Article |
NOPdb: Nucleolar Proteome Database
Division of Gene Regulation and Expression, Wellcome Trust Biocentre, School of Life Sciences, University of Dundee Dundee DD1 5EH, UK 1Department of Biochemistry and Molecular Biology, University of Southern Denmark Campusvej 55, DK-5230 Odense M, Denmark
*To whom correspondence should be addressed. Tel: +1 617 253 0265; Fax: +1 617 253 3867; Email: akleung{at}mit.edu
Received August 13, 2005. Accepted August 16, 2005.
The Nucleolar Proteome Database (NOPdb) archives data on >700 proteins that were identified by multiple mass spectrometry (MS) analyses from highly purified preparations of human nucleoli, the most prominent nuclear organelle. Each protein entry is annotated with information about its corresponding gene, its domain structures and relevant protein homologues across species, as well as documenting its MS identification history including all the peptides sequenced by tandem MS/MS. Moreover, data showing the quantitative changes in the relative levels of
500 nucleolar proteins are compared at different timepoints upon transcriptional inhibition. Correlating changes in protein abundance at multiple timepoints, highlighted by visualization means in the NOPdb, provides clues regarding the potential interactions and relationships between nucleolar proteins and thereby suggests putative functions for factors within the 30% of the proteome which comprises novel/uncharacterized proteins. The NOPdb (http://www.lamondlab.com/NOPdb) is searchable by either gene names, nucleotide or protein sequences, Gene Ontology terms or motifs, or by limiting the range for isoelectric points and/or molecular weights and links to other databases (e.g. LocusLink, OMIM and PubMed).
Present address: Anthony K. L. Leung, Center for Cancer Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
V. Matafora, A. D'Amato, S. Mori, F. Blasi, and A. Bachi Proteomics Analysis of Nucleolar SUMO-1 Target Proteins upon Proteasome Inhibition Mol. Cell. Proteomics, October 1, 2009; 8(10): 2243 - 2255. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. Ukil, C. P. De Souza, H.-L. Liu, and S. A. Osmani Nucleolar Separation from Chromosomes during Aspergillus nidulans Mitosis Can Occur Without Spindle Forces Mol. Biol. Cell, April 15, 2009; 20(8): 2132 - 2145. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y. Ahmad, F.-M. Boisvert, P. Gregor, A. Cobley, and A. I. Lamond NOPdb: Nucleolar Proteome Database--2008 update Nucleic Acids Res., January 1, 2009; 37(suppl_1): D181 - D184. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. H. Wong, K. H. Brettingham-Moore, L. Chan, J. M. Quach, M. A. Anderson, E. L. Northrop, R. Hannan, R. Saffery, M. L. Shaw, E. Williams, et al. Centromere RNA is a key component for the assembly of nucleoproteins at the nucleolus and centromere Genome Res., August 1, 2007; 17(8): 1146 - 1160. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Benezra, R. S. Greenberg, and S. K. Masur Localization of ZO-1 in the Nucleolus of Corneal Fibroblasts Invest. Ophthalmol. Vis. Sci., May 1, 2007; 48(5): 2043 - 2049. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Holzel, T. Grimm, M. Rohrmoser, A. Malamoussi, T. Harasim, A. Gruber-Eber, E. Kremmer, and D. Eick The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing Nucleic Acids Res., February 16, 2007; 35(3): 789 - 800. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y. Zhang, Y. Zhang, J. Adachi, J. V. Olsen, R. Shi, G. de Souza, E. Pasini, L. J. Foster, B. Macek, A. Zougman, et al. MAPU: Max-Planck Unified database of organellar, cellular, tissue and body fluid proteomes Nucleic Acids Res., January 12, 2007; 35(suppl_1): D771 - D779. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Bove, C. L.H. Hord, and M. A. Mullen The blossoming of RNA biology: Novel insights from plant systems RNA, December 1, 2006; 12(12): 2035 - 2046. [Full Text] [PDF] |
||||
![]() |
J. R. Boyne and A. Whitehouse Nucleolar trafficking is essential for nuclear export of intronless herpesvirus mRNA PNAS, October 10, 2006; 103(41): 15190 - 15195. [Abstract] [Full Text] [PDF] |
||||






