KIXBASE: A comprehensive web resource for identification and exploration of KIX domains.
Thakur, Jitendra K
Springer Science and Business Media LLC
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Yadav, A., Thakur, J. K., & Yadav, G. (2017). KIXBASE: A comprehensive web resource for identification and exploration of KIX domains.. Sci Rep, 7 (1), 14924. https://doi.org/10.1038/s41598-017-14617-0
The KIX domain has emerged in the last two decades as a critical site of interaction for transcriptional assembly, regulation and gene expression. Discovered in 1994, this conserved, triple helical globular domain has been characterised in various coactivator proteins of yeast, mammals and plants, including the p300/CBP (a histone acetyl transferase), MED15 (a subunit of the mediator complex of RNA polymerase II), and RECQL5 helicases. In this work, we describe the first rigorous meta analysis of KIX domains across all forms of life, leading to the development of KIXBASE, a predictive web server and global repository for detection and analysis of KIX domains. To our knowledge, KIXBASE comprises the largest online collection of KIX sequences, enabling assessments at the level of both sequence and structure, incorporating PSIPRED and MUSTER at the backend for further annotation and quality assessment. In addition, KIXBASE provides useful information about critical aspects of KIX domains such as their intrinsic disorder, hydrophobicity profiles, functional classification and annotation based on domain architectures. KIXBASE represents a significant enrichment of the currently annotated KIX dataset, especially in the plant kingdom, thus highlighting potential targets for biochemical characterization. The KIX webserver and database are both freely available to the scientific community, at http://www.nipgr.res.in/kixbase/home.php .
Animals, Humans, Sequence Alignment, Amino Acid Sequence, Models, Molecular, Internet, Software, p300-CBP Transcription Factors, RecQ Helicases, Mediator Complex, Protein Domains
External DOI: https://doi.org/10.1038/s41598-017-14617-0
This record's URL: https://www.repository.cam.ac.uk/handle/1810/280195
Attribution 4.0 International
Licence URL: https://creativecommons.org/licenses/by/4.0/