 Ubiquitin-Conjugating Enzymes
"Ubiquitin-Conjugating Enzymes" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.
| Descriptor ID |
D044763
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| MeSH Number(s) |
D08.811.464.938.500
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| Concept/Terms |
Ubiquitin-Conjugating Enzymes- Ubiquitin-Conjugating Enzymes
- Enzymes, Ubiquitin-Conjugating
- Ubiquitin Conjugating Enzymes
- Ubiquitin-Conjugating Enzyme E2
- E2, Ubiquitin-Conjugating Enzyme
- Enzyme E2, Ubiquitin-Conjugating
- Ubiquitin Conjugating Enzyme E2
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Below are MeSH descriptors whose meaning is more general than "Ubiquitin-Conjugating Enzymes".
Below are MeSH descriptors whose meaning is more specific than "Ubiquitin-Conjugating Enzymes".
This graph shows the total number of publications written about "Ubiquitin-Conjugating Enzymes" by people in this website by year, and whether "Ubiquitin-Conjugating Enzymes" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
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| 2003 | 1 | 0 | 1 | | 2004 | 0 | 1 | 1 | | 2006 | 1 | 0 | 1 | | 2009 | 1 | 0 | 1 | | 2010 | 2 | 0 | 2 | | 2011 | 1 | 0 | 1 | | 2013 | 1 | 0 | 1 | | 2016 | 0 | 1 | 1 | | 2017 | 0 | 1 | 1 | | 2019 | 1 | 0 | 1 | | 2020 | 1 | 0 | 1 | | 2021 | 2 | 0 | 2 | | 2024 | 1 | 0 | 1 | | 2025 | 1 | 0 | 1 |
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Below are the most recent publications written about "Ubiquitin-Conjugating Enzymes" by people in Profiles.
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Bukhari Z, Gu L, Nederstigt AE, Cope LJ, Bolhuis DL, Harvey K, Allen T, Hill S, Yang Y, Lawson G, Lu C, Tran T, Pineda L, Low L, Chiang A, Song J, Fong MV, Rangel VM, Chan WK, Kleiger G, Goldfarb D, Vierra CA, Brown NG, Harrison JS. Linked-domain inhibitors designed to block UBE2D induce the unfolded protein response. Cell Chem Biol. 2025 Dec 18; 32(12):1532-1544.e7.
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Chambers LR, Ye Q, Cai J, Gong M, Ledvina HE, Zhou H, Whiteley AT, Suhandynata RT, Corbett KD. A eukaryotic-like ubiquitination system in bacterial antiviral defence. Nature. 2024 07; 631(8022):843-849.
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Welsh KA, Bolhuis DL, Nederstigt AE, Boyer J, Temple BRS, Bonacci T, Gu L, Ordureau A, Harper JW, Steimel JP, Zhang Q, Emanuele MJ, Harrison JS, Brown NG. Functional conservation and divergence of the helix-turn-helix motif of E2 ubiquitin-conjugating enzymes. EMBO J. 2022 02 01; 41(3):e108823.
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Schultz-Rogers L, Lach FP, Rickman KA, Ferrer A, Mangaonkar AA, Schwab TL, Schmitz CT, Clark KJ, Dsouza NR, Zimmermann MT, Litzow M, Jacobi N, Klee EW, Smogorzewska A, Patnaik MM. A homozygous missense variant in UBE2T is associated with a mild Fanconi anemia phenotype. Haematologica. 2021 04 01; 106(4):1188-1192.
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Kumar R, Singh AK, Starokadomskyy P, Luo W, Theiss AL, Burstein E, Venuprasad K. Cutting Edge: Hypoxia-Induced Ubc9 Promoter Hypermethylation Regulates IL-17 Expression in Ulcerative Colitis. J Immunol. 2021 03 01; 206(5):936-940.
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Martinez-Chacin RC, Bodrug T, Bolhuis DL, Kedziora KM, Bonacci T, Ordureau A, Gibbs ME, Weissmann F, Qiao R, Grant GD, Cook JG, Peters JM, Wade Harper J, Emanuele MJ, Brown NG. Ubiquitin chain-elongating enzyme UBE2S activates the RING E3 ligase APC/C for substrate priming. Nat Struct Mol Biol. 2020 06; 27(6):550-560.
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Watson ER, Grace CRR, Zhang W, Miller DJ, Davidson IF, Prabu JR, Yu S, Bolhuis DL, Kulko ET, Vollrath R, Haselbach D, Stark H, Peters JM, Brown NG, Sidhu SS, Schulman BA. Protein engineering of a ubiquitin-variant inhibitor of APC/C identifies a cryptic K48 ubiquitin chain binding site. Proc Natl Acad Sci U S A. 2019 08 27; 116(35):17280-17289.
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Liang K, Volk AG, Haug JS, Marshall SA, Woodfin AR, Bartom ET, Gilmore JM, Florens L, Washburn MP, Sullivan KD, Espinosa JM, Cannova J, Zhang J, Smith ER, Crispino JD, Shilatifard A. Therapeutic Targeting of MLL Degradation Pathways in MLL-Rearranged Leukemia. Cell. 2017 Jan 12; 168(1-2):59-72.e13.
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Singh AK, Pandey RK, Shaha C, Madhubala R. MicroRNA expression profiling of Leishmania donovani-infected host cells uncovers the regulatory role of MIR30A-3p in host autophagy. Autophagy. 2016 10 02; 12(10):1817-1831.
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Jacobson AD, MacFadden A, Wu Z, Peng J, Liu CW. Autoregulation of the 26S proteasome by in situ ubiquitination. Mol Biol Cell. 2014 Jun 15; 25(12):1824-35.
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