Evidence map›Paper›PMID 20018847›Full record

ArticleThe Journal of biological chemistry2010

A novel type of E3 ligase for the Ufm1 conjugation system.

Kanako Tatsumi, Yu-shin Sou, Norihiro Tada, Eri Nakamura, Shun-ichiro Iemura, Tohru Natsume, Sung Hwan Kang, Chin Ha Chung, Masanori Kasahara, Eiki Kominami and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.

0numbers the graph read from it
0cells of the map it votes in
151citing papers in PubMed
2.2field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

151 citing papers in PubMed, 256 citations in OpenAlex.

  1. Review
  2. Article
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  5. Review
  6. The mechanistic basis and cellular functions of UFMylation.Nature reviews. Molecular cell biology · 2026
    Review
  7. Article
  8. Article
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  12. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
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  15. Article
  16. Review
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91 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 6 institutions in 3 countries.

Kanako TatsumiLaboratory of Frontier Science, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan.
Yu-shin Sou
Norihiro Tada
Eri Nakamura
Shun-ichiro Iemura
Tohru Natsume
Sung Hwan Kang
Chin Ha Chung
Masanori Kasahara
Eiki Kominami
Masayuki Yamamoto
Keiji Tanaka
Masaaki Komatsu
Juntendo University · JPNational Institute of Advanced Industrial Science and Technology · JPSeoul National University · KRUniversity of Tsukuba · JPHokkaido University · JPTokyo Metropolitan Institute of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin fold modifier 1 (Ufm1) is the most recently discovered ubiquitin-like modifier whose conjugation (ufmylation) system is conserved in multicellular organisms. Ufm1 is known to covalently attach with cellular protein(s) via a specific E1-activating enzyme (Uba5) and an E2-conjugating enzyme (Ufc1), but its E3-ligating enzyme(s) as well as the target protein(s) remain unknown. Herein, we report both a novel E3 ligase for Ufm1, designated Ufl1, and an Ufm1-specific substrate ligated by Ufl1, C20orf116. Ufm1 was covalently conjugated with C20orf116. Although Ufl1 has no obvious sequence homology to any other known E3s for ubiquitin and ubiquitin-like modifiers, the C20orf116 x Ufm1 formation was greatly accelerated by Ufl1. The C20orf116 x Ufm1 conjugate was cleaved by Ufm1-specific proteases, implying the reversibility of ufmylation. The conjugation was abundant in the liver and lungs of Ufm1-transgenic mice, fractionated into membrane fraction, and impaired in Uba5 knock-out cells. Intriguingly, immunological analysis revealed localizations of Ufl1 and C20orf116 mainly to the endoplasmic reticulum. Our results provide novel insights into the Ufm1 system involved in cellular regulation of multicellular organisms.

Indexed as

AnimalsCarrier ProteinsEndoplasmic ReticulumHumansMiceMice, KnockoutProteinsUbiquitinUbiquitin-Activating EnzymesUbiquitin-Protein LigasesCarrier ProteinsProteinsUBA5 protein, humanUbiquitinUbiquitin-Activating EnzymesUbiquitin-Protein LigasesUFM1-binding protein 1 containing a PCI domain, mouseUFM1 protein, humanUfm1 protein, mouse

Identifiers

PMID20018847
PMCPMC2820770
OpenAlexW2080972425

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.