Evidence map›Paper›PMID 28073915›Full record

ArticleThe Journal of biological chemistry2017

UbE2E1/UBCH6 Is a Critical

Keith Wheaton, Feroz Sarkari, Beena Stanly Johns, Hossein Davarinejad, Olga Egorova, Lilia Kaustov, Brian Raught, Vivian Saridakis, Yi Sheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Ubiquitin-conjugating Enzymes in Cancer.International journal of biological sciences · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis.Frontiers in cell and developmental biology · 2022
    Review
  8. Review
  9. Identification ofOncology letters · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
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

9 authors at 2 institutions in 1 country.

Keith WheatonFrom the Department of Biology, York University, Toronto, Ontario M3J1P3 and.
Feroz SarkariFrom the Department of Biology, York University, Toronto, Ontario M3J1P3 and.
Beena Stanly JohnsFrom the Department of Biology, York University, Toronto, Ontario M3J1P3 and.
Hossein DavarinejadFrom the Department of Biology, York University, Toronto, Ontario M3J1P3 and.
Olga EgorovaFrom the Department of Biology, York University, Toronto, Ontario M3J1P3 and.
Lilia Kaustovthe Princess Margaret Cancer Centre, University Health Network, Toronto, Ontario M5G 1L7, Canada.
Brian Raughtthe Princess Margaret Cancer Centre, University Health Network, Toronto, Ontario M5G 1L7, Canada.
Vivian SaridakisFrom the Department of Biology, York University, Toronto, Ontario M3J1P3 and.
Yi ShengFrom the Department of Biology, York University, Toronto, Ontario M3J1P3 and yisheng@yorku.ca.
York University · CAPrincess Margaret Cancer Centre · CA

Funding

CIHR 106583
6 · The paper itself

Abstract

UbE2E1/UbcH6 is an E2 ubiquitin-conjugating enzyme that is regulated by USP7. We identified UbE2E1 as a novel component of Polycomb repressive complex 1 (PRC1), the E3 ligase complex responsible for histone H2A ubiquitination and gene silencing. We demonstrate that UbE2E1 is critical for the monoubiquitination of H2A at residue Lys-119 (uH2AK119) through its association with the PRC1 complex. UbE2E1 interacts with PRC1 subunits including Ring1A and Ring1B. Overexpression of UbE2E1 results in increased levels of uH2AK119, whereas overexpression of catalytically inactive UbE2E1_C131A or UbE2E1 knockdown results in decreased levels of uH2AK119. The down-regulation of H2A ubiquitination by loss of function of UbE2E1 is correlated with alleviated p16

Indexed as

CatalysisCell Cycle ProteinsCell Line, TumorCyclin-Dependent Kinase Inhibitor p16Gene SilencingHistonesHumansLysineProtein BindingUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseCell Cycle ProteinsCyclin-Dependent Kinase Inhibitor p16HistonesLysinePRC1 protein, humanUBE2E1 protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseUSP7 protein, humandeubiquitylation (deubiquitination)gene silencingh2a ubiquitinationhistone modificationPolycomb repressive complexubiquitin-conjugating enzyme (E2 enzyme)ubiquitylation (ubiquitination)uH2AK119

Identifiers

PMID28073915
PMCPMC5314184
OpenAlexW2570733907

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.