Unknown

Dataset Information

0

Predicting DNA-binding specificities of eukaryotic transcription factors.


ABSTRACT: Today, annotated amino acid sequences of more and more transcription factors (TFs) are readily available. Quantitative information about their DNA-binding specificities, however, are hard to obtain. Position frequency matrices (PFMs), the most widely used models to represent binding specificities, are experimentally characterized only for a small fraction of all TFs. Even for some of the most intensively studied eukaryotic organisms (i.e., human, rat and mouse), roughly one-sixth of all proteins with annotated DNA-binding domain have been characterized experimentally. Here, we present a new method based on support vector regression for predicting quantitative DNA-binding specificities of TFs in different eukaryotic species. This approach estimates a quantitative measure for the PFM similarity of two proteins, based on various features derived from their protein sequences. The method is trained and tested on a dataset containing 1 239 TFs with known DNA-binding specificity, and used to predict specific DNA target motifs for 645 TFs with high accuracy.

SUBMITTER: Schroder A 

PROVIDER: S-EPMC2994704 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Predicting DNA-binding specificities of eukaryotic transcription factors.

Schröder Adrian A   Eichner Johannes J   Supper Jochen J   Eichner Jonas J   Wanke Dierk D   Henneges Carsten C   Zell Andreas A  

PloS one 20101130 11


Today, annotated amino acid sequences of more and more transcription factors (TFs) are readily available. Quantitative information about their DNA-binding specificities, however, are hard to obtain. Position frequency matrices (PFMs), the most widely used models to represent binding specificities, are experimentally characterized only for a small fraction of all TFs. Even for some of the most intensively studied eukaryotic organisms (i.e., human, rat and mouse), roughly one-sixth of all proteins  ...[more]

Similar Datasets

| S-EPMC2692596 | biostudies-literature
| S-EPMC8009048 | biostudies-literature
| S-EPMC7532196 | biostudies-literature
| S-EPMC3926073 | biostudies-literature
| S-EPMC6322389 | biostudies-literature
2017-05-05 | GSE94634 | GEO
| S-EPMC4403198 | biostudies-literature
| S-EPMC3834811 | biostudies-literature
| S-EPMC2666811 | biostudies-literature
| PRJEB29730 | ENA