Evidence map›Paper›PMID 25610865›Full record

ArticleBioMed research international2014

DBC1/CCAR2 and CCAR1 Are Largely Disordered Proteins that Have Evolved from One Common Ancestor.

Jessica Brunquell, Jia Yuan, Aqeela Erwin, Sandy D Westerheide, Bin Xue

Open access · hybridAbstract read
In one paragraph

Article in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-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

17 citing papers in PubMed, 27 citations in OpenAlex.

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  5. CCAR2 functions downstream of the Shieldin complex to promote double-strand break end-joining.Proceedings of the National Academy of Sciences of the United States of America · 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

5 authors at 1 institution in 1 country.

Jessica BrunquellDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, 4202 East Fowler Avenue, ISA 2015, Tampa, FL 33620, USA.ORCID 0000-0002-7268-9447
Jia YuanDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, 4202 East Fowler Avenue, ISA 2015, Tampa, FL 33620, USA.
Aqeela ErwinDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, 4202 East Fowler Avenue, ISA 2015, Tampa, FL 33620, USA.ORCID 0000-0002-0215-0868
Sandy D WesterheideDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, 4202 East Fowler Avenue, ISA 2015, Tampa, FL 33620, USA.
Bin XueDepartment of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, 4202 East Fowler Avenue, ISA 2015, Tampa, FL 33620, USA.
University of South Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deleted in breast cancer 1 (DBC1, CCAR2, KIAA1967) is a large, predominantly nuclear, multidomain protein that modulates gene expression by inhibiting several epigenetic modifiers, including the deacetylases SIRT1 and HDAC3, and the methyltransferase SUV39H1. DBC1 shares many highly conserved protein domains with its paralog cell cycle and apoptosis regulator 1 (CCAR1, CARP-1). In this study, we examined the full-length sequential and structural properties of DBC1 and CCAR1 from multiple species and correlated these properties with evolution. Our data shows that the conserved domains shared between DBC1 and CCAR1 have similar domain structures, as well as similar patterns of predicted disorder in less-conserved intrinsically disordered regions. Our analysis indicates similarities between DBC1, CCAR1, and the nematode protein lateral signaling target 3 (LST-3), suggesting that DBC1 and CCAR1 may have evolved from LST-3. Our data also suggests that DBC1 emerged later in evolution than CCAR1. DBC1 contains regions that show less conservation across species as compared to the same regions in CCAR1, suggesting a continuously evolving scenario for DBC1. Overall, this study provides insight into the structure and evolution of DBC1 and CCAR1, which may impact future studies on the biological functions of these proteins.

Indexed as

Evolution, MolecularAdaptor Proteins, Signal TransducingAnimalsApoptosis Regulatory ProteinsCell Cycle ProteinsHistone Deacetylase 3Histone DeacetylasesHumansMethyltransferasesProtein Structure, TertiaryRepressor ProteinsSirtuin 1Structure-Activity RelationshipAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsCCAR1 protein, humanCCAR2 protein, humanCell Cycle ProteinsHistone Deacetylase 3Histone DeacetylasesMethyltransferasesRepressor ProteinsSIRT1 protein, humanSirtuin 1SUV39H1 protein, human

Identifiers

PMID25610865
PMCPMC4287135
OpenAlexW2055630652

What OpenQuestion holds

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LicenceCC BY
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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.