accessibility of its catalytic site and WW domains.Biophysical journal · 2022Article
- Review
- Non-lysine ubiquitylation: Doing things differently.Frontiers in molecular biosciences · 2022Review
42 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issuedWeissman, Allan M [corrected to Weisman, Allan M]
- Erratum issuedWeisman, Allan M [corrected to Weissman, Allan M]
Authors and funding
13 authors at 1 institution in 1 country.
Funding
Abstract
Ubiquitin (Ub) regulates diverse functions in eukaryotes through its attachment to other proteins. The defining step in this protein modification pathway is the attack of a substrate lysine residue on Ub bound through its C-terminus to the active site cysteine residue of a Ub-conjugating enzyme (E2) or certain Ub ligases (E3s). So far, these E2 and E3 cysteine residues are the only enzyme groups known to participate in the catalysis of conjugation. Here we show that a strictly conserved E2 asparagine residue is critical for catalysis of E2- and E2/RING E3-dependent isopeptide bond formation, but dispensable for upstream and downstream reactions of Ub thiol ester formation. In contrast, the strictly conserved histidine and proline residues immediately upstream of the asparagine are dispensable for catalysis of isopeptide bond formation. We propose that the conserved asparagine side chain stabilizes the oxyanion intermediate formed during lysine attack. The E2 asparagine is the first non-covalent catalytic group to be proposed in any Ub conjugation factor.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.