Evidence map›Paper›PMID 24194591›Full record

ArticleNucleic acids research2014

LenVarDB: database of length-variant protein domains.

Eshita Mutt, Oommen K Mathew, Ramanathan Sowdhamini

Abstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Genome-Wide Identification of Sigma Factors inInternational journal of molecular sciences · 2026
    Article
  2. PASS2: update of database of structure-based sequence alignments.Database : the journal of biological databases and curation · 2025
    Article
  3. Article
  4. Article
4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Eshita MuttInternational Institute of Information Technology-Hyderabad, Gachibowli, Hyderabad 500032, Andhra Pradesh, India, National Centre for Biological Sciences (TIFR), UAS-GKVK Campus, Bellary Road, Bangalore 560065, Karnataka, India and SASTRA University, Tirumalaisamudram, Thanjavur 613401, Tamil Nadu, India.
Oommen K Mathew
Ramanathan Sowdhamini

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein domains are functionally and structurally independent modules, which add to the functional variety of proteins. This array of functional diversity has been enabled by evolutionary changes, such as amino acid substitutions or insertions or deletions, occurring in these protein domains. Length variations (indels) can introduce changes at structural, functional and interaction levels. LenVarDB (freely available at http://caps.ncbs.res.in/lenvardb/) traces these length variations, starting from structure-based sequence alignments in our Protein Alignments organized as Structural Superfamilies (PASS2) database, across 731 structural classification of proteins (SCOP)-based protein domain superfamilies connected to 2 730 625 sequence homologues. Alignment of sequence homologues corresponding to a structural domain is available, starting from a structure-based sequence alignment of the superfamily. Orientation of the length-variant (indel) regions in protein domains can be visualized by mapping them on the structure and on the alignment. Knowledge about location of length variations within protein domains and their visual representation will be useful in predicting changes within structurally or functionally relevant sites, which may ultimately regulate protein function. Non-technical summary: Evolutionary changes bring about natural changes to proteins that may be found in many organisms. Such changes could be reflected as amino acid substitutions or insertions-deletions (indels) in protein sequences. LenVarDB is a database that provides an early overview of observed length variations that were set among 731 protein families and after examining >2 million sequences. Indels are followed up to observe if they are close to the active site such that they can affect the activity of proteins. Inclusion of such information can aid the design of bioengineering experiments.

Indexed as

Databases, ProteinINDEL MutationProtein Structure, TertiaryGenetic VariationInternetModels, MolecularProteinsSequence AlignmentSequence Analysis, ProteinProteins

Identifiers

PMID24194591
PMCPMC3964994

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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.