Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (454K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (19)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Sullivan, S. A.
Right arrow Articles by Landsman, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sullivan, S. A.
Right arrow Articles by Landsman, D.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2000, Vol. 28, No. 1 320-322
© 2000 Oxford University Press

The Histone Database: a comprehensive WWW resource for histones and histone fold-containing proteins

Steven A. Sullivan, L. Aravind1, Izabela Makalowska2, Andreas D. Baxevanis2 and David Landsman*

Computational Biology Branch, National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Building 38A Room 8N805, Bethesda, MD 20894, USA, 1Department of Biology, Texas A&M University, College Station, TX 70843, USA and 2Genome Technology Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD 20892-4470, USA

The Histone Database (HDB) is an annotated and searchable collection of all full-length sequences and structures of histone and non-histone proteins containing the histone fold motif. These sequences are both eukaryotic and archaeal in origin. Several new histone fold-containing proteins have been identified, including Spt7p, and a few false positives have been removed from the earlier version of HDB. Database contents include compilations of post-translational modifications for each of the core and linker histones, as well as genomic information in the form of map loci for the human histone gene complement, with the genetic loci linked to Online Mendelian Inheritance in Man (OMIM). Conflicts between similar sequence entries from a number of source databases are also documented. Newly added to the HDB are multiple sequence alignments in which predicted functions of histone fold amino acid residues are annotated. The database is freely accessible through the WWW at http://genome.nhgri.nih.gov/histones/

* To whom correspondence should be addressed. Tel: +1 301 435 5981; Fax: +1 301 480 9241; Email: landsman@ncbi.nlm.nih.gov


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Nucleic Acids ResHome page
Y. Zhang, J. Lv, H. Liu, J. Zhu, J. Su, Q. Wu, Y. Qi, F. Wang, and X. Li
HHMD: the human histone modification database
Nucleic Acids Res., November 5, 2009; (2009) gkp968v1.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Fries, C. Betz, K. Sohn, S. Caesar, G. Schlenstedt, and S. M. Bailer
A Novel Conserved Nuclear Localization Signal Is Recognized by a Group of Yeast Importins
J. Biol. Chem., July 6, 2007; 282(27): 19292 - 19301.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
G. Zhu, H. Chen, B.-K. Choi, F. Del Piero, and D. M. Schifferli
Histone H1 Proteins Act As Receptors for the 987P Fimbriae of Enterotoxigenic Escherichia coli
J. Biol. Chem., June 17, 2005; 280(24): 23057 - 23065.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
S. Sullivan, D. W. Sink, K. L. Trout, I. Makalowska, P. M. Taylor, A. D. Baxevanis, and D. Landsman
The Histone Database
Nucleic Acids Res., January 1, 2002; 30(1): 341 - 342.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
J. Kirchner, S. L. Sanders, E. Klebanow, and P. A. Weil
Molecular Genetic Dissection of TAF25, an Essential Yeast Gene Encoding a Subunit Shared by TFIID and SAGA Multiprotein Transcription Factors
Mol. Cell. Biol., October 1, 2001; 21(19): 6668 - 6680.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
Y.-G. Gangloff, S. L. Sanders, C. Romier, D. Kirschner, P. A. Weil, L. Tora, and I. Davidson
Histone Folds Mediate Selective Heterodimerization of Yeast TAFII25 with TFIID Components yTAFII47 and yTAFII65 and with SAGA Component ySPT7
Mol. Cell. Biol., March 1, 2001; 21(5): 1841 - 1853.
[Abstract] [Full Text]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.