Evidence map›Paper›PMID 30836974›Full record

ArticleBMC structural biology2019

Classification of the human THAP protein family identifies an evolutionarily conserved coiled coil region.

Hiral M Sanghavi, Sairam S Mallajosyula, Sharmistha Majumdar

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in BMC structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. From Thanatos to transcription: the emerging biology of THAP proteins.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. [Effects ofZhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2026
    Article
  3. Sea CucumberResearch square · 2026
    Article
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  7. Mutation of the Thap4 gene causes dwarfism and testicular anomalies in rats and mice.Mammalian genome : official journal of the International Mammalian Genome Society · 2024
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Hiral M SanghaviDiscipline of Biological Engineering, Indian Institute of Technology Gandhinagar, Gandhinagar, India.
Sairam S MallajosyulaDiscipline of Chemistry, Indian Institute of Technology Gandhinagar, Gandhinagar, India.
Sharmistha MajumdarDiscipline of Biological Engineering, Indian Institute of Technology Gandhinagar, Gandhinagar, India. sharmistham@iitgn.ac.in.ORCID 0000-0003-4356-7237
Indian Institute of Technology Gandhinagar · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe THAP (Thanatos Associated Proteins) protein family in humans is implicated in various important cellular processes like epigenetic regulation, maintenance of pluripotency, transposition and disorders like cancers and hemophilia. The human THAP protein family which consists of twelve members of different lengths has a well characterized amino terminal, zinc-coordinating, DNA-binding domain called the THAP domain. However, the carboxy terminus of most THAP proteins is yet to be structurally characterized. A coiled coil region is known to help in protein oligomerization in THAP1 and THAP11. It is not known if other human THAP proteins oligomerize. We have used bioinformatic tools to explore the possibility of dimerization of THAP proteins via a coiled coil region.

resultsClassification of human THAP protein into three size based groups led to the identification of an evolutionarily conserved alpha helical region, downstream of the amino terminal THAP domain. Secondary structure predictions, alpha helical wheel plots and protein models demonstrated the strong possibility of coiled coil formation in this conserved, leucine rich region of all THAP proteins except THAP10.

conclusionsThe identification of a predicted oligomerization region in the human THAP protein family opens new directions to investigate the members of this protein family.

Indexed as

Amino Acid SequenceComputational BiologyConserved SequenceDNA-Binding ProteinsEvolution, MolecularHumansModels, MolecularProtein DomainsProtein MultimerizationProtein Structure, SecondaryDNA-Binding ProteinsClassificationLeucine zipperOligomerizationTHAP proteins

Identifiers

PMID30836974
PMCPMC6402169
OpenAlexW2939044534

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.