Skip Navigation


Bioinformatics Advance Access originally published online on September 7, 2004
Bioinformatics 2005 21(3):410-412; doi:10.1093/bioinformatics/bti011
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow All Versions of this Article:
21/3/410    most recent
bti011v1
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 (54)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Finn, R. D.
Right arrow Articles by Bateman, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Finn, R. D.
Right arrow Articles by Bateman, A.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Bioinformatics vol. 21 issue 3 © Oxford University Press 2005; all rights reserved.

iPfam: visualization of protein–protein interactions in PDB at domain and amino acid resolutions

Robert D. Finn *, Mhairi Marshall and Alex Bateman

The Wellcome Trust Sanger Institute The Wellcome Trust Genome Campus, Hinxton CB10 1SA, UK

*To whom correspondence should be addressed.

Summary: There are many resources that contain information about binary interactions between proteins. However, protein interactions are defined by only a subset of residues in any protein. We have implemented a web resource that allows the investigation of protein interactions in the Protein Data Bank structures at the level of Pfam domains and amino acid residues. This detailed knowledge relies on the fact that there are a large number of multidomain proteins and protein complexes being deposited in the structure databases. The resource called iPfam is hosted within the Pfam UK website. Most resources focus on the interactions between proteins; iPfam includes these as well as interactions between domains in a single protein.

Availability: iPfam is available on the Web for browsing at http://www.sanger.ac.uk/Software/Pfam/iPfam/; the source-data for iPfam is freely available in relational tables via the ftp site ftp://ftp.sanger.ac.uk/pub/databases/Pfam/database_files/

Contact: rdf{at}sanger.ac.uk


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
BioinformaticsHome page
J. Goll, S. V. Rajagopala, S. C. Shiau, H. Wu, B. T. Lamb, and P. Uetz
MPIDB: the microbial protein interaction database
Bioinformatics, August 1, 2008; 24(15): 1743 - 1744.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
M. Michaut, S. Kerrien, L. Montecchi-Palazzi, F. Chauvat, C. Cassier-Chauvat, J.-C. Aude, P. Legrain, and H. Hermjakob
InteroPORC: automated inference of highly conserved protein interaction networks
Bioinformatics, July 15, 2008; 24(14): 1625 - 1631.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
J. Guo, X. Wu, D.-Y. Zhang, and K. Lin
Genome-wide inference of protein interaction sites: lessons from the yeast high-quality negative protein-protein interaction dataset
Nucleic Acids Res., April 1, 2008; 36(6): 2002 - 2011.
[Abstract] [Full Text] [PDF]


Home page
Genome ResHome page
M. K. Basu, L. Carmel, I. B. Rogozin, and E. V. Koonin
Evolution of protein domain promiscuity in eukaryotes
Genome Res., March 1, 2008; 18(3): 449 - 461.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
B. Raghavachari, A. Tasneem, T. M. Przytycka, and R. Jothi
DOMINE: a database of protein domain interactions
Nucleic Acids Res., January 11, 2008; 36(suppl_1): D656 - D661.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
P. Pagel, M. Oesterheld, O. Tovstukhina, N. Strack, V. Stumpflen, and D. Frishman
DIMA 2.0 predicted and known domain interactions
Nucleic Acids Res., January 11, 2008; 36(suppl_1): D651 - D655.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
R. D. Finn, J. Tate, J. Mistry, P. C. Coggill, S. J. Sammut, H.-R. Hotz, G. Ceric, K. Forslund, S. R. Eddy, E. L. L. Sonnhammer, et al.
The Pfam protein families database
Nucleic Acids Res., January 11, 2008; 36(suppl_1): D281 - D288.
[Abstract] [Full Text] [PDF]


Home page
Brief BioinformHome page
M. Brilli, R. Fani, and P. Lio
Current trends in the bioinformatic sequence analysis of metabolic pathways in prokaryotes
Brief Bioinform, January 1, 2008; 9(1): 34 - 45.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
J. Hernandez-Toro, C. Prieto, and J. De Las Rivas
APID2NET: unified interactome graphic analyzer
Bioinformatics, September 15, 2007; 23(18): 2495 - 2497.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
A. Schlicker, C. Huthmacher, F. Ramirez, T. Lengauer, and M. Albrecht
Functional evaluation of domain domain interactions and human protein interaction networks
Bioinformatics, April 1, 2007; 23(7): 859 - 865.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
P. J. Kundrotas and E. Alexov
PROTCOM: searchable database of protein complexes enhanced with domain-domain structures
Nucleic Acids Res., January 12, 2007; 35(suppl_1): D575 - D579.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
A. Ceol, A. Chatr-aryamontri, E. Santonico, R. Sacco, L. Castagnoli, and G. Cesareni
DOMINO: a database of domain-peptide interactions
Nucleic Acids Res., January 12, 2007; 35(suppl_1): D557 - D560.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
P. M. Kim, L. J. Lu, Y. Xia, and M. B. Gerstein
Relating Three-Dimensional Structures to Protein Networks Provides Evolutionary Insights
Science, December 22, 2006; 314(5807): 1938 - 1941.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. Paarmann, B. Schmitt, B. Meyer, M. Karas, and H. Betz
Mass Spectrometric Analysis of Glycine Receptor-associated Gephyrin Splice Variants
J. Biol. Chem., November 17, 2006; 281(46): 34918 - 34925.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
H. Li, J. Li, and L. Wong
Discovering motif pairs at interaction sites from protein sequences on a proteome-wide scale
Bioinformatics, April 15, 2006; 22(8): 989 - 996.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
P. Pagel, M. Oesterheld, V. Stumpflen, and D. Frishman
The DIMA web resource--exploring the protein domain network
Bioinformatics, April 15, 2006; 22(8): 997 - 998.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
A. Henschel, W. K. Kim, and M. Schroeder
Equivalent binding sites reveal convergently evolved interaction motifs
Bioinformatics, March 1, 2006; 22(5): 550 - 555.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
R. D. Finn, J. Mistry, B. Schuster-Bockler, S. Griffiths-Jones, V. Hollich, T. Lassmann, S. Moxon, M. Marshall, A. Khanna, R. Durbin, et al.
Pfam: clans, web tools and services
Nucleic Acids Res., January 1, 2006; 34(suppl_1): D247 - D251.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
X.-W. Chen and M. Liu
Prediction of protein-protein interactions using random decision forest framework
Bioinformatics, December 15, 2005; 21(24): 4394 - 4400.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
G. Pugalenthi, G. Archunan, and R. Sowdhamini
DIAL: a web-based server for the automatic identification of structural domains in proteins
Nucleic Acids Res., July 1, 2005; 33(suppl_2): W130 - W132.
[Abstract] [Full Text] [PDF]



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.