Evidence map›Paper›PMID 21647451›Full record

ArticlePloS one2011

Discovery of protein phosphorylation motifs through exploratory data analysis.

Yi-Cheng Chen, Kripamoy Aguan, Chu-Wen Yang, Yao-Tsung Wang, Nikhil R Pal, I-Fang Chung

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Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

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8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

  1. Article
  2. Review
  3. Phosphorylation Site Motifs in Plant Protein Kinases and Their Substrates.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Yi-Cheng ChenInstitute of Biomedical Informatics, National Yang-Ming University, Taipei, Taiwan.
Kripamoy Aguan
Chu-Wen Yang
Yao-Tsung Wang
Nikhil R Pal
I-Fang Chung

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe need for efficient algorithms to uncover biologically relevant phosphorylation motifs has become very important with rapid expansion of the proteomic sequence database along with a plethora of new information on phosphorylation sites. Here we present a novel unsupervised method, called Motif Finder (in short, F-Motif) for identification of phosphorylation motifs. F-Motif uses clustering of sequence information represented by numerical features that exploit the statistical information hidden in some foreground data. Furthermore, these identified motifs are then filtered to find "actual" motifs with statistically significant motif scores. RESULTS AND DISCUSSION: We have applied F-Motif to several new and existing data sets and compared its performance with two well known state-of-the-art methods. In almost all cases F-Motif could identify all statistically significant motifs extracted by the state-of-the-art methods. More importantly, in addition to this, F-Motif uncovers several novel motifs. We have demonstrated using clues from the literature that most of these new motifs discovered by F-Motif are indeed novel. We have also found some interesting phenomena. For example, for CK2 kinase, the conserved sites appear only on the right side of S. However, for CDK kinase, the adjacent site on the right of S is conserved with residue P. In addition, three different encoding methods, including a novel position contrast matrix (PCM) and the simplest binary coding, are used and the ability of F-motif to discover motifs remains quite robust with respect to encoding schemes.

conclusionsAn iterative algorithm proposed here uses exploratory data analysis to discover motifs from phosphorylated data. The effectiveness of F-Motif has been demonstrated using several real data sets as well as using a synthetic data set. The method is quite general in nature and can be used to find other types of motifs also. We have also provided a server for F-Motif at http://f-motif.classcloud.org/, http://bio.classcloud.org/f-motif/ or http://ymu.classcloud.org/f-motif/.

Indexed as

AlgorithmsAmino Acid MotifsAmino Acid SequenceComputational BiologyConsensus SequenceDatabases, ProteinHumansPeptide FragmentsPhosphoproteinsPhosphorylationPeptide FragmentsPhosphoproteins

Identifiers

PMID21647451
PMCPMC3102080

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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.