Evidence map›Paper›PMID 24337577›Full record

ArticleThe Journal of biological chemistry2014

Protein interaction screening for the ankyrin repeats and suppressor of cytokine signaling (SOCS) box (ASB) family identify Asb11 as a novel endoplasmic reticulum resident ubiquitin ligase.

Christina Aaen Andresen, Stine Smedegaard, Kathrine Beck Sylvestersen, Charlotte Svensson, Diego Iglesias-Gato, Giuseppe Cazzamali, Tine Kragh Nielsen, Michael Lund Nielsen, Amilcar Flores-Morales

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. Trial
  2. ASB9 promotes ubiquitin-mediated degradation of TNP2 to facilitate histone-to-protamine transition in humans and mice.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Functional Variants Associated WithFrontiers in genetics · 2022
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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.

Christina Aaen AndresenFrom the Departments of Disease Biology.
Stine Smedegaard
Kathrine Beck Sylvestersen
Charlotte Svensson
Diego Iglesias-Gato
Giuseppe Cazzamali
Tine Kragh Nielsen
Michael Lund Nielsen
Amilcar Flores-Morales
University of Copenhagen · DKNovo Nordisk Foundation · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ankyrin and SOCS (suppressor of cytokine signaling) box (ASB) family of proteins function as the substrate recognition subunit in a subset of Elongin-Cullin-SOCS (ECS) E3 ubiquitin ligases. Despite counting 18 members in humans, the identity of the physiological targets of the Asb proteins remains largely unexplored. To increase our understanding of the function of ASB proteins, we conducted a family-wide SILAC (stable isotope labeling by amino acids in cell culture)-based protein/protein interaction analysis. This investigation led to the identification of novel as well as known ASB-associated proteins like Cullin 5 and Elongins B/C. We observed that several proteins can be bound by more than one Asb protein. The additional exploration of this phenomenon demonstrated that ASB-Cullin 5 complexes can oligomerize and provides evidence that Cullin 5 forms heterodimeric complexes with the Cullin 4a-DDB1 complex. We also demonstrated that ASB11 is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex. Moreover, expression of ASB11 can increase Ribophorin 1 protein turnover in vivo. In summary, we provide a comprehensive protein/protein interaction data resource that can aid the biological and functional characterization of ASB ubiquitin ligases.

Indexed as

Cullin ProteinsDNA-Binding ProteinsEndoplasmic ReticulumHEK293 CellsHeLa CellsHumansMembrane ProteinsMultienzyme ComplexesSuppressor of Cytokine Signaling ProteinsUbiquitinationCUL5 protein, humanCullin ProteinsDDB1 protein, humanDNA-Binding ProteinsMembrane ProteinsMultienzyme ComplexesribophorinSuppressor of Cytokine Signaling ProteinsEndoplasmic Reticulum (ER)GlycationMass Spectrometry (MS)ProteomicsUbiquitin LigaseUbiquitylation

Identifiers

PMID24337577
PMCPMC3900953
OpenAlexW2108941867

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.