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Nucleic Acids Res. 2015 Jan;43(Database issue):D277-82. doi: 10.1093/nar/gku954. Epub 2014 Oct 16.

MoonProt: a database for proteins that are known to moonlight.

Author information

1
Department of Bioengineering, University of Illinois at Chicago, Chicago, IL 60607, USA.
2
Department of Biological Sciences, MC567, University of Illinois at Chicago, 900 S. Ashland Ave., Chicago, IL 60607, USA.
3
Center for Pharmaceutical Biotechnology, College of Pharmacy, University of Illinois at Chicago, 900 S. Ashland Ave., Chicago, IL 60607, USA.
4
Illinois Institute of Technology, 3300 S Federal St, Chicago, IL 60616, USA.
5
Department of Bioengineering, University of Illinois at Chicago, Chicago, IL 60607, USA Department of Biological Sciences, MC567, University of Illinois at Chicago, 900 S. Ashland Ave., Chicago, IL 60607, USA cjeffery@uic.edu.

Abstract

Moonlighting proteins comprise a class of multifunctional proteins in which a single polypeptide chain performs multiple biochemical functions that are not due to gene fusions, multiple RNA splice variants or pleiotropic effects. The known moonlighting proteins perform a variety of diverse functions in many different cell types and species, and information about their structures and functions is scattered in many publications. We have constructed the manually curated, searchable, internet-based MoonProt Database (http://www.moonlightingproteins.org) with information about the over 200 proteins that have been experimentally verified to be moonlighting proteins. The availability of this organized information provides a more complete picture of what is currently known about moonlighting proteins. The database will also aid researchers in other fields, including determining the functions of genes identified in genome sequencing projects, interpreting data from proteomics projects and annotating protein sequence and structural databases. In addition, information about the structures and functions of moonlighting proteins can be helpful in understanding how novel protein functional sites evolved on an ancient protein scaffold, which can also help in the design of proteins with novel functions.

PMID:
25324305
PMCID:
PMC4384022
DOI:
10.1093/nar/gku954
[Indexed for MEDLINE]
Free PMC Article

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